About this Journal Submit a Manuscript Table of Contents
BioMed Research International
Volume 2013 (2013), Article ID 683095, 18 pages
http://dx.doi.org/10.1155/2013/683095
Review Article

The Role of Cytidine Deaminases on Innate Immune Responses against Human Viral Infections

1Programa de Oncovirologia, Instituto Nacional de Câncer, Rua André Cavalcanti, No. 37–4  Andar, Bairro de Fátima, 20231-050 Rio de Janeiro, RJ, Brazil
2Departamento de Genética, Universidade Federal do Rio de Janeiro, 21949-570 Rio de Janeiro, RJ, Brazil

Received 16 March 2013; Revised 29 May 2013; Accepted 31 May 2013

Academic Editor: Enrique Medina-Acosta

Copyright © 2013 Valdimara C. Vieira and Marcelo A. Soares. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. A. Iwasaki, “A virological view of innate immune recognition,” Annual Review of Microbiology, vol. 66, pp. 177–196, 2012. View at Publisher · View at Google Scholar
  2. O. Takeuchi and S. Akira, “Innate immunity to virus infection,” Immunological Reviews, vol. 227, no. 1, pp. 75–86, 2009. View at Publisher · View at Google Scholar · View at Scopus
  3. M. R. Thompson, J. J. Kaminski, E. A. Kurt-Jones, and K. A. Fitzgerald, “Pattern recognition receptors and the innate immune response to viral infection,” Viruses, vol. 3, no. 6, pp. 920–940, 2011. View at Publisher · View at Google Scholar · View at Scopus
  4. D. B. Stetson and R. Medzhitov, “Type I interferons in host defense,” Immunity, vol. 25, no. 3, pp. 373–381, 2006. View at Publisher · View at Google Scholar · View at Scopus
  5. S. G. Conticello, C. J. F. Thomas, S. K. Petersen-Mahrt, and M. S. Neuberger, “Evolution of the AID/APOBEC family of polynucleotide (deoxy)cytidine deaminases,” Molecular Biology and Evolution, vol. 22, no. 2, pp. 367–377, 2005. View at Publisher · View at Google Scholar · View at Scopus
  6. T. Muto, M. Muramatsu, M. Taniwaki, K. Kinoshita, and T. Honjo, “Isolation, tissue distribution, and chromosomal localization of the human activation-induced cytidine deaminase (AID) gene,” Genomics, vol. 68, no. 1, pp. 85–88, 2000. View at Scopus
  7. R. Espinosa III, T. Funahashi, C. Hadjiagapiou, M. M. le Beau, and N. O. Davidson, “Assignment of the gene encoding the human apolipoprotein B mRNA editing enzyme (APOBEC1) to chromosome 12p13.1,” Genomics, vol. 24, no. 2, pp. 414–415, 1994. View at Publisher · View at Google Scholar · View at Scopus
  8. W. Liao, S. Hong, B. H. Chann, F. B. Rudolph, S. Clark, and L. Chan, “APOBEC-2, a cardiac- and skeletal muscle-specific member of the cytidine deaminase supergene family,” Biochemical and Biophysical Research Communications, vol. 260, pp. 398–404, 1999. View at Publisher · View at Google Scholar
  9. A. Jarmuz, A. Chester, J. Bayliss et al., “An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22,” Genomics, vol. 79, no. 3, pp. 285–296, 2002. View at Publisher · View at Google Scholar · View at Scopus
  10. I. B. Rogozin, M. K. Basu, I. K. Jordan, Y. I. Pavlov, and E. V. Koonin, “APOBEC4, a new member of the AID/APOBEC family of polynucleotide (deoxy)cytidine deaminases predicted by computational analysis,” Cell Cycle, vol. 4, no. 9, pp. 1281–1285, 2005. View at Scopus
  11. J. E. Wedekind, G. S. C. Dance, M. P. Sowden, and H. C. Smith, “Messenger RNA editing in mammals: new members of the APOBEC family seeking roles in the family business,” Trends in Genetics, vol. 19, no. 4, pp. 207–216, 2003. View at Publisher · View at Google Scholar · View at Scopus
  12. B. Teng, C. F. Burant, and N. O. Davidson, “Molecular cloning of an apolipoprotein B messenger RNA editing protein,” Science, vol. 260, no. 5115, pp. 1816–1818, 1993. View at Scopus
  13. R. S. Harris, S. K. Petersen-Mahrt, and M. S. Neuberger, “RNA editing enzyme APOBEC1 and some of its homologs can act as DNA mutators,” Molecular Cell, vol. 10, no. 5, pp. 1247–1253, 2002. View at Publisher · View at Google Scholar · View at Scopus
  14. Y. Yang, Y. Yang, and H. C. Smith, “Multiple protein domains determine the cell type-specific nuclear distribution of the catalytic subunit required for apolipoprotein B mRNA editing,” Proceedings of the National Academy of Sciences of the United States of America, vol. 94, no. 24, pp. 13075–13080, 1997. View at Publisher · View at Google Scholar · View at Scopus
  15. P. P. Lau, W. Xiong, H.-J. Zhu, S.-H. Chen, and L. Chan, “Apolipoprotein B mRNA editing is an intranuclear event that occurs posttranscriptionally coincident with splicing and polyadenylation,” The Journal of Biological Chemistry, vol. 266, no. 30, pp. 20550–20554, 1991. View at Scopus
  16. M. P. Sowden, N. Ballatori, K. L. de Mesy Jensen, L. Hamilton Reed, and H. C. Smith, “The editosome for cytidine to uridine mRNA editing has a native complexity of 27S: identification of intracellular domains containing active and inactive editing factors,” Journal of Cell Science, vol. 115, no. 5, pp. 1027–1039, 2002. View at Scopus
  17. S. Anant and N. O. Davidson, “Molecular mechanisms of apolipoprotein B mRNA editing,” Current Opinion in Lipidology, vol. 12, no. 2, pp. 159–165, 2001. View at Publisher · View at Google Scholar · View at Scopus
  18. S. Anant and N. O. Davidson, “An AU-rich sequence element (UUUN[A/U]U) downstream of the edited C in apolipoprotein B mRNA is a high-affinity binding site for Apobec-1: binding of Apobec-1 to this motif in the 3' untranslated region of c-myc increases mRNA stability,” Molecular and Cellular Biology, vol. 20, no. 6, pp. 1982–1992, 2000. View at Publisher · View at Google Scholar · View at Scopus
  19. B. R. Rosenberg, C. E. Hamilton, M. M. Mwangi, S. Dewell, and F. N. Papavasiliou, “Transcriptome-wide sequencing reveals numerous APOBEC1 mRNA-editing targets in transcript 3' UTRs,” Nature Structural & Molecular Biology, vol. 18, no. 2, pp. 230–238, 2011. View at Publisher · View at Google Scholar · View at Scopus
  20. S. K. Dickerson, E. Market, E. Besmer, and F. N. Papavasiliou, “AID mediates hypermutation by deaminating single stranded DNA,” The Journal of Experimental Medicine, vol. 197, no. 10, pp. 1291–1296, 2003. View at Publisher · View at Google Scholar · View at Scopus
  21. R. Bransteitter, P. Pham, M. D. Scharfft, and M. F. Goodman, “Activation-induced cytidine deaminase deaminates deoxycytidine on single-stranded DNA but requires the action of RNase,” Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 7, pp. 4102–4107, 2003. View at Publisher · View at Google Scholar · View at Scopus
  22. C. Rada, J. M. Jarvis, and C. Milstein, “AID-GFP chemirec protein increases hypermutation og Ig genes with no evidence of nuclear localization,” Proceedings of the National Academy of Sciences of the United States of America, vol. 99, no. 10, pp. 7003–7008, 2002. View at Publisher · View at Google Scholar · View at Scopus
  23. S. S. Brar, M. Watson, and M. Diaz, “Activation-induced cytosine deaminase (AID) is actively exported out of the nucleus but retained by the induction of DNA breaks,” The Journal of Biological Chemistry, vol. 279, no. 25, pp. 26395–26401, 2004. View at Publisher · View at Google Scholar · View at Scopus
  24. S. Ito, H. Nagaoka, R. Shinkura et al., “Activation-induced cytidine deaminase shuttles between nucleus and cytoplasm like apolipoprotein B mRNA editing catalytic polypeptide 1,” Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no. 7, pp. 1975–1980, 2004. View at Publisher · View at Google Scholar · View at Scopus
  25. K. M. McBride, V. Barreto, A. R. Ramiro, P. Stavropoulos, and M. C. Nussenzweig, “Somatic hypermutation is limited by CRM1-dependent nuclear export of activation-induced deaminase,” The Journal of Experimental Medicine, vol. 199, no. 9, pp. 1235–1244, 2004. View at Publisher · View at Google Scholar · View at Scopus
  26. M. Muramatsu, K. Kinoshita, S. Fagarasan, S. Yamada, Y. Shinkai, and T. Honjo, “Class switch recombination and hypermutation require activation-induced cytidine deaminase (AID), a potential RNA editing enzyme,” Cell, vol. 102, no. 5, pp. 553–563, 2000. View at Scopus
  27. J. M. Di Noia and M. S. Neuberger, “Molecular mechanisms of antibody somatic hypermutation,” Annual Review of Biochemistry, vol. 76, pp. 1–22, 2007. View at Publisher · View at Google Scholar · View at Scopus
  28. M. Muramatsu, V. S. Sankaranand, S. Anant et al., “Specific expression of activation-induced cytidine deaminase (AID), a novel member of the RNA-editing deaminase family in germinal center B cells,” The Journal of Biological Chemistry, vol. 274, no. 26, pp. 18470–18476, 1999. View at Publisher · View at Google Scholar · View at Scopus
  29. C. Popp, W. Dean, S. Feng et al., “Genome-wide erasure of DNA methylation in mouse primordial germ cells is affected by AID deficiency,” Nature, vol. 463, no. 7284, pp. 1101–1105, 2010. View at Publisher · View at Google Scholar · View at Scopus
  30. N. Bhutani, J. J. Brady, M. Damian, A. Sacco, S. Y. Corbel, and H. M. Blau, “Reprogramming towards pluripotency requires AID-dependent DNA demethylation,” Nature, vol. 463, no. 7284, pp. 1042–1047, 2010. View at Publisher · View at Google Scholar · View at Scopus
  31. J. U. Guo, Y. Su, C. Zhong, G.-L. Ming, and H. Song, “Hydroxylation of 5-methylcytosine by TET1 promotes active DNA demethylation in the adult brain,” Cell, vol. 145, no. 3, pp. 423–434, 2011. View at Publisher · View at Google Scholar · View at Scopus
  32. Y. Sato, H. C. Probst, R. Tatsumi, Y. Ikeuchi, M. S. Neuberger, and C. Rada, “Deficiency in APOBEC2 leads to a shift in muscle fiber type, diminished body mass, and myopathy,” The Journal of Biological Chemistry, vol. 285, no. 10, pp. 7111–7118, 2010. View at Publisher · View at Google Scholar · View at Scopus
  33. J. E. Wedekind, R. Gillilan, A. Janda et al., “Nanostructures of APOBEC3G support a hierarchical assembly model of high molecular mass ribonucleoprotein particles from dimeric subunits,” The Journal of Biological Chemistry, vol. 281, no. 50, pp. 38122–38126, 2006. View at Publisher · View at Google Scholar · View at Scopus
  34. F. Navarro, B. Bollman, H. Chen et al., “Complementary function of the two catalytic domains of APOBEC3G,” Virology, vol. 333, no. 2, pp. 374–386, 2005. View at Publisher · View at Google Scholar · View at Scopus
  35. R. C. L. Beale, S. K. Petersen-Mahrt, I. N. Watt, R. S. Harris, C. Rada, and M. S. Neuberger, “Comparison of the differential context-dependence of DNA deamination by APOBEC enzymes: correlation with mutation spectra in vivo,” Journal of Molecular Biology, vol. 337, no. 3, pp. 585–596, 2004. View at Publisher · View at Google Scholar · View at Scopus
  36. A. E. Armitage, A. Katzourakis, T. de Oliveira et al., “Conserved footprints of APOBEC3G on hypermutated human immunodeficiency virus type 1 and human endogenous retrovirus HERV-K(HML2) sequences,” Journal of Virology, vol. 82, no. 17, pp. 8743–8761, 2008. View at Publisher · View at Google Scholar · View at Scopus
  37. K. N. Bishop, R. K. Holmes, A. M. Sheehy, N. O. Davidson, S.-J. Cho, and M. H. Malim, “Cytidine deamination of retroviral DNA by diverse APOBEC proteins,” Current Biology, vol. 14, no. 15, pp. 1392–1396, 2004. View at Publisher · View at Google Scholar · View at Scopus
  38. R. S. Harris, K. N. Bishop, A. M. Sheehy et al., “DNA deamination mediates innate immunity to retroviral infection,” Cell, vol. 113, no. 6, pp. 803–809, 2003. View at Publisher · View at Google Scholar · View at Scopus
  39. H. P. Bogerd, H. L. Wiegand, B. P. Doehle, K. K. Lueders, and B. R. Cullen, “APOBEC3A and APOBEC3B are potent inhibitors of LTR-retrotransposon function in human cells,” Nucleic Acids Research, vol. 34, no. 1, pp. 89–95, 2006. View at Publisher · View at Google Scholar · View at Scopus
  40. M. Kinomoto, T. Kanno, M. Shimura et al., “All APOBEC3 family proteins differentially inhibit LINE-1 retrotransposition,” Nucleic Acids Research, vol. 35, no. 9, pp. 2955–2964, 2007. View at Publisher · View at Google Scholar · View at Scopus
  41. F. Delebecque, R. Suspène, S. Calattini et al., “Restriction of foamy viruses by APOBEC cytidine deaminases,” Journal of Virology, vol. 80, no. 2, pp. 605–614, 2006. View at Publisher · View at Google Scholar · View at Scopus
  42. Q. Yu, D. Chen, R. König, R. Mariani, D. Unutmaz, and N. R. Landau, “APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication,” The Journal of Biological Chemistry, vol. 279, no. 51, pp. 53379–53386, 2004. View at Publisher · View at Google Scholar · View at Scopus
  43. J. L. Anderson and T. J. Hope, “APOBEC3G restricts early HIV-1 replication in the cytoplasm of target cells,” Virology, vol. 375, no. 1, pp. 1–12, 2008. View at Publisher · View at Google Scholar · View at Scopus
  44. K. N. Bishop, R. K. Holmes, and M. H. Malim, “Antiviral potency of APOBEC proteins does not correlate with cytidine deamination,” Journal of Virology, vol. 80, no. 17, pp. 8450–8458, 2006. View at Publisher · View at Google Scholar · View at Scopus
  45. K. N. Bishop, M. Verma, E.-Y. Kim, S. M. Wolinsky, and M. H. Malim, “APOBEC3G inhibits elongation of HIV-1 reverse transcripts,” PLoS Pathogens, vol. 4, no. 12, Article ID e1000231, 2008. View at Publisher · View at Google Scholar · View at Scopus
  46. M. D. Stenglein, M. B. Burns, M. Li, J. Lengyel, and R. S. Harris, “APOBEC3 proteins mediate the clearance of foreign DNA from human cells,” Nature Structural & Molecular Biology, vol. 17, no. 2, pp. 222–229, 2010. View at Publisher · View at Google Scholar · View at Scopus
  47. R. Suspène, M.-M. Aynaud, D. Guétard et al., “Somatic hypermutation of human mitochondrial and nuclear DNA by APOBEC3 cytidine deaminases, a pathway for DNA catabolism,” Proceedings of the National Academy of Sciences of the United States of America, vol. 108, no. 12, pp. 4858–4863, 2011. View at Publisher · View at Google Scholar · View at Scopus
  48. M. B. Burns, L. Lackey, M. A. Carpenter, et al., “APOBEC3B is an enzymatic source of mutation in breast cancer,” Nature, vol. 494, pp. 366–370, 2013. View at Publisher · View at Google Scholar
  49. R. P. Bennett, V. Presnyak, J. E. Wedekind, and H. C. Smith, “Nuclear exclusion of the HIV-1 host defense factor APOBEC3G requires a novel cytoplasmic retention signal and is not dependent on RNA binding,” The Journal of Biological Chemistry, vol. 283, no. 12, pp. 7320–7327, 2008. View at Publisher · View at Google Scholar · View at Scopus
  50. L. Lackey, Z. L. Demorest, A. M. Land, J. F. Hultquist, W. L. Brown, and R. S. Harris, “APOBEC3B and AID have similar nuclear import mechanisms,” Journal of Molecular Biology, vol. 419, no. 5, pp. 301–314, 2012. View at Publisher · View at Google Scholar · View at Scopus
  51. M. M. H. Li and M. Emerman, “Polymorphism in human APOBEC3H affects a phenotype dominant for subcellular localization and antiviral activity,” Journal of Virology, vol. 85, no. 16, pp. 8197–8207, 2011. View at Publisher · View at Google Scholar · View at Scopus
  52. A. M. Land, E. K. Law, M. A. Carpenter, L. Lackey, W. L. Brown, and R. S. Harris, “Endogenous APOBEC3A is cytoplasmic and non-genotoxic,” The Journal of Biological Chemistry, 2013. View at Publisher · View at Google Scholar
  53. Y.-L. Chiu, V. B. Soros, J. F. Kreisberg, K. Stopak, W. Yonemoto, and W. C. Greene, “Cellular APOBEC3G restricts HIV-1 infection in resting CD4+ T cells,” Nature, vol. 435, no. 7038, pp. 108–114, 2005. View at Publisher · View at Google Scholar · View at Scopus
  54. Y.-L. Chiu and W. C. Greene, “The APOBEC3 cytidine deaminases: an innate defensive network opposing exogenous retroviruses and endogenous retroelements,” Annual Review of Immunology, vol. 26, pp. 317–353, 2008. View at Publisher · View at Google Scholar · View at Scopus
  55. H. C. Smith, R. P. Bennett, A. Kizilyer, W. M. McDougall, and K. M. Prohaska, “Functions and regulation of the APOBEC family of proteins,” Seminars in Cell and Developmental Biology, vol. 23, no. 3, pp. 258–268, 2012. View at Publisher · View at Google Scholar · View at Scopus
  56. X. Wang, P. T. Dolan, Y. Dang, and Y.-H. Zheng, “Biochemical differentiation of APOBEC3F and APOBEC3G proteins associated with HIV-1 life cycle,” The Journal of Biological Chemistry, vol. 282, no. 3, pp. 1585–1594, 2007. View at Publisher · View at Google Scholar · View at Scopus
  57. L. Tan, P. T. N. Sarkis, T. Wang, C. Tian, and X.-F. Yu, “Sole copy of Z2-type human cytidine deaminase APOBEC3H has inhibitory activity against retrotransposons and HIV-1,” The FASEB Journal, vol. 23, no. 1, pp. 279–287, 2009. View at Publisher · View at Google Scholar · View at Scopus
  58. A. M. Niewiadomska, C. Tian, L. Tan, T. Wang, P. T. N. Sarkis, and X.-F. Yu, “Differential inhibition of long interspersed element 1 by APOBEC3 does not correlate with high-molecular-mass-complex formation or P-body association,” Journal of Virology, vol. 81, no. 17, pp. 9577–9583, 2007. View at Publisher · View at Google Scholar · View at Scopus
  59. J. F. Kreisberg, W. Yonemoto, and W. C. Greene, “Endogenous factors enhance HIV infection of tissue naive CD4 T cells by stimulating high molecular mass APOBEC3G complex formation,” The Journal of Experimental Medicine, vol. 203, no. 4, pp. 865–870, 2006. View at Publisher · View at Google Scholar · View at Scopus
  60. K. S. Stopak, Y.-L. Chiu, J. Kropp, R. M. Grant, and W. C. Greene, “Distinct patterns of cytokine regulation of APOBEC3G expression and activity in primary lymphocytes, macrophages, and dendritic cells,” The Journal of Biological Chemistry, vol. 282, no. 6, pp. 3539–3546, 2007. View at Publisher · View at Google Scholar · View at Scopus
  61. P. J. Ellery, E. Tippett, Y.-L. Chiu et al., “The CD16+ monocyte subset is more permissive to infection and preferentially harbors HIV-1 in vivo,” Journal of Immunology, vol. 178, no. 10, pp. 6581–6589, 2007. View at Scopus
  62. M. Kamata, Y. Nagaoka, and I. S. Y. Chen, “Reassessing the role of APOBEC3G in human immunodeficiency virus type 1 infection of quiescent CD4+ T-cells,” PLoS Pathogens, vol. 5, no. 3, Article ID e1000342, 2009. View at Publisher · View at Google Scholar · View at Scopus
  63. F. R. Santoni de Sio and D. Trono, “APOBEC3G-depleted resting CD4+ T cells remain refractory to HIV1 infection,” PLoS ONE, vol. 4, no. 8, article e6571, 2009. View at Publisher · View at Google Scholar · View at Scopus
  64. V. B. Soros, W. Yonemoto, and W. C. Greene, “Newly synthesized APOBEC3G is incorporated into HIV virions, inhibited by HIV RNA, and subsequently activated by RNase H,” PLoS Pathogens, vol. 3, no. 2, article e15, 2007. View at Publisher · View at Google Scholar · View at Scopus
  65. M. A. Khan, R. Goila-Gaur, S. Kao, E. Miyagi, R. C. Walker Jr., and K. Strebel, “Encapsidation of APOBEC3G into HIV-1 virions involves lipid raft association and does not correlate with APOBEC3G oligomerization,” Retrovirology, vol. 6, article 1742, 2009. View at Publisher · View at Google Scholar · View at Scopus
  66. J. Ma, X. Li, J. Xu, et al., “The cellular source for APOBEC3G’s incorporation into HIV-1,” Retrovirology, vol. 8, article 2, 2011.
  67. Y.-L. Chiu, H. E. Witkowska, S. C. Hall et al., “High-molecular-mass APOBEC3G complexes restrict Alu retrotransposition,” Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 42, pp. 15588–15593, 2006. View at Publisher · View at Google Scholar · View at Scopus
  68. S. Gallois-Montbrun, B. Kramer, C. M. Swanson et al., “Antiviral protein APOBEC3G localizes to ribonucleoprotein complexes found in P bodies and stress granules,” Journal of Virology, vol. 81, no. 5, pp. 2165–2178, 2007. View at Publisher · View at Google Scholar · View at Scopus
  69. S. Gallois-Montbrun, R. K. Holmes, C. M. Swanson et al., “Comparison of cellular ribonucleoprotein complexes associated with the APOBEC3F and APOBEC3G antiviral proteins,” Journal of Virology, vol. 82, no. 11, pp. 5636–5642, 2008. View at Publisher · View at Google Scholar · View at Scopus
  70. S. L. Kozak, M. Marin, K. M. Rose, C. Bystrom, and D. Kabat, “The anti-HIV-1 editing enzyme APOBEC3G binds HIV-1 RNA and messenger RNAs that shuttle between polysomes and stress granules,” The Journal of Biological Chemistry, vol. 281, no. 39, pp. 29105–29119, 2006. View at Publisher · View at Google Scholar · View at Scopus
  71. M. J. Wichroski, G. B. Robb, and T. M. Rana, “Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies,” PLoS Pathogens, vol. 2, no. 5, article e41, 2006. View at Publisher · View at Google Scholar · View at Scopus
  72. P. K. Phalora, N. M. Sherer, S. M. Wolinsky, C. M. Swanson, and M. H. Malim, “HIV-1 replication and APOBEC3 antiviral activity are not regulated by P bodies,” Journal of Virology, vol. 86, no. 21, pp. 11712–11724, 2012. View at Publisher · View at Google Scholar
  73. A. G. Lada, C. Frahm Krick, S. G. Kozmin et al., “Mutator effects and mutation signatures of editing deaminases produced in bacteria and yeast,” Biochemistry, vol. 76, no. 1, pp. 131–146, 2011. View at Publisher · View at Google Scholar · View at Scopus
  74. S. G. Conticello, “Creative deaminases, self-inflicted damage, and genome evolution,” Annals of the New York Academy of Sciences, vol. 1267, pp. 79–85, 2012.
  75. C. Münk, B. E. O. Jensen, J. Zielonka, D. Häussinger, and C. Kamp, “Running loose or getting lost: how HIV-1 counters and capitalizes on APOBEC3-induced mutagenesis through its Vif protein,” Viruses, vol. 4, pp. 3132–3161, 2012. View at Publisher · View at Google Scholar
  76. F. Severi, A. Chicca, and S. G. Conticello, “Analysis of reptilian APOBEC1 suggests that RNA Editing may not be its ancestral function,” Molecular Biology and Evolution, vol. 28, no. 3, pp. 1125–1129, 2011. View at Publisher · View at Google Scholar · View at Scopus
  77. R. S. Harris and M. T. Liddament, “Retroviral restriction by APOBEC proteins,” Nature Reviews Immunology, vol. 4, no. 11, pp. 868–877, 2004. View at Publisher · View at Google Scholar · View at Scopus
  78. C. Münk, A. Willemsen, and I. Bravo, “An ancient history of gene duplications, fusions and losses in the evolution of APOBEC3 mutators in mammals,” BMC Evolutionary Biology, vol. 12, article 71, 2012.
  79. R. S. LaRue, S. R. Jónsson, K. A. T. Silverstein et al., “The artiodactyl APOBEC3 innate immune repertoire shows evidence for a multi-functional domain organization that existed in the ancestor of placental mammals,” BMC Molecular Biology, vol. 9, no. 104, pp. 1–20, 2008. View at Publisher · View at Google Scholar · View at Scopus
  80. C. Münk, T. Beck, J. Zielonka et al., “Functions, structure, and read-through alternative splicing of feline APOBEC3 genes,” Genome Biology, vol. 9, no. 3, article R48, 2008. View at Publisher · View at Google Scholar · View at Scopus
  81. G. G. Schumann, “APOBEC3 proteins: major players in intracellular defence against LINE-1-mediated retrotransposition,” Biochemical Society Transactions, vol. 35, no. 3, pp. 637–642, 2007. View at Publisher · View at Google Scholar · View at Scopus
  82. A. Koito and T. Ikeda, “Intrinsic immunity against retrotransposons by APOBEC cytidine deaminases,” Frontiers in Microbiology, vol. 4, pp. 1–9, 2013.
  83. H. P. Bogerd, H. L. Wiegand, A. E. Hulme et al., “Cellular inhibitors of long interspersed element 1 and Alu retrotransposition,” Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 23, pp. 8780–8785, 2006. View at Publisher · View at Google Scholar · View at Scopus
  84. A. E. Hulme, H. P. Bogerd, B. R. Cullen, and J. V. Moran, “Selective inhibition of Alu retrotransposition by APOBEC3G,” Gene, vol. 390, no. 1-2, pp. 199–205, 2007. View at Publisher · View at Google Scholar · View at Scopus
  85. C. Esnault, O. Heidmann, F. Delebecque et al., “APOBEC3G cytidine deaminase inhibits retrotransposition of endogenous retroviruses,” Nature, vol. 433, no. 7024, pp. 430–433, 2005. View at Publisher · View at Google Scholar · View at Scopus
  86. C. Esnault, J. Millet, O. Schwartz, and T. Heidmann, “Dual inhibitory effects of APOBEC family proteins on retrotransposition of mammalian endogenous retroviruses,” Nucleic Acids Research, vol. 34, no. 5, pp. 1522–1531, 2006. View at Publisher · View at Google Scholar · View at Scopus
  87. A. J. Schumacher, D. V. Nissley, and R. S. Harris, “APOBEC3G hypermutates genomic DNA and inhibits Ty1 retrotransposition in yeast,” Proceedings of the National Academy of Sciences of the United States of America, vol. 102, no. 28, pp. 9854–9859, 2005. View at Publisher · View at Google Scholar · View at Scopus
  88. D. A. Macduff, Z. L. Demorest, and R. S. Harris, “AID can restrict L1 retrotransposition suggesting a dual role in innate and adaptive immunity,” Nucleic Acids Research, vol. 37, no. 6, pp. 1854–1867, 2009. View at Publisher · View at Google Scholar · View at Scopus
  89. T. Ikeda, K. H. Abd El Galil, K. Tokunaga et al., “Intrinsic restriction activity by apolipoprotein B mRNA editing enzyme APOBEC1 against the mobility of autonomous retrotransposons,” Nucleic Acids Research, vol. 39, no. 13, pp. 5538–5554, 2011. View at Publisher · View at Google Scholar · View at Scopus
  90. M. Metzner, H.-M. Jäck, and M. Wabl, “LINE-1 retroelements complexed and inhibited by activation induced cytidine deaminase,” PloS One, vol. 7, no. 11, article e49358, 2012.
  91. K. N. Bishop, R. K. Holmes, A. M. Sheehy, and M. H. Malim, “APOBEC-mediated editing of viral RNA,” Science, vol. 305, no. 5684, article 645, 2004. View at Publisher · View at Google Scholar · View at Scopus
  92. T. Ikeda, T. Ohsugi, T. Kimura et al., “The antiretroviral potency of APOBEC1 deaminase from small animal species,” Nucleic Acids Research, vol. 36, no. 21, pp. 6859–6871, 2008. View at Publisher · View at Google Scholar · View at Scopus
  93. V. Petit, D. Guétard, M. Renard et al., “Murine APOBEC1 is a powerful mutator of retroviral and cellular RNA in vitro and in vivo,” Journal of Molecular Biology, vol. 385, no. 1, pp. 65–78, 2009. View at Publisher · View at Google Scholar · View at Scopus
  94. P. An, R. Johnson, J. Phair et al., “APOBEC3B deletion and risk of HIV-1 acquisition,” The Journal of Infectious Diseases, vol. 200, no. 7, pp. 1054–1058, 2009. View at Publisher · View at Google Scholar · View at Scopus
  95. H. Abe, H. Ochi, T. Maekawa et al., “Effects of structural variations of APOBEC3A and APOBEC3B genes in chronic hepatitis B virus infection,” Hepatology Research, vol. 39, no. 12, pp. 1159–1168, 2009. View at Publisher · View at Google Scholar · View at Scopus
  96. S. Itaya, T. Nakajima, G. Kaur et al., “No evidence of an association between the APOBEC3B deletion polymorphism and susceptibility to HIV infection and AIDS in Japanese and indian populations,” The Journal of Infectious Diseases, vol. 202, no. 5, pp. 815–816, 2010. View at Publisher · View at Google Scholar · View at Scopus
  97. T. Zhang, J. Cai, J. Chang, et al., “Evidence of associations of APOBEC3B gene deletion with susceptibility to persistent HBV infection and hepatocellular carcinoma,” Human Molecular Genetics, vol. 22, no. 6, pp. 1262–1269, 2012.
  98. S. Ezzikouri, B. Kitab, K. Rebbani, et al., “Polymorphic APOBEC3 modulates chronic hepatitis B in Moroccan population,” Journal of Viral Hepatitis, pp. 1–9, 2012. View at Publisher · View at Google Scholar
  99. P. An, G. Bleiber, P. Duggal et al., “APOBEC3G genetic variants and their influence on the progression to AIDS,” Journal of Virology, vol. 78, no. 20, pp. 11070–11076, 2004. View at Publisher · View at Google Scholar · View at Scopus
  100. H. Do, A. Vasilescu, G. Diop et al., “Exhaustive genotyping of the CEM15 (APOBEC3G) gene and absence of association with AIDS progression in a French cohort,” The Journal of Infectious Diseases, vol. 191, no. 2, pp. 159–163, 2005. View at Publisher · View at Google Scholar · View at Scopus
  101. C. Pace, J. Keller, D. Nolan et al., “Population level analysis of human immunodeficiency virus type 1 hypermutation and its relationship with APOBEC3G and vif genetic variation,” Journal of Virology, vol. 80, no. 18, pp. 9259–9269, 2006. View at Publisher · View at Google Scholar · View at Scopus
  102. H. S. Valcke, N. F. Bernard, J. Bruneau, M. Alary, C. M. Tsoukas, and M. Roger, “APOBEC3G genetic variants and their association with risk of HIV infection in highly exposed Caucasians,” AIDS, vol. 20, no. 15, pp. 1984–1986, 2006. View at Publisher · View at Google Scholar · View at Scopus
  103. A. Rathore, A. Chatterjee, N. Yamamoto, and T. N. Dhole, “Absence of H186R polymorphism in exon 4 of the APOBEC3G gene among north Indian individuals,” Genetic Testing, vol. 12, no. 3, pp. 453–456, 2008. View at Publisher · View at Google Scholar · View at Scopus
  104. K. Reddy, C. A. Winkler, L. Werner, K. Mlisana, S. S. Abdool Karim, and T. Ndung'U, “Apobec3g expression is dysregulated in primary hiv-1 infection and polymorphic variants influence cd4+ t-cell counts and plasma viral load,” AIDS, vol. 24, no. 2, pp. 195–204, 2010. View at Publisher · View at Google Scholar · View at Scopus
  105. F. A. de Maio, C. A. Rocco, P. C. Aulicino, R. Bologna, A. Mangano, and L. Sen, “Effect of HIV-1 Vif variability on progression to pediatric AIDS and its association with APOBEC3G and CUL5 polymorphisms,” Infection, Genetics and Evolution, vol. 11, no. 6, pp. 1256–1262, 2011. View at Publisher · View at Google Scholar · View at Scopus
  106. M. C. Bizinoto, É. Leal, R. S. Diaz, and L. M. Janini, “Loci polymorphisms of the APOBEC3G gene in HIV type 1-infected Brazilians,” AIDS Research and Human Retroviruses, vol. 27, no. 2, pp. 137–141, 2011. View at Publisher · View at Google Scholar · View at Scopus
  107. F. A. de Maio, C. A. Rocco, P. C. Aulicino, R. Bologna, A. Mangano, and L. Sen, “APOBEC3-mediated editing in HIV type 1 from pediatric patients and its association with APOBEC3G/CUL5 polymorphisms and Vif variability,” AIDS Research and Human Retroviruses, vol. 28, no. 6, pp. 619–627, 2012. View at Publisher · View at Google Scholar
  108. K. K. Singh, Y. Wang, K. P. Gray, et al., “Genetic variants in the host restriction factor APOBEC3G are associated with HIV-1-related disease progression and central nervous system impairment in children,” Journal of Acquired Immune Deficiency Syndromes, vol. 62, no. 2, pp. 197–203, 2013. View at Publisher · View at Google Scholar
  109. R. Cagliani, S. Riva, M. Fumagalli et al., “A positively selected APOBEC3H haplotype is associated with natural resistance to HIV-1 infection,” Evolution, vol. 65, no. 11, pp. 3311–3322, 2011. View at Publisher · View at Google Scholar · View at Scopus
  110. P. A. Gourraud, A. Karaouni, J. M. Woo et al., “APOBEC3H haplotypes and HIV-1 pro-viral vif DNA sequence diversity in early untreated human immunodeficiency virus-1 infection,” Human Immunology, vol. 72, no. 3, pp. 207–212, 2011. View at Publisher · View at Google Scholar · View at Scopus
  111. J. A. Levy, “HIV pathogenesis: 25 years of progress and persistent challenges,” AIDS, vol. 23, no. 2, pp. 147–160, 2009. View at Publisher · View at Google Scholar · View at Scopus
  112. S. Cen, F. Guo, M. Niu, J. Saadatmand, J. Deflassieux, and L. Kleiman, “The interaction between HIV-1 gag and APOBEC3G,” The Journal of Biological Chemistry, vol. 279, no. 32, pp. 33177–33184, 2004. View at Publisher · View at Google Scholar · View at Scopus
  113. T. M. Alce and W. Popik, “APOBEC3G is incorporated into virus-like particles by a direct interaction with HIV-1 gag nucleocapsid protein,” The Journal of Biological Chemistry, vol. 279, no. 33, pp. 34083–34086, 2004. View at Publisher · View at Google Scholar · View at Scopus
  114. K. Luo, B. Liu, Z. Xiao et al., “Amino-terminal region of the human immunodeficiency virus type 1 nucleocapsid is required for human APOBEC3G packaging,” Journal of Virology, vol. 78, no. 21, pp. 11841–11852, 2004. View at Publisher · View at Google Scholar · View at Scopus
  115. V. Zennou, D. Perez-Caballero, H. Göttlinger, and P. D. Bieniasz, “APOBEC3G incorporation into human immunodeficiency virus type 1 particles,” Journal of Virology, vol. 78, no. 21, pp. 12058–12061, 2004. View at Publisher · View at Google Scholar · View at Scopus
  116. M. Douaisi, S. Dussart, M. Courcoul, G. Bessou, R. Vigne, and E. Decroly, “HIV-1 and MLV Gag proteins are sufficient to recruit APOBEC3G into virus-like particles,” Biochemical and Biophysical Research Communications, vol. 321, no. 3, pp. 566–573, 2004. View at Publisher · View at Google Scholar · View at Scopus
  117. A. Schäfer, H. P. Bogerd, and B. R. Cullen, “Specific packaging of APOBEC3G into HIV-1 virions is mediated by the nucleocapsid domain of the gag polyprotein precursor,” Virology, vol. 328, no. 2, pp. 163–168, 2004. View at Publisher · View at Google Scholar · View at Scopus
  118. E. S. Svarovskaia, H. Xu, J. L. Mbisa et al., “Human apolipoprotein B mRNA-editing enzyme-catalytic polypeptide-like 3G (APOBEC3G) is incorporated into HIV-1 virions through interactions with viral and nonviral RNAs,” The Journal of Biological Chemistry, vol. 279, no. 34, pp. 35822–35828, 2004. View at Publisher · View at Google Scholar · View at Scopus
  119. A. Burnett and P. Spearman, “APOBEC3G multimers are recruited to the plasma membrane for packaging into human immunodeficiency virus type 1 virus-like particles in an RNA-dependent process requiring the NC basic linker,” Journal of Virology, vol. 81, no. 10, pp. 5000–5013, 2007. View at Publisher · View at Google Scholar · View at Scopus
  120. T. Wang, W. Zhang, C. Tian et al., “Distinct viral determinants for the packaging of human cytidine deaminases APOBEC3G and APOBEC3C,” Virology, vol. 377, no. 1, pp. 71–79, 2008. View at Publisher · View at Google Scholar · View at Scopus
  121. D. Lecossier, F. Bouchonnet, F. Clavel, and A. J. Hance, “Hypermutation of HIV-1 DNA in the absence of the Vif protein,” Science, vol. 300, no. 5622, p. 1112, 2003. View at Publisher · View at Google Scholar · View at Scopus
  122. B. Schröfelbauer, Q. Yu, S. G. Zeitlin, and N. R. Landau, “Human immunodeficiency virus type 1 Vpr induces the degradation of the UNG and SMUG Uracil-DNA glycosylases,” Journal of Virology, vol. 79, no. 17, pp. 10978–10987, 2005. View at Publisher · View at Google Scholar · View at Scopus
  123. B. Yang, K. Chen, C. Zhang, S. Huang, and H. Zhang, “Virion-associated uracil DNA glycosylase-2 and apurinic/apyrimidinic endonuclease are involved in the degradation of APOBEC3G-edited nascent HIV-1 DNA,” The Journal of Biological Chemistry, vol. 282, no. 16, pp. 11667–11675, 2007. View at Publisher · View at Google Scholar · View at Scopus
  124. S. M. Kaiser and M. Emerman, “Uracil DNA glycosylase is dispensable for human immunodeficiency virus type 1 replication and does not contribute to the antiviral effects of the cytidine deaminase Apobec3G,” Journal of Virology, vol. 80, no. 2, pp. 875–882, 2006. View at Publisher · View at Google Scholar · View at Scopus
  125. M.-A. Langlois and M. S. Neuberger, “Human APOBEC3G can restrict retroviral infection in avian cells and acts independently of both UNG and SMUG1,” Journal of Virology, vol. 82, no. 9, pp. 4660–4664, 2008. View at Publisher · View at Google Scholar · View at Scopus
  126. R. K. Holmes, F. A. Koning, K. N. Bishop, and M. H. Malim, “APOBEC3F can inhibit the accumulation of HIV-1 reverse transcription products in the absence of hypermutation: comparisons with APOBEC3G,” The Journal of Biological Chemistry, vol. 282, no. 4, pp. 2587–2595, 2007. View at Publisher · View at Google Scholar · View at Scopus
  127. Y. Iwatani, D. S. B. Chan, F. Wang et al., “Deaminase-independent inhibition of HIV-1 reverse transcription by APOBEC3G,” Nucleic Acids Research, vol. 35, no. 21, pp. 7096–7108, 2007. View at Publisher · View at Google Scholar · View at Scopus
  128. E. N. C. Newman, R. K. Holmes, H. M. Craig et al., “Antiviral function of APOBEC3G can be dissociated from cytidine deaminase activity,” Current Biology, vol. 15, no. 2, pp. 166–170, 2005. View at Publisher · View at Google Scholar · View at Scopus
  129. J. L. Mbisa, R. Barr, J. A. Thomas et al., “Human immunodeficiency virus type 1 cDNAs produced in the presence of APOBEC3G exhibit defects in plus-strand DNA transfer and integration,” Journal of Virology, vol. 81, no. 13, pp. 7099–7110, 2007. View at Publisher · View at Google Scholar · View at Scopus
  130. K. Gillick, D. Pollpeter, P. Phalora, E. Y. Kim, S. M. Wolinsky, and M. H. Malim, “Suppression of HIV-1 infection by APOBEC3 proteins in primary human CD4+ T cells is associated with inhibition of processive reverse transcription as well as excessive cytidine deamination,” Journal of Virology, vol. 87, no. 3, pp. 1508–1517, 2013. View at Publisher · View at Google Scholar
  131. F. Guo, S. Cen, M. Niu, J. Saadatmand, and L. Kleiman, “Inhibition of tRNA3Lys-primed reverse transcription by human APOBEC3G during human immunodeficiency virus type 1 replication,” Journal of Virology, vol. 80, no. 23, pp. 11710–11722, 2006. View at Publisher · View at Google Scholar · View at Scopus
  132. X.-Y. Li, F. Guo, L. Zhang, L. Kleiman, and S. Cen, “APOBEC3G inhibits DNA strand transfer during HIV-1 reverse transcription,” The Journal of Biological Chemistry, vol. 282, no. 44, pp. 32065–32074, 2007. View at Publisher · View at Google Scholar · View at Scopus
  133. X. Wang, Z. Ao, L. Chen, G. Kobinger, J. Peng, and X. Yao, “The cellular antiviral protein APOBEC3G interacts with HIV-1 reverse transcriptase and inhibits its function during viral replication,” Journal of Virology, vol. 86, no. 7, pp. 3777–3786, 2012. View at Publisher · View at Google Scholar
  134. K. Luo, T. Wang, B. Liu et al., “Cytidine deaminases APOBEC3G and APOBEC3F interact with human immunodeficiency virus type 1 integrase and inhibit proviral DNA formation,” Journal of Virology, vol. 81, no. 13, pp. 7238–7248, 2007. View at Publisher · View at Google Scholar · View at Scopus
  135. J. L. Mbisa, W. Bu, and V. K. Pathak, “APOBEC3F and APOBEC3G inhibit HIV-1 DNA integration by different mechanisms,” Journal of Virology, vol. 84, no. 10, pp. 5250–5259, 2010. View at Publisher · View at Google Scholar · View at Scopus
  136. N. Casartelli, F. Guivel-Benhassine, R. Bouziat, S. Brandler, O. Schwartz, and A. Moris, “The antiviral factor APOBEC3G improves CTL recognition of cultured HIV-infected T cells,” The Journal of Experimental Medicine, vol. 207, no. 1, pp. 39–49, 2010. View at Publisher · View at Google Scholar · View at Scopus
  137. J. M. Norman, M. Mashiba, L. A. McNamara et al., “The antiviral factor APOBEC3G enhances the recognition of HIV-infected primary T cells by natural killer cells,” Nature Immunology, vol. 12, no. 10, pp. 975–983, 2011. View at Publisher · View at Google Scholar · View at Scopus
  138. A. M. Sheehy, N. C. Gaddis, and M. H. Malim, “The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif,” Nature Medicine, vol. 9, no. 11, pp. 1404–1407, 2003. View at Publisher · View at Google Scholar · View at Scopus
  139. X. Yu, Y. Yu, B. Liu et al., “Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex,” Science, vol. 302, no. 5647, pp. 1056–1060, 2003. View at Publisher · View at Google Scholar · View at Scopus
  140. S. G. Conticello, R. S. Harris, and M. S. Neuberger, “The Vif protein of HIV triggers degradation of the human antiretroviral DNA deaminase APOBEC3G,” Current Biology, vol. 13, no. 22, pp. 2009–2013, 2003. View at Publisher · View at Google Scholar · View at Scopus
  141. K. Shirakawa, A. Takaori-Kondo, M. Kobayashi et al., “Ubiquitination of APOBEC3 proteins by the Vif-Cullin5-ElonginB-ElonginC complex,” Virology, vol. 344, no. 2, pp. 263–266, 2006. View at Publisher · View at Google Scholar · View at Scopus
  142. R. Mariani, D. Chen, B. Schröfelbauer et al., “Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif,” Cell, vol. 114, no. 1, pp. 21–31, 2003. View at Publisher · View at Google Scholar · View at Scopus
  143. A. Mehle, B. Strack, P. Ancuta, C. Zhang, M. McPike, and D. Gabuzda, “Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway,” The Journal of Biological Chemistry, vol. 279, no. 9, pp. 7792–7798, 2004. View at Publisher · View at Google Scholar · View at Scopus
  144. S. Opi, S. Kao, R. Goila-Gaur et al., “Human immunodeficiency virus type 1 Vif inhibits packaging and antiviral activity of a degradation-resistant APOBEC3G variant,” Journal of Virology, vol. 81, no. 15, pp. 8236–8246, 2007. View at Publisher · View at Google Scholar · View at Scopus
  145. S. Kao, M. A. Khan, E. Miyagi, R. Plishka, A. Buckler-White, and K. Strebel, “The human immunodeficiency virus type 1 Vif protein reduces intracellular expression and inhibits packaging of APOBEC3G (CEM15), a cellular inhibitor of virus infectivity,” Journal of Virology, vol. 77, no. 21, pp. 11398–11407, 2003. View at Publisher · View at Google Scholar · View at Scopus
  146. K. Stopak, C. de Noronha, W. Yonemoto, and W. C. Greene, “HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability,” Molecular Cell, vol. 12, no. 3, pp. 591–601, 2003. View at Publisher · View at Google Scholar · View at Scopus
  147. G. Mercenne, S. Bernacchi, D. Richer et al., “HIV-1 Vif binds to APOBEC3G mRNA and inhibits its translation,” Nucleic Acids Research, vol. 38, no. 2, pp. 633–646, 2009. View at Publisher · View at Google Scholar · View at Scopus
  148. C. Chaipan, J. L. Smith, W. S. Hu, and V. K. Pathak, “APOBEC3G restricts HIV-1 to a greater extent than APOBEC3F and APOBEC3DE in human primary CD4+ T cells and macrophages,” Journal of Virology, vol. 87, no. 1, pp. 444–453, 2013. View at Publisher · View at Google Scholar
  149. L. C. F. Mulder, M. Ooms, S. Majdak et al., “Moderate influence of human APOBEC3F on HIV-1 replication in primary lymphocytes,” Journal of Virology, vol. 84, no. 18, pp. 9613–9617, 2010. View at Publisher · View at Google Scholar · View at Scopus
  150. M. T. Liddament, W. L. Brown, A. J. Schumacher, and R. S. Harris, “APOBEC3F properties and hypermutation preferences indicate activity against HIV-1 in vivo,” Current Biology, vol. 14, no. 15, pp. 1385–1391, 2004. View at Publisher · View at Google Scholar · View at Scopus
  151. H. L. Wiegand, B. P. Doehle, H. P. Bogerd, and B. R. Cullen, “A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins,” The EMBO Journal, vol. 23, no. 12, pp. 2451–2458, 2004. View at Publisher · View at Google Scholar · View at Scopus
  152. K. Bourara, T. J. Liegler, and R. M. Grant, “Target cell APOBEC3C can induce limited G-to-A mutation in HIV-1,” PLoS Pathogens, vol. 3, no. 10, pp. 1477–1485, 2007. View at Publisher · View at Google Scholar · View at Scopus
  153. Y. Dang, M. S. Lai, X. Wang, Y. Han, R. Lampen, and Y.-H. Zheng, “Human cytidine deaminase APOBEC3H restricts HIV-1 replication,” The Journal of Biological Chemistry, vol. 283, no. 17, pp. 11606–11614, 2008. View at Publisher · View at Google Scholar · View at Scopus
  154. Y. Dang, X. Wang, W. J. Esselman, and Y.-H. Zheng, “Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family,” Journal of Virology, vol. 80, no. 21, pp. 10522–10533, 2006. View at Publisher · View at Google Scholar · View at Scopus
  155. B. P. Doehle, A. Schäfer, and B. R. Cullen, “Human APOBEC3B is a potent inhibitor of HIV-1 infectivity and is resistant to HIV-1 Vif,” Virology, vol. 339, no. 2, pp. 281–288, 2005. View at Publisher · View at Google Scholar · View at Scopus
  156. A. Harari, M. Ooms, L. C. F. Mulder, and V. Simon, “Polymorphisms and splice variants influence the antiretroviral activity of Human APOBEC3H,” Journal of Virology, vol. 83, no. 1, pp. 295–303, 2009. View at Publisher · View at Google Scholar · View at Scopus
  157. X. Wang, A. Abudu, S. Son, Y. Dang, P. J. Venta, and Y.-H. Zheng, “Analysis of human APOBEC3H haplotypes and anti-human immunodeficiency virus type 1 activity,” Journal of Virology, vol. 85, no. 7, pp. 3142–3152, 2011. View at Publisher · View at Google Scholar · View at Scopus
  158. J. S. Albin and R. S. Harris, “Interactions of host APOBEC3 restriction factors with HIV-1 in vivo: implications for therapeutics,” Expert Reviews in Molecular Medicine, vol. 12, no. e4, pp. 1–26, 2010. View at Publisher · View at Google Scholar · View at Scopus
  159. J. A. Vázquez-Pérez, C. E. Ormsby, R. Hernández-Juan, K. J. Torres, and G. Reyes-Terán, “APOBEC3G mRNA expression in exposed seronegative and early stage HIV infected individuals decreases with removal of exposure and with disease progression,” Retrovirology, vol. 6, article 23, 2009. View at Publisher · View at Google Scholar · View at Scopus
  160. A. M. Land, T. B. Ball, M. Luo et al., “Human immunodeficiency virus (HIV) type 1 proviral hypermutation correlates with CD4 count in HIV-infected women from Kenya,” Journal of Virology, vol. 82, no. 16, pp. 8172–8182, 2008. View at Publisher · View at Google Scholar · View at Scopus
  161. Y. Kourteva, M. de Pasquale, T. Allos, C. McMunn, and R. T. D’Aquila, “APOBEC3G expression and hypermutation are inversely associated with human immunodeficiency virus type 1 (HIV-1) burden in vivo,” Virology, vol. 430, pp. 1–9, 2012. View at Publisher · View at Google Scholar
  162. N. K. Ulenga, A. D. Sarr, D. Hamel, J.-L. Sankale, S. Mboup, and P. J. Kanki, “The level of APOBEC3G (hA3G)-related G-to-A mutations does not correlate with viral load in HIV type 1-infected individuals,” AIDS Research and Human Retroviruses, vol. 24, no. 10, pp. 1285–1290, 2008. View at Publisher · View at Google Scholar · View at Scopus
  163. A. Piantadosi, D. Humes, B. Chohan, R. S. McClelland, and J. Overbaugh, “Analysis of the percentage of human immunodeficiency virus type 1 sequences that are hypermutated and markers of disease progression in a longitudinal cohort, including one individual with a partially defective vif,” Journal of Virology, vol. 83, no. 16, pp. 7805–7814, 2009. View at Publisher · View at Google Scholar · View at Scopus
  164. N. D. Amoêdo, A. O. Afonso, S. M. Cunha, R. H. Oliveira, E. S. Machado, and M. A. Soares, “Expression of APOBEC3G/3F and G-to-A hypermutation levels in HIV-1-infected children with different profiles of disease progression,” PloS One, vol. 6, no. 8, article e24118, 2011. View at Scopus
  165. X. Jin, A. Brooks, H. Chen, R. Bennett, R. Reichman, and H. Smith, “APOBEC3G/CEM15 (hA3G) mRNA levels associate inversely with human immunodeficiency virus viremia,” Journal of Virology, vol. 79, no. 17, pp. 11513–11516, 2005. View at Publisher · View at Google Scholar · View at Scopus
  166. M. Zhao, W. Geng, Y. Jiang et al., “The associations of hA3G and hA3B mRNA levels with HIV disease progression among HIV-infected individuals of China,” Journal of Acquired Immune Deficiency Syndromes, vol. 53, supplement 1, pp. S4–S9, 2010. View at Publisher · View at Google Scholar · View at Scopus
  167. N. K. Ulenga, A. D. Sarr, S. Thakore-Meloni, J.-L. Sankalé, G. Eisen, and P. J. Kanki, “Relationship between human immunodeficiency type 1 infection and expression of human APOBEC3G and APOBEC3F,” The Journal of Infectious Diseases, vol. 198, no. 4, pp. 486–492, 2008. View at Publisher · View at Google Scholar · View at Scopus
  168. S.-J. Cho, H. Drechsler, R. C. Burke, M. Q. Arens, W. Powderly, and N. O. Davidson, “APOBEC3F and APOBEC3G mRNA levels do not correlate with human immunodeficiency virus type 1 plasma viremia or CD4+ T-cell count,” Journal of Virology, vol. 80, no. 4, pp. 2069–2072, 2006. View at Publisher · View at Google Scholar · View at Scopus
  169. M. Biasin, L. Piacentini, S. Lo Caputo et al., “Apolipoprotein B mRNA-editing enzyme, catalytic polypeptide-like 3G: a possible role in the resistance to HIV of HIV-exposed seronegative individuals,” The Journal of Infectious Diseases, vol. 195, no. 7, pp. 960–964, 2007. View at Publisher · View at Google Scholar · View at Scopus
  170. T. Ejima, M. Hirota, T. Mizukami, M. Otsuka, and M. Fujita, “An anti-HIV-1 compound that increases steady-state expression of apoplipoprotein B mRNA-editing enzyme-catalytic polypeptide-like 3G,” International Journal of Molecular Medicine, vol. 28, no. 4, pp. 613–616, 2011. View at Publisher · View at Google Scholar · View at Scopus
  171. S. Cen, Z.-G. Peng, X.-Y. Li et al., “Small molecular compounds inhibit HIV-1 replication through specifically stabilizing APOBEC3G,” The Journal of Biological Chemistry, vol. 285, no. 22, pp. 16546–16552, 2010. View at Publisher · View at Google Scholar · View at Scopus
  172. R. Nathans, H. Cao, N. Sharova et al., “Small-molecule inhibition of HIV-1 Vif,” Nature Biotechnology, vol. 26, no. 10, pp. 1187–1192, 2008. View at Publisher · View at Google Scholar · View at Scopus
  173. Z. Xiao, E. Ehrlich, K. Luo, Y. Xiong, and X.-F. Yu, “Zinc chelation inhibits HIV Vif activity and liberates antiviral function of the cytidine deaminase APOBEC3G,” The FASEB Journal, vol. 21, no. 1, pp. 217–222, 2007. View at Publisher · View at Google Scholar · View at Scopus
  174. J. F. Hultquist and R. S. Harris, “Leveraging APOBEC3 proteins to alter the HIV mutation rate and combat AIDS,” Future Virology, vol. 4, no. 6, pp. 605–619, 2009. View at Publisher · View at Google Scholar · View at Scopus
  175. L. C. F. Mulder, A. Harari, and V. Simon, “Cytidine deamination induced HIV-1 drug resistance,” Proceedings of the National Academy of Sciences of the United States of America, vol. 105, no. 14, pp. 5501–5506, 2008. View at Publisher · View at Google Scholar · View at Scopus
  176. P. Jern, R. A. Russell, V. K. Pathak, and J. M. Coffin, “Likely role of APOBEC3G-mediated G-to-A mutations in HIV-1 evolution and drug resistance,” PLoS Pathogens, vol. 5, no. 4, Article ID e1000367, 2009. View at Publisher · View at Google Scholar · View at Scopus
  177. N. Wood, T. Bhattacharya, B. F. Keele et al., “HIV evolution in early infection: selection pressures, patterns of insertion and deletion, and the impact of APOBEC,” PLoS Pathogens, vol. 5, no. 5, Article ID e1000414, 2009. View at Publisher · View at Google Scholar · View at Scopus
  178. G. Haché, K. Shindo, J. S. Albin, and R. S. Harris, “Evolution of HIV-1 isolates that use a novel Vif-independent mechanism to resist restriction by human APOBEC3G,” Current Biology, vol. 18, no. 11, pp. 819–824, 2008. View at Publisher · View at Google Scholar · View at Scopus
  179. S. K. Pillai, J. K. Wong, and J. D. Barbour, “Turning up the volume on mutational pressure: is more of a good thing always better? (A case study of HIV-1 Vif and APOBEC3),” Retrovirology, vol. 5, article 26, 2008. View at Publisher · View at Google Scholar · View at Scopus
  180. E.-Y. Kim, T. Bhattacharya, K. Kunstman et al., “Human APOBEC3G-mediated editing can promote HIV-1 sequence diversification and accelerate adaptation to selective pressure,” Journal of Virology, vol. 84, no. 19, pp. 10402–10405, 2010. View at Publisher · View at Google Scholar · View at Scopus
  181. H. A. Sadler, M. D. Stenglein, R. S. Harris, and L. M. Mansky, “APOBEC3G contributes to HIV-1 variation through sublethal mutagenesis,” Journal of Virology, vol. 84, no. 14, pp. 7396–7404, 2010. View at Publisher · View at Google Scholar · View at Scopus
  182. S. Fourati, I. Malet, S. Lambert, et al., “E138K and M184I mutations in HIV-1 reverse transcriptase coemerge as a result of APOBEC3 editing in the absence of drug exposure,” AIDS, vol. 26, no. 13, pp. 1619–1624, 2012. View at Publisher · View at Google Scholar
  183. M. E. Olson, M. Li, R. S. Harris, and D. A. Harki, “Small-molecule APOBEC3G DNA cytosine deaminase inhibitors based on a 4-amino-1, 2, 4-triazole-3-thiol scaffold,” ChemMedChem, vol. 8, pp. 112–117, 2013. View at Publisher · View at Google Scholar
  184. M. Li, S. M. D. Shandilya, M. A. Carpenter et al., “First-in-class small molecule inhibitors of the single-strand DNA cytosine deaminase APOBEC3G,” ACS Chemical Biology, vol. 7, no. 3, pp. 506–517, 2012. View at Publisher · View at Google Scholar · View at Scopus
  185. M. Matsuoka and K.-T. Jeang, “Human T-cell leukaemia virus type 1 (HTLV-1) infectivity and cellular transformation,” Nature Reviews Cancer, vol. 7, no. 4, pp. 270–280, 2007. View at Publisher · View at Google Scholar · View at Scopus
  186. P. Kannian and P. L. Green, “Human T lymphotropic virus type 1 (HTLV-1): molecular biology and oncogenesis,” Viruses, vol. 2, no. 9, pp. 2037–2077, 2010. View at Publisher · View at Google Scholar · View at Scopus
  187. J. H. Richardson, A. J. Edwards, J. K. Cruickshank, P. Rudge, and A. G. Dalgleish, “In vivo cellular tropism of human T-cell leukemia virus type 1,” Journal of Virology, vol. 64, no. 11, pp. 5682–5687, 1990. View at Scopus
  188. E. W. Refsland, M. D. Stenglein, K. Shindo, J. S. Albin, W. L. Brown, and R. S. Harris, “Quantitative profiling of the full APOBEC3 mRNA repertoire in lymphocytes and tissues: implications for HIV-1 restriction,” Nucleic Acids Research, vol. 38, no. 13, pp. 4274–4284, 2010. View at Publisher · View at Google Scholar · View at Scopus
  189. M. Ooms, A. Krikoni, A. K. Kress, V. Simon, and C. Münk, “APOBEC3A, APOBEC3B, and APOBEC3H haplotype 2 restrict human T-lymphotropic virus type 1,” Journal of Virology, vol. 86, no. 11, pp. 6097–6108, 2012. View at Publisher · View at Google Scholar
  190. J.-P. Vartanian, U. Plikat, M. Henry et al., “HIV genetic variation is directed and restricted by DNA precursor availability,” Journal of Molecular Biology, vol. 270, no. 2, pp. 139–151, 1997. View at Publisher · View at Google Scholar · View at Scopus
  191. J. Fan, M. Guangyong, K. Nosaka et al., “APOBEC3G generates nonsense mutations in human T-cell leukemia virus type 1 proviral genomes in vivo,” Journal of Virology, vol. 84, no. 14, pp. 7278–7287, 2010. View at Publisher · View at Google Scholar · View at Scopus
  192. R. Mahieux, R. Suspène, F. Delebecque et al., “Extensive editing of a small fraction of human T-cell leukemia virus type 1 genomes by four APOBEC3 cytidine deaminases,” Journal of General Virology, vol. 86, no. 9, pp. 2489–2494, 2005. View at Publisher · View at Google Scholar · View at Scopus
  193. A. Sasada, A. Takaori-Kondo, K. Shirakawa et al., “APOBEC3G targets human T-cell leukemia virus type 1,” Retrovirology, vol. 2, pp. 1–10, 2005. View at Publisher · View at Google Scholar · View at Scopus
  194. E. Wattel, J.-P. Vartanian, C. Pannetier, and S. Wain-Hobson, “Clonal expansion of human T-cell leukemia virus type I-infected cells in asymptomatic and symptomatic carriers without malignancy,” Journal of Virology, vol. 69, no. 5, pp. 2863–2868, 1995. View at Scopus
  195. M. Cavrois, S. Wain-Hobson, A. Gessain, Y. Plumelle, and E. Wattel, “Adult T-cell leukemia/lymphoma on a background of clonally expanding human T-cell leukemia virus type-1-positive cells,” Blood, vol. 88, no. 12, pp. 4646–4650, 1996. View at Scopus
  196. M. Cavrois, I. Leclercq, O. Gout, A. Gessain, S. Wain-Hobson, and E. Wattel, “Persistent oligoclonal expansion of human T-cell leukemia virus type 1-infected circulating cells in patients with Tropical spastic paraparesis/HTLV-1 associated myelopathy,” Oncogene, vol. 17, no. 1, pp. 77–82, 1998. View at Scopus
  197. D. Derse, S. A. Hill, G. Princler, P. Lloyd, and G. Heidecker, “Resistance of human T cell leukemia virus type 1 to APOBEC3G restriction is mediated by elements in nucleocapsid,” Proceedings of the National Academy of Sciences of the United States of America, vol. 104, no. 8, pp. 2915–2920, 2007. View at Publisher · View at Google Scholar · View at Scopus
  198. J.-H. Kao and D.-S. Chen, “Global control of hepatitis B virus infection,” Lancet Infectious Diseases, vol. 2, no. 7, pp. 395–403, 2002. View at Publisher · View at Google Scholar · View at Scopus
  199. WHO, “HBV Fact Sheet no. 204,” http://www.who.int/mediacentre/factsheets/fs204/en/.
  200. M. C. Gonzalez, R. Suspène, M. Henry, D. Guétard, S. Wain-Hobson, and J.-P. Vartanian, “Human APOBEC1 cytidine deaminase edits HBV DNA,” Retrovirology, vol. 6, article 96, 2009. View at Publisher · View at Google Scholar · View at Scopus
  201. C. Rösler, J. Köck, M. Kann et al., “APOBEC-mediated interference with hepadnavirus production,” Hepatology, vol. 42, no. 2, pp. 301–309, 2005. View at Publisher · View at Google Scholar · View at Scopus
  202. R. Suspène, D. Guétard, M. Henry, P. Sommer, S. Wain-Hobson, and J.-P. Vartanian, “Extensive editing of both hepatitis B virus DNA strands by APOBEC3 cytidine deaminases in vitro and in vivo,” Proceedings of the National Academy of Sciences of the United States of America, vol. 102, no. 23, pp. 8321–8326, 2005. View at Publisher · View at Google Scholar · View at Scopus
  203. T. F. Baumert, C. Rösler, M. H. Malim, and F. von Weizsäcker, “Hepatitis B virus DNA is subject to extensive editing by the human deaminase AP0BEC3C,” Hepatology, vol. 46, no. 3, pp. 682–689, 2007. View at Publisher · View at Google Scholar · View at Scopus
  204. J. Köck and H. E. Blum, “Hypermutation of hepatitis B virus genomes by APOBEC3G, APOBEC3C and APOBEC3H,” Journal of General Virology, vol. 89, no. 5, pp. 1184–1191, 2008. View at Publisher · View at Google Scholar · View at Scopus
  205. M. Henry, D. Guétard, R. Suspène, C. Rusniok, S. Wain-Hobson, and J.-P. Vartanian, “Genetic editing of HBV DNA by monodomain human APOBEC3 cytidine deaminases and the recombinant nature of APOBEC3G,” PLoS ONE, vol. 4, no. 1, article e4277, 2009. View at Publisher · View at Google Scholar · View at Scopus
  206. J.-P. Vartanian, M. Henry, A. Marchio et al., “Massive APOBEC3 editing of hepatitis B viral DNA in cirrhosis,” PLoS Pathogens, vol. 6, no. 5, Article ID e1000928, 2010. View at Publisher · View at Google Scholar · View at Scopus
  207. P. Turelli, B. Mangeat, S. Jost, S. Vianin, and D. Trono, “Inhibition of Hepatitis B virus replication by APOBEC3G,” Science, vol. 303, no. 5665, article 1829, 2004. View at Publisher · View at Google Scholar · View at Scopus
  208. D. H. Nguyen, S. Gummuluru, and J. Hu, “Deamination-independent inhibition of hepatitis B virus reverse transcription by APOBEC3G,” Journal of Virology, vol. 81, no. 9, pp. 4465–4472, 2007. View at Publisher · View at Google Scholar · View at Scopus
  209. W. Zhang, X. Zhang, C. Tian et al., “Cytidine deaminase APOBEC3B interacts with heterogeneous nuclear ribonucleoprotein K and suppresses hepatitis B virus expression,” Cellular Microbiology, vol. 10, no. 1, pp. 112–121, 2008. View at Publisher · View at Google Scholar · View at Scopus
  210. M. Bonvin, F. Achermann, I. Greeve et al., “Interferon-inducible expression of APOBEC3 editing enzymes in human hepatocytes and inhibition of hepatitis B virus replication,” Hepatology, vol. 43, no. 6, pp. 1364–1374, 2006. View at Publisher · View at Google Scholar · View at Scopus
  211. Y. Tanaka, H. Marusawa, H. Seno et al., “Anti-viral protein APOBEC3G is induced by interferon-α stimulation in human hepatocytes,” Biochemical and Biophysical Research Communications, vol. 341, no. 2, pp. 314–319, 2006. View at Publisher · View at Google Scholar · View at Scopus
  212. C. Noguchi, N. Hiraga, N. Mori et al., “Dual effect of APOBEC3G on Hepatitis B virus,” Journal of General Virology, vol. 88, no. 2, pp. 432–440, 2007. View at Publisher · View at Google Scholar · View at Scopus
  213. S. Günther, G. Sommer, U. Plikat et al., “Naturally occurring hepatitis B virus genomes bearing the hallmarks of retroviral G → A hypermutation,” Virology, vol. 235, no. 1, pp. 104–108, 1997. View at Publisher · View at Google Scholar · View at Scopus
  214. S. Margeridon-Thermet, N. S. Shulman, A. Ahmed et al., “Ultra-deep pyrosequencing of hepatitis b virus quasispecies from nucleoside and nucleotide reverse-transcriptase inhibitor (NRTI)-treated patients and NRTI-naive patients,” The Journal of Infectious Diseases, vol. 199, no. 9, pp. 1275–1285, 2009. View at Publisher · View at Google Scholar · View at Scopus
  215. S. Proto, J. A. Taylor, S. Chokshi, N. Navaratnam, and N. V. Naoumov, “APOBEC and iNOS are not the main intracellular effectors of IFN-γ-mediated inactivation of Hepatitis B virus replication,” Antiviral Research, vol. 78, no. 3, pp. 260–267, 2008. View at Publisher · View at Google Scholar · View at Scopus
  216. S. Jost, P. Turelli, B. Mangeat, U. Protzer, and D. Trono, “Induction of antiviral cytidine deaminases does not explain the inhibition of hepatitis B virus replication by interferons,” Journal of Virology, vol. 81, no. 19, pp. 10588–10596, 2007. View at Publisher · View at Google Scholar · View at Scopus
  217. R. Xu, X. Zhang, W. Zhang, Y. Fang, S. Zheng, and X.-F. Yu, “Association of human APOBEC3 cytidine deaminases with the generation of hepatitis virus B x antigen mutants and hepatocellular carcinoma,” Hepatology, vol. 46, no. 6, pp. 1810–1820, 2007. View at Publisher · View at Google Scholar · View at Scopus
  218. D. Moradpour, F. Penin, and C. M. Rice, “Replication of hepatitis C virus,” Nature Reviews Microbiology, vol. 5, no. 6, pp. 453–463, 2007. View at Publisher · View at Google Scholar · View at Scopus
  219. M. Levrero, “Viral hepatitis and liver cancer: the case of hepatitis C,” Oncogene, vol. 25, no. 27, pp. 3834–3847, 2006. View at Publisher · View at Google Scholar · View at Scopus
  220. Z.-G. Peng, Z.-Y. Zhao, Y.-P. Li et al., “Host apolipoprotein b messenger RNA-editing enzyme catalytic polypeptide-like 3G is an innate defensive factor and drug target against hepatitis C virus,” Hepatology, vol. 53, no. 4, pp. 1080–1089, 2011. View at Publisher · View at Google Scholar · View at Scopus
  221. Y. Komohara, H. Yano, S. Shichijo, K. Shimotohno, K. Itoh, and A. Yamada, “High expression of APOBEC3G in patients infected with hepatitis C virus,” Journal of Molecular Histology, vol. 37, no. 8-9, pp. 327–332, 2006. View at Publisher · View at Google Scholar · View at Scopus
  222. M. Á. Jiménez-Sousa, R. Almansa, C. de la Fuente et al., “Gene expression profiling in the first twelve weeks of treatment in chronic hepatitis C patients,” Enfermedades Infecciosas y Microbiologia Clinica, vol. 29, no. 8, pp. 573–580, 2011. View at Publisher · View at Google Scholar · View at Scopus
  223. S. K. Pillai, M. Abdel-Mohsen, J. Guatelli et al., “Role of retroviral restriction factors in the interferon-α-mediated suppression of HIV-1 in vivo,” Proceedings of the National Academy of Sciences of the United States of America, vol. 109, no. 8, pp. 3035–3040, 2012. View at Publisher · View at Google Scholar · View at Scopus
  224. N. Muñoz, X. Castellsagué, A. B. de González, and L. Gissmann, “HPV in the etiology of human cancer,” Vaccine, vol. 24, supplement 3, pp. S3/1–S3/10, 2006.
  225. J.-P. Vartanian, D. Guétard, M. Henry, and S. Wain-Hobson, “Evidence for editing of human papillomavirus DNA by APOBEC3 in benign and precancerous lesions,” Science, vol. 320, no. 5873, pp. 230–233, 2008. View at Publisher · View at Google Scholar · View at Scopus
  226. R. Suspène, M.-M. Aynaud, S. Koch et al., “Genetic editing of herpes simplex virus 1 and epstein-barr herpesvirus genomes by Human APOBEC3 cytidine deaminases in culture and in vivo,” Journal of Virology, vol. 85, no. 15, pp. 7594–7602, 2011. View at Publisher · View at Google Scholar · View at Scopus
  227. P. Gee, Y. Ando, H. Kitayama et al., “APOBEC1-mediated editing and attenuation of herpes simplex virus 1 DNA indicate that neurons have an antiviral role during herpes simplex encephalitis,” Journal of Virology, vol. 85, no. 19, pp. 9726–9736, 2011. View at Publisher · View at Google Scholar · View at Scopus
  228. R. J. Whitley, D. W. Kimberlin, and B. Roizman, “Herpes simplex viruses,” Clinical Infectious Diseases, vol. 26, no. 3, pp. 541–555, 1998. View at Scopus
  229. R. J. Whitley and B. Roizman, “Herpes simplex virus infections,” The Lancet, vol. 357, no. 9267, pp. 1513–1518, 2001. View at Publisher · View at Google Scholar · View at Scopus
  230. C. Chisholm and L. Lopez, “Cutaneous infections caused by herpesviridae: a review,” Archives of Pathology and Laboratory Medicine, vol. 135, no. 10, pp. 1357–1362, 2011. View at Publisher · View at Google Scholar · View at Scopus
  231. N. Mendoza, M. Diamantis, A. Arora et al., “Mucocutaneous manifestations of Epstein-Barr virus infection,” American Journal of Clinical Dermatology, vol. 9, no. 5, pp. 295–305, 2008. View at Publisher · View at Google Scholar · View at Scopus
  232. J. M. Kidd, T. L. Newman, E. Tuzun, R. Kaul, and E. E. Eichler, “Population stratification of a common APOBEC gene deletion polymorphism,” PLoS Genetics, vol. 3, no. 4, article e63, 2007. View at Publisher · View at Google Scholar · View at Scopus
  233. M. OhAinle, J. A. Kerns, M. M. H. Li, H. S. Malik, and M. Emerman, “Antiretroelement activity of APOBEC3H was lost twice in recent human evolution,” Cell Host & Microbe, vol. 4, no. 3, pp. 249–259, 2008. View at Publisher · View at Google Scholar · View at Scopus
  234. P. An and C. A. Winkler, “Host genes associated with HIV/AIDS: advances in gene discovery,” Trends in Genetics, vol. 26, no. 3, pp. 119–131, 2010. View at Publisher · View at Google Scholar · View at Scopus
  235. J. R. Lingappa, S. Petrovski, E. Kahle et al., “Genomewide association study for determinants of HIV-1 acquisition and viral set point in HIV-1 serodiscordant couples with quantified virus exposure,” PLoS ONE, vol. 6, no. 12, article e28632, 2011. View at Publisher · View at Google Scholar · View at Scopus
  236. D. van Manen, A. B. van Wout, and H. Schuitemaker, “Genome-wide association studies on HIV susceptibility, pathogenesis and pharmacogenomics,” Retrovirology, vol. 9, no. 70, pp. 1–8, 2012. View at Publisher · View at Google Scholar
  237. Y. Kamatani, S. Wattanapokayakit, H. Ochi et al., “A genome-wide association study identifies variants in the HLA-DP locus associated with chronic hepatitis B in Asians,” Nature Genetics, vol. 41, no. 5, pp. 591–595, 2009. View at Publisher · View at Google Scholar · View at Scopus
  238. H. Zhang, Y. Zhai, Z. Hu et al., “Genome-wide association study identifies 1p36.22 as a new susceptibility locus for hepatocellular carcinoma in chronic hepatitis B virus carriers,” Nature Genetics, vol. 42, no. 9, pp. 755–758, 2010. View at Publisher · View at Google Scholar · View at Scopus
  239. S. Li, J. Qian, Y. Yang, et al., “GWAS identifies novel susceptibility loci on 6p21. 32 and 21q21. 3 for hepatocellular carcinoma in chronic hepatitis B virus carriers,” PLoS Genetics, vol. 8, no. 7, pp. 1–8, 2012.