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Advances in Virology
Volume 2012 (2012), Article ID 803535, 8 pages
http://dx.doi.org/10.1155/2012/803535
Research Article

Resistance of Subtype C HIV-1 Strains to Anti-V3 Loop Antibodies

1Department of Pharmacology, New York University School of Medicine (NYSoM), New York, NY 10016, USA
2Public Health Research Institute and New Jersey Medical School, University of Medicine and Dentistry of New Jersey, Newark, NJ 07101, USA
3Department of Pathology, New York University School of Medicine (NYSoM), New York, NY 10016, USA

Received 19 October 2011; Accepted 2 January 2012

Academic Editor: Domenico Genovese

Copyright © 2012 David Almond et al. 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. K. K. Ariën, G. Vanham, and E. J. Arts, “Is HIV-1 evolving to a less virulent form in humans?” Nature Reviews Microbiology, vol. 5, no. 2, pp. 141–151, 2007. View at Publisher · View at Google Scholar · View at Scopus
  2. S. C. Ball, A. Abraha, K. R. Collins et al., “Comparing the ex vivo fitness of CCR5-tropic human immunodeficiency virus type 1 isolates of subtypes B and C,” Journal of Virology, vol. 77, no. 2, pp. 1021–1038, 2003. View at Publisher · View at Google Scholar · View at Scopus
  3. J. R. Rusche, K. Javaherian, C. McDanal et al., “Antibodies that inhibit fusion of human immunodeficiency virus-infected cells bind a 24-amino acid sequence of the viral envelope, gp120,” Proceedings of the National Academy of Sciences of the United States of America, vol. 85, no. 9, pp. 3198–3202, 1988. View at Scopus
  4. T. J. Palker, M. E. Clark, A. J. Langlois et al., “Type-specific neutralization of the human immunodeficiency virus with antibodies to env-encoded synthetic peptides,” Proceedings of the National Academy of Sciences of the United States of America, vol. 85, no. 6, pp. 1932–1936, 1988. View at Publisher · View at Google Scholar · View at Scopus
  5. J. Goudsmit, C. Debouck, R. H. Meloen et al., “Human immunodeficiency virus type 1 neutralization epitope with conserved architecture elicits early type-specific antibodies in experimentally infected chimpanzees,” Proceedings of the National Academy of Sciences of the United States of America, vol. 85, no. 12, pp. 4478–4482, 1988. View at Scopus
  6. C. C. Huang, M. Tang, M. Y. Zhang et al., “Structural biology: structure of a V3-containing HIV-1 gp120 core,” Science, vol. 310, no. 5750, pp. 1025–1028, 2005. View at Publisher · View at Google Scholar · View at Scopus
  7. M. B. Patel, N. G. Hoffman, and R. Swanstrom, “Subtype-specific conformational differences within the V3 region of subtype B and subtype C human immunodeficiency virus type 1 Env proteins,” Journal of Virology, vol. 82, no. 2, pp. 903–916, 2008. View at Publisher · View at Google Scholar · View at Scopus
  8. L. Xiao, S. M. Owen, I. Goldman et al., “CCR5 coreceptor usage of non-syncytium-inducing primary HIV-1 is independent of phylogenetically distinct global HIV-1 isolates: delineation of consensus motif in the V3 domain that predicts CCR-5 usage,” Virology, vol. 240, no. 1, pp. 83–92, 1998. View at Publisher · View at Google Scholar · View at Scopus
  9. T. Shioda, J. A. Levy, and C. Cheng-Mayer, “Macrophage and T cell-line tropisms of HIV-1 are determined by specific regions of the envelope gp120 gene,” Nature, vol. 349, no. 6305, pp. 167–169, 1991. View at Publisher · View at Google Scholar · View at Scopus
  10. S. S. Hwang, T. J. Boyle, H. K. Lyerly, and B. R. Cullen, “Identification of the envelope V3 loop as the primary determinant of cell tropism in HIV-1,” Science, vol. 253, no. 5015, pp. 71–74, 1991. View at Scopus
  11. R. A. M. Fouchier, M. Groenink, N. A. Kootstra et al., “Phenotype-associated sequence variation in the third variable domain of the human immunodeficiency virus type 1 gp120 molecule,” Journal of Virology, vol. 66, no. 5, pp. 3183–3187, 1992. View at Scopus
  12. J. J. De Jong, A. De Ronde, W. Keulen, M. Tersmette, and J. Goudsmit, “Minimal requirements for the human immunodeficiency virus type 1 V3 domain to support the syncytium-inducing phenotype: analysis by single amino acid substitution,” Journal of Virology, vol. 66, no. 11, pp. 6777–6780, 1992. View at Scopus
  13. J. De Jong, F. Simon, G. Van Der Groen et al., “V3 loop sequence analysis of seven HIV type 1 group O isolates phenotyped in peripheral blood mononuclear cells and MT-2 cells,” AIDS Research and Human Retroviruses, vol. 12, no. 16, pp. 1503–1507, 1996. View at Scopus
  14. T. Cardozo, J. Swetnam, A. Pinter et al., “Worldwide distribution of HIV type 1 epitopes recognized by human anti-V3 monoclonal antibodies,” AIDS Research and Human Retroviruses, vol. 25, no. 4, pp. 441–450, 2009. View at Publisher · View at Google Scholar
  15. R. L. Stanfield, M. K. Gorny, S. Zolla-Pazner, and I. A. Wilson, “Crystal structures of human immunodeficiency virus type 1 (HIV-1) neutralizing antibody 2219 in complex with three different V3 peptides reveal a new binding mode for HIV-1 cross-reactivity,” Journal of Virology, vol. 80, no. 12, pp. 6093–6105, 2006. View at Publisher · View at Google Scholar · View at Scopus
  16. R. L. Stanfield, M. K. Gorny, C. Williams, S. Zolla-Pazner, and I. A. Wilson, “Structural Rationale for the Broad Neutralization of HIV-1 by Human Monoclonal Antibody 447–52D,” Structure, vol. 12, no. 2, pp. 193–204, 2004. View at Publisher · View at Google Scholar · View at Scopus
  17. C. P. Krachmarov, W. J. Honnen, S. C. Kayman, M. K. Gorny, S. Zolla-Pazner, and A. Pinter, “Factors determining the breadth and potency of neutralization by V3-specific human monoclonal antibodies derived from subjects infected with clade A or clade B strains of human immunodeficiency virus type 1,” Journal of Virology, vol. 80, no. 14, pp. 7127–7135, 2006. View at Publisher · View at Google Scholar · View at Scopus
  18. D. Almond, et al., “Dynamic characterization of the V3 loop crown,” Antiviral Therapy, vol. 12, supplement 2, pp. P13–P31, 2007.
  19. A. Verma and W. Wenzel, “Conformational landscape of the HIV-V3 hairpin loop from all-atom free-energy simulations,” Journal of Chemical Physics, vol. 128, no. 10, Article ID 105103, 6 pages, 2008. View at Publisher · View at Google Scholar · View at Scopus
  20. D. Almond, T. Kimura, X. Kong, J. Swetnam, S. Zolla-Pazner, and T. Cardozo, “Structural conservation predominates over sequence variability in the crown of HIV type 1's V3 loop,” AIDS Research and Human Retroviruses, vol. 26, no. 6, pp. 717–723, 2010. View at Publisher · View at Google Scholar · View at Scopus
  21. R. Abagyan and M. Totrov, “Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins,” Journal of Molecular Biology, vol. 235, no. 3, pp. 983–1002, 1994. View at Publisher · View at Google Scholar · View at Scopus
  22. M. Totrov and R. Abagyan, “Rapid boundary element solvation electrostatics calculations in folding simulations: successful folding of a 23-residue peptide,” Biopolymers, vol. 60, no. 2, pp. 124–133, 2001. View at Publisher · View at Google Scholar · View at Scopus
  23. C. P. Krachmarov, S. C. Kayman, W. J. Honnen, O. Trochev, and A. Pinter, “V3-specific polyclonal antibodies affinity purified from sera of infected humans effectively neutralize primary isolates of human immunodeficiency virus type 1,” AIDS Research and Human Retroviruses, vol. 17, no. 18, pp. 1737–1748, 2001. View at Publisher · View at Google Scholar · View at Scopus
  24. R. I. Connor, B. K. Chen, S. Choe, and N. R. Landau, “Vpr is required for efficient replication of human immunodeficiency virus type-1 in mononuclear phagocytes,” Virology, vol. 206, no. 2, pp. 935–944, 1995. View at Publisher · View at Google Scholar · View at Scopus
  25. M. Sharon, N. Kessler, R. Levy, S. Zolla-Pazner, M. Görlach, and J. Anglister, “Alternative conformations of HIV-1 V3 loops mimic β hairpins in chemokines, suggesting a mechanism for coreceptor selectivity,” Structure, vol. 11, no. 2, pp. 225–236, 2003. View at Publisher · View at Google Scholar · View at Scopus
  26. B. Gaschen, J. Taylor, K. Yusim et al., “Diversity considerations in HIV-1 vaccine selection,” Science, vol. 296, no. 5577, pp. 2354–2360, 2002. View at Publisher · View at Google Scholar · View at Scopus
  27. S. Zolla-Pazner, P. Zhong, K. Revesz et al., “The cross-clade neutralizing activity of a human monoclonal antibody is determined by the GPGR V3 motif of HIV type 1,” AIDS Research and Human Retroviruses, vol. 20, no. 11, pp. 1254–1258, 2004. View at Publisher · View at Google Scholar · View at Scopus
  28. B. F. Haynes, “Case control study of the RV144 trial for immune correlates: the analysis and way forward,” in AIDS Vaccine, Mary Ann Leibert, Bangkok, Thailand, 2011.