Table of Contents Author Guidelines Submit a Manuscript
BioMed Research International
Volume 2015, Article ID 102129, 11 pages
http://dx.doi.org/10.1155/2015/102129
Review Article

Biologically Active and Antimicrobial Peptides from Plants

1Departamento de Bioquímica, Universidade Federal de Minas Gerais, 31270-901 Belo Horizonte, Brazil
2Unidad Profesional Interdisciplinaria de Biotecnología, Instituto Politécnico Nacional, Avenida Acueducto S/N, Colonia Barrio La Laguna Ticomán, 07320 Mexico City, Mexico

Received 15 August 2014; Revised 13 October 2014; Accepted 31 October 2014

Academic Editor: Dennis K. Bideshi

Copyright © 2015 Carlos E. Salas 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. I. Y. Park, J. H. Cho, K. S. Kim, Y.-B. Kim, M. S. Kim, and S. C. Kim, “Helix stability confers salt resistance upon helical antimicrobial peptides,” The Journal of Biological Chemistry, vol. 279, no. 14, pp. 13896–13901, 2004. View at Publisher · View at Google Scholar · View at Scopus
  2. Z. Wang and G. Wang, “APD: the antimicrobial peptide database,” Nucleic Acids Research, vol. 32, pp. D590–D592, 2004. View at Publisher · View at Google Scholar · View at Scopus
  3. H. I. Zeya and J. K. Spitznagel, “Antibacterial and enzymic basic proteins from leukocyte lysosomes: separation and identification,” Science, vol. 142, no. 3595, pp. 1085–1087, 1963. View at Publisher · View at Google Scholar · View at Scopus
  4. D. Hultmark, H. Steiner, T. Rasmuson, and H. G. Boman, “Insect immunity. Purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia,” European Journal of Biochemistry, vol. 106, no. 1, pp. 7–16, 1980. View at Google Scholar · View at Scopus
  5. Y. Yamaguchi and A. Huffaker, “Endogenous peptide elicitors in higher plants,” Current Opinion in Plant Biology, vol. 14, no. 4, pp. 351–357, 2011. View at Publisher · View at Google Scholar · View at Scopus
  6. R. E. W. Hancock, “Peptide antibiotics,” The Lancet, vol. 349, no. 9049, pp. 418–422, 1997. View at Publisher · View at Google Scholar · View at Scopus
  7. H. G. Boman, “Innate immunity and the normal microflora,” Immunological Reviews, vol. 173, no. 1, pp. 5–16, 2000. View at Publisher · View at Google Scholar · View at Scopus
  8. H. M. Ward, Disease in Plants, Macmillan, 1901.
  9. J.-P. S. Powers, A. Rozek, and R. E. W. Hancock, “Structure-activity relationships for the β-hairpin cationic antimicrobial peptide polyphemusin I,” Biochimica et Biophysica Acta: Proteins and Proteomics, vol. 1698, no. 2, pp. 239–250, 2004. View at Publisher · View at Google Scholar · View at Scopus
  10. L. A. J. Mur, P. Kenton, A. J. Lloyd, H. Ougham, and E. Prats, “The hypersensitive response; the centenary is upon us but how much do we know?” Journal of Experimental Botany, vol. 59, no. 3, pp. 501–520, 2008. View at Publisher · View at Google Scholar · View at Scopus
  11. T. C. Mettenleiter, “Brief overview on cellular virus receptors,” Virus Research, vol. 82, no. 1-2, pp. 3–8, 2002. View at Publisher · View at Google Scholar · View at Scopus
  12. A. A. Bahar and D. Ren, “Antimicrobial peptides,” Pharmaceuticals, vol. 6, no. 12, pp. 1543–1575, 2013. View at Publisher · View at Google Scholar · View at Scopus
  13. H. Jenssen, P. Hamill, and R. E. W. Hancock, “Peptide antimicrobial agents,” Clinical Microbiology Reviews, vol. 19, no. 3, pp. 491–511, 2006. View at Publisher · View at Google Scholar · View at Scopus
  14. N. L. van der Weerden, R. E. W. Hancock, and M. A. Anderson, “Permeabilization of fungal hyphae by the plant defensin NaD1 occurs through a cell wall-dependent process,” Journal of Biological Chemistry, vol. 285, no. 48, pp. 37513–37520, 2010. View at Publisher · View at Google Scholar · View at Scopus
  15. R. Nawrot, J. Barylski, G. Nowicki, J. Broniarczyk, W. Buchwald, and A. Goździcka-Józefiak, “Plant antimicrobial peptides,” Folia Microbiologica, vol. 59, no. 3, pp. 181–196, 2014. View at Publisher · View at Google Scholar · View at Scopus
  16. S. Grün, C. Lindermayr, S. Sell, and J. Durner, “Nitric oxide and gene regulation in plants,” Journal of Experimental Botany, vol. 57, no. 3, pp. 507–516, 2006. View at Publisher · View at Google Scholar · View at Scopus
  17. N. Sitaram and R. Nagaraj, “Interaction of antimicrobial peptides with biological and model membranes: structural and charge requirements for activity,” Biochimica et Biophysica Acta: Biomembranes, vol. 1462, no. 1-2, pp. 29–54, 1999. View at Publisher · View at Google Scholar · View at Scopus
  18. S. Yokoyama, Y. Iida, Y. Kawasaki, Y. Minami, K. Watanabe, and F. Yagi, “The chitin-binding capability of Cy-AMP1 from cycad is essential to antifungal activity,” Journal of Peptide Science, vol. 15, no. 7, pp. 492–497, 2009. View at Publisher · View at Google Scholar · View at Scopus
  19. C. P. Selitrennikoff, “Antifungal Proteins,” Applied and Environmental Microbiology, vol. 67, no. 7, pp. 2883–2894, 2001. View at Publisher · View at Google Scholar · View at Scopus
  20. A. Perez, Q.-X. Li, P. Perez-Romero et al., “A new class of receptor for herpes simplex virus has heptad repeat motifs that are common to membrane fusion proteins,” Journal of Virology, vol. 79, no. 12, pp. 7419–7430, 2005. View at Publisher · View at Google Scholar · View at Scopus
  21. W. Edward Robinson Jr., B. McDougall, D. Tran, and M. E. Selsted, “Anti-HIV-1 activity of indolicidin, an antimicrobial peptide from neutrophils,” Journal of Leukocyte Biology, vol. 63, no. 1, pp. 94–100, 1998. View at Google Scholar · View at Scopus
  22. B. Stec, “Plant thionins: the structural perspective,” Cellular and Molecular Life Sciences, vol. 63, no. 12, pp. 1370–1385, 2006. View at Publisher · View at Google Scholar · View at Scopus
  23. P. B. Pelegrini, B. F. Quirino, and O. L. Franco, “Plant cyclotides: an unusual class of defense compounds,” Peptides, vol. 28, no. 7, pp. 1475–1481, 2007. View at Publisher · View at Google Scholar · View at Scopus
  24. H. U. Stotz, J. G. Thomson, and Y. Wang, “Plant defensins: defense, development and application,” Plant Signaling & Behavior, vol. 4, no. 11, pp. 1010–1012, 2009. View at Publisher · View at Google Scholar · View at Scopus
  25. R. Fernandez-de Caleya, B. Gonzalez-Pascual, F. García-Olmedo, and P. Carbonero, “Susceptibility of phytopathogenic bacteria to wheat purothionins in vitro,” Applied Microbiology, vol. 23, no. 5, pp. 998–1000, 1972. View at Google Scholar · View at Scopus
  26. Y. Liu, W. Gong, C. C. Huang, W. Herr, and X. Cheng, “Crystal structure of the conserved core of the herpes simplex virus transcriptional regulatory protein VP16,” Genes and Development, vol. 13, no. 13, pp. 1692–1703, 1999. View at Publisher · View at Google Scholar · View at Scopus
  27. M. Bruix, M. A. Jiménez, J. Santoro et al., “Solution structure of γ1-H and γ1-P thionins from barley and wheat endosperm determined by 1H-NMR: a structural motif common to toxic arthropod proteins,” Biochemistry, vol. 32, no. 2, pp. 715–724, 1993. View at Publisher · View at Google Scholar · View at Scopus
  28. B. Yasin, W. Wang, M. Pang et al., “θ defensins protect cells from infection by herpes simplex virus by inhibiting viral adhesion and entry,” Journal of Virology, vol. 78, no. 10, pp. 5147–5156, 2004. View at Publisher · View at Google Scholar · View at Scopus
  29. P. B. Pelegrini, R. P. Del Sarto, O. N. Silva, O. L. Franco, and M. F. Grossi-De-Sa, “Antibacterial peptides from plants: what they are and how they probably work,” Biochemistry Research International, vol. 2011, Article ID 250349, 9 pages, 2011. View at Publisher · View at Google Scholar · View at Scopus
  30. S. Sinha, N. Cheshenko, R. I. Lehrer, and B. C. Herold, “NP-1, a rabbit α-defensin, prevents the entry and intercellular spread of herpes simplex virus type 2,” Antimicrobial Agents and Chemotherapy, vol. 47, no. 2, pp. 494–500, 2003. View at Publisher · View at Google Scholar · View at Scopus
  31. M. Wachinger, A. Kleinschmidt, D. Winder et al., “Antimicrobial peptides melittin and cecropin inhibit replication of human immunodeficiency virus 1 by suppressing viral gene expression,” Journal of General Virology, vol. 79, no. 4, pp. 731–740, 1998. View at Google Scholar · View at Scopus
  32. S. Laquerre, R. Argnani, D. B. Anderson, S. Zucchini, R. Manservigi, and J. C. Glorioso, “Heparan sulfate proteoglycan binding by herpes simplex virus type 1 glycoproteins B and C, which differ in their contributions to virus attachment, penetration, and cell-to-cell spread,” Journal of Virology, vol. 72, no. 7, pp. 6119–6130, 1998. View at Google Scholar · View at Scopus
  33. J. H. Andersen, H. Jenssen, K. Sandvik, and T. J. Gutteberg, “Anti-HSV activity of lactoferrin and lactoferricin is dependent on the presence of heparan sulphate at the cell surface,” Journal of Medical Virology, vol. 74, no. 2, pp. 262–271, 2004. View at Publisher · View at Google Scholar · View at Scopus
  34. D. WuDunn and P. G. Spear, “Initial interaction of herpes simplex virus with cells is binding to heparan sulfate,” Journal of Virology, vol. 63, no. 1, pp. 52–58, 1989. View at Google Scholar · View at Scopus
  35. Y. Liu, J. Luo, C. Xu et al., “Purification, characterization, and molecular cloning of the gene of a seed-specific antimicrobial protein from pokeweed,” Plant Physiology, vol. 122, no. 4, pp. 1015–1024, 2000. View at Publisher · View at Google Scholar · View at Scopus
  36. R. H. Tailor, D. P. Acland, S. Attenborough et al., “A novel family of small cysteine-rich antimicrobial peptides from seed of Impatiens balsamina is derived from a single precursor protein,” The Journal of Biological Chemistry, vol. 272, no. 39, pp. 24480–24487, 1997. View at Publisher · View at Google Scholar · View at Scopus
  37. D. Palumbo, M. Iannaccone, A. Porta, and R. Capparelli, “Experimental antibacterial therapy with puroindolines, lactoferrin and lysozyme in Listeria monocytogenes-infected mice,” Microbes and Infection, vol. 12, no. 7, pp. 538–545, 2010. View at Publisher · View at Google Scholar · View at Scopus
  38. J. P. Marcus, J. L. Green, K. C. Goulter, and J. M. Manners, “A family of antimicrobial peptides is produced by processing of a 7S globulin protein in Macadamia integrifolia kernels,” Plant Journal, vol. 19, no. 6, pp. 699–710, 1999. View at Publisher · View at Google Scholar · View at Scopus
  39. F. R. G. Terras, K. Eggermont, V. Kovaleva et al., “Small cysteine-rich antifungal proteins from radish: their role in host defense,” The Plant Cell, vol. 7, no. 5, pp. 573–588, 1995. View at Publisher · View at Google Scholar · View at Scopus
  40. U. Zottich, M. Da Cunha, A. O. Carvalho et al., “Purification, biochemical characterization and antifungal activity of a new lipid transfer protein (LTP) from Coffea canephora seeds with α-amylase inhibitor properties,” Biochimica et Biophysica Acta: General Subjects, vol. 1810, no. 4, pp. 375–383, 2011. View at Publisher · View at Google Scholar · View at Scopus
  41. C. Remuzgo, T. S. Oewel, S. Daffre et al., “Chemical synthesis, structure-activity relationship, and properties of shepherin I: a fungicidal peptide enriched in glycine-glycine-histidine motifs,” Amino Acids, vol. 46, no. 11, pp. 2573–2586, 2014. View at Publisher · View at Google Scholar
  42. M. Berrocal-Lobo, A. Segura, M. Moreno, G. López, F. García-Olmedo, and A. Molina, “Snakin-2, an antimicrobial peptide from potato whose gene is locally induced by wounding and responds to pathogen infection,” Plant Physiology, vol. 128, no. 3, pp. 951–961, 2002. View at Publisher · View at Google Scholar · View at Scopus
  43. M. Fujimura, Y. Minami, K. Watanabe, and K. Tadera, “Purification, characterization, and sequencing of a novel type of antimicrobial peptides, Fa-AMP1 and Fa-AMP2, from seeds of buckwheat (Fagopyrum esculentum Moench.),” Bioscience, Biotechnology and Biochemistry, vol. 67, no. 8, pp. 1636–1642, 2003. View at Publisher · View at Google Scholar · View at Scopus
  44. A. Segura, M. Moreno, A. Molina, and F. García-Olmedo, “Novel defensin subfamily from spinach (Spinacia oleracea),” FEBS Letters, vol. 435, no. 2-3, pp. 159–162, 1998. View at Publisher · View at Google Scholar · View at Scopus
  45. J. H. Wong and T. B. Ng, “Lunatusin, a trypsin-stable antimicrobial peptide from lima beans (Phaseolus lunatus L.),” Peptides, vol. 26, no. 11, pp. 2086–2092, 2005. View at Publisher · View at Google Scholar · View at Scopus
  46. H. W. Jack and B. N. Tzi, “Vulgarinin, a broad-spectrum antifungal peptide from haricot beans (Phaseolus vulgaris),” International Journal of Biochemistry and Cell Biology, vol. 37, no. 8, pp. 1626–1632, 2005. View at Publisher · View at Google Scholar · View at Scopus
  47. L. A. Rivillas-Acevedo and M. Soriano-García, “Isolation and biochemical characterization of an antifungal peptide from Amaranthus hypochondriacus seeds,” Journal of Agriculture and Food Chemistry, vol. 55, no. 25, pp. 10156–10161, 2007. View at Google Scholar
  48. S. Sharma, H. N. Verma, and N. K. Sharma, “Cationic bioactive peptide from the seeds of benincasa hispida,” International Journal of Peptides, vol. 2014, Article ID 156060, 12 pages, 2014. View at Publisher · View at Google Scholar · View at Scopus
  49. X. Y. Ye, T. B. Ng, and P. F. Rao, “Cicerin and arietin, novel chickpea peptides with different antifungal potencies,” Peptides, vol. 23, no. 5, pp. 817–822, 2002. View at Publisher · View at Google Scholar · View at Scopus
  50. Y. S. Chan, J. H. Wong, E. F. Fang, W. L. Pan, and T. B. Ng, “An antifungal peptide from Phaseolus vulgaris cv. brown kidney bean,” Acta Biochim Biophys Sinica, vol. 44, no. 4, pp. 307–315, 2012. View at Publisher · View at Google Scholar · View at Scopus
  51. X. Wu, J. Sun, G. Zhang, H. Wang, and T. B. Ng, “An antifungal defensin from Phaseolus vulgaris cv. “Cloud Bean”,” Phytomedicine, vol. 18, no. 2-3, pp. 104–109, 2011. View at Publisher · View at Google Scholar · View at Scopus
  52. A. B. R. Thomson, M. Keelan, A. Thiesen, M. T. Clandinin, M. Ropeleski, and G. E. Wild, “Small bowel review: normal physiology part 1,” Digestive Diseases and Sciences, vol. 46, no. 12, pp. 2567–2587, 2001. View at Publisher · View at Google Scholar · View at Scopus
  53. P. Hördegen, J. Cabaret, H. Hertzberg, W. Langhans, and V. Maurer, “In vitro screening of six anthelmintic plant products against larval Haemonchus contortus with a modified methyl-thiazolyl-tetrazolium reduction assay,” Journal of Ethnopharmacology, vol. 108, no. 1, pp. 85–89, 2006. View at Publisher · View at Google Scholar · View at Scopus
  54. M. Zasloff, “Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor,” Proceedings of the National Academy of Sciences of the United States of America, vol. 84, no. 15, pp. 5449–5453, 1987. View at Publisher · View at Google Scholar · View at Scopus
  55. Y. Park, S.-H. Jang, D. G. Lee, and K.-S. Hahm, “Antinematodal effect of antimicrobial peptide, PMAP-23, isolated from porcine myeloid against Caenorhabditis elegans,” Journal of Peptide Science, vol. 10, no. 5, pp. 304–311, 2004. View at Publisher · View at Google Scholar · View at Scopus
  56. S. Tagboto and S. Townson, “Antiparasitic properties of medicinal plants and other naturally occurring products,” Advances in Parasitology, vol. 50, pp. 199–295, 2001. View at Publisher · View at Google Scholar · View at Scopus
  57. G. Stepek, D. J. Buttle, I. R. Duce, A. Lowe, and J. M. Behnke, “Assessment of the anthelmintic effect of natural plant cysteine proteinases against the gastrointestinal nematode, Heligmosomoides polygyrus, in vitro,” Parasitology, vol. 130, no. 2, pp. 203–211, 2005. View at Publisher · View at Google Scholar · View at Scopus
  58. N. Benkerroum, “Antimicrobial peptides generated from milk proteins: a survey and prospects for application in the food industry. A review,” International Journal of Dairy Technology, vol. 63, no. 3, pp. 320–338, 2010. View at Publisher · View at Google Scholar · View at Scopus
  59. E. Abeyrathne, H. Y. Lee, C. Jo, K. C. Nam, and D. U. Ahn, “Enzymatic hydrolysis of ovalbumin and the functional properties of the hydrolysates,” Poultry science, vol. 93, no. 10, pp. 2678–2686, 2014. View at Publisher · View at Google Scholar
  60. M. V. Ramos, D. P. Souza, M. T. R. Gomes et al., “A phytopathogenic cysteine peptidase from latex of wild rubber vine Cryptostegia grandiflora,” The Protein Journal, vol. 33, no. 2, pp. 199–209, 2014. View at Publisher · View at Google Scholar · View at Scopus
  61. D. P. Souza, C. D. T. Freitas, D. A. Pereira et al., “Laticifer proteins play a defensive role against hemibiotrophic and necrotrophic phytopathogens,” Planta, vol. 234, no. 1, pp. 183–193, 2011. View at Publisher · View at Google Scholar · View at Scopus
  62. I. López-Expósito, A. Quirós, L. Amigo, and I. Recio, “Casein hydrolysates as a source of antimicrobial, antioxidant and antihypertensive peptides,” Le Lait, vol. 87, no. 4-5, pp. 241–249, 2007. View at Publisher · View at Google Scholar · View at Scopus
  63. M. Paul and G. A. Somkuti, “Hydrolytic breakdown of lactoferricin by lactic acid bacteria,” Journal of Industrial Microbiology and Biotechnology, vol. 37, no. 2, pp. 173–178, 2010. View at Publisher · View at Google Scholar · View at Scopus
  64. G. Le Henanff, T. Heitz, P. Mestre, J. Mutterer, B. Walter, and J. Chong, “Characterization of Vitis vinifera NPR1 homologs involved in the regulation of pathogenesis-related gene expression,” BMC Plant Biology, vol. 9, article 54, 2009. View at Publisher · View at Google Scholar · View at Scopus
  65. F. T. Lay and M. A. Anderson, “Defensins—components of the innate immune system in plants,” Current Protein & Peptide Science, vol. 6, no. 1, pp. 85–101, 2005. View at Publisher · View at Google Scholar · View at Scopus
  66. T. Ganz, M. E. Selsted, D. Szklarek et al., “Defensins. Natural peptide antibiotics of human neutrophils,” The Journal of Clinical Investigation, vol. 76, no. 4, pp. 1427–1435, 1985. View at Publisher · View at Google Scholar · View at Scopus
  67. A. Patil, A. L. Hughes, and G. Zhang, “Rapid evolution and diversification of mammalian α-defensins as revealed by comparative analysis of rodent and primate genes,” Physiological Genomics, vol. 20, pp. 1–11, 2005. View at Publisher · View at Google Scholar · View at Scopus
  68. C. Tian, B. Gao, Q. Fang, G. Ye, and S. Zhu, “Antimicrobial peptide-like genes in Nasonia vitripennis: a genomic perspective,” BMC Genomics, vol. 11, no. 1, article 187, 2010. View at Publisher · View at Google Scholar · View at Scopus
  69. T. Saito, S. I. Kawabata, T. Shigenaga et al., “A novel big defensin identified in horseshoe crab hemocytes: isolation, amino acid sequence, and antibacterial activity,” Journal of Biochemistry, vol. 117, no. 5, pp. 1131–1137, 1995. View at Google Scholar · View at Scopus
  70. B. P. H. J. Thomma, B. P. A. Cammue, and K. Thevissen, “Plant defensins,” Planta, vol. 216, no. 2, pp. 193–202, 2002. View at Publisher · View at Google Scholar · View at Scopus
  71. L. Galgóczy, L. Kovács, and C. Vágvölgyi, “Defensin-like antifungal proteins secreted by filamentous fungi,” in Current Research, Technology and Education Topics in Applied Microbiology and Microbial Technology, pp. 550–559, 2010. View at Google Scholar
  72. P. D. Games, I. S. dos Santos, É. O. Mello et al., “Isolation, characterization and cloning of a cDNA encoding a new antifungal defensin from Phaseolus vulgaris L. seeds,” Peptides, vol. 29, no. 12, pp. 2090–2100, 2008. View at Publisher · View at Google Scholar · View at Scopus
  73. W. F. Broekaert, B. P. A. Cammue, M. F. C. de Bolle, K. Thevissen, G. W. de Samblanx, and R. W. Osborn, “Antimicrobial peptides from plants,” Critical Reviews in Plant Sciences, vol. 16, no. 3, pp. 297–323, 1997. View at Publisher · View at Google Scholar · View at Scopus
  74. R. W. Osborn, G. W. De Samblanx, K. Thevissen et al., “Isolation and characterisation of plant defensins from seeds of Asteraceae, Fabaceae, Hippocastanaceae and Saxifragaceae,” FEBS Letters, vol. 368, no. 2, pp. 257–262, 1995. View at Publisher · View at Google Scholar · View at Scopus
  75. F. García-Olmedo, A. Molina Fernández, J. M. Alamillo, and P. Rodriguez Palenzuela, “Plant defence peptides,” Peptide Science, vol. 47, no. 6, pp. 479–491, 1998. View at Google Scholar
  76. E. I. Finkina, E. I. Shramova, A. A. Tagaev, and T. V. Ovchinnikova, “A novel defensin from the lentil Lens culinaris seeds,” Biochemical and Biophysical Research Communications, vol. 371, no. 4, pp. 860–865, 2008. View at Publisher · View at Google Scholar · View at Scopus
  77. N. P. Möller, K. E. Scholz-Ahrens, N. Roos, and J. Schrezenmeir, “Bioactive peptides and proteins from foods: indication for health effects,” European Journal of Nutrition, vol. 47, no. 4, pp. 171–182, 2008. View at Publisher · View at Google Scholar · View at Scopus
  78. J. Boye, F. Zare, and A. Pletch, “Pulse proteins: processing, characterization, functional properties and applications in food and feed,” Food Research International, vol. 43, no. 2, pp. 414–431, 2010. View at Publisher · View at Google Scholar · View at Scopus
  79. J. Ruiz-Ruiz, G. Dávila-Ortíz, L. Chel-Guerrero, and D. Betancur-Ancona, “Angiotensin I-converting enzyme inhibitory and antioxidant peptide fractions from hard-to-cook bean enzymatic hydrolysates,” Journal of Food Biochemistry, vol. 37, no. 1, pp. 26–35, 2013. View at Publisher · View at Google Scholar · View at Scopus
  80. T. de Jesús Ariza-Ortega, E. Y. Zenón-Briones, J. L. Castrejón-Flores, J. Yáñez-Fernández, Y. de las Mercedes Gómez-Gómez, and M. Del Carmen Oliver-Salvador, “Angiotensin-I-converting enzyme inhibitory, antimicrobial, and antioxidant effect of bioactive peptides obtained from different varieties of common beans (Phaseolus vulgaris L.) with in vivo antihypertensive activity in spontaneously hypertensive rats,” European Food Research and Technology, vol. 239, no. 5, pp. 785–794, 2014. View at Publisher · View at Google Scholar
  81. E. Borjórquez-Balam, J. C. Ruiz Ruiz, M. Segura-Campos, D. Betancur Ancona, and L. Chel Guerrero, “Evaluación de la capacidad antimicrobiana de fracciones peptídicas de hidrolizados proteínicos de frijol lima (Phaseolus lunatus),” in Bioactividad de péptidos derivados de proteínas alimentarias, M. Segura-Campos, L. Chel Guerrero, and D. Betancur Ancona, Eds., pp. 139–154, OmniaScience Monographs, 2013. View at Google Scholar
  82. M. D. M. Yust, J. Pedroche, C. Megías et al., “Rapeseed protein hydrolysates: a source of HIV protease peptide inhibitors,” Food Chemistry, vol. 87, no. 3, pp. 387–392, 2004. View at Publisher · View at Google Scholar · View at Scopus
  83. T. C. Johnson, K. Wada, B. B. Buchanan, and A. Holmgren, “Reduction of purothionin by the wheat seed thioredoxin system,” Plant Physiology, vol. 85, no. 2, pp. 446–451, 1987. View at Google Scholar
  84. J. H. Wong, X. Q. Zhang, H. X. Wang, and T. B. Ng, “A mitogenic defensin from white cloud beans (Phaseolus vulgaris),” Peptides, vol. 27, no. 9, pp. 2075–2081, 2006. View at Publisher · View at Google Scholar · View at Scopus
  85. A. D. Befus, C. Mowat, M. Gilchrist, J. Hu, S. Solomon, and A. Bateman, “Neutrophil defensins induce histamine secretion from mast cells: mechanisms of action,” Journal of Immunology, vol. 163, no. 2, pp. 947–953, 1999. View at Google Scholar · View at Scopus
  86. D. Yang, O. Chertov, S. N. Bykovskaia et al., “β-Defensins: Linking innate and adaptive immunity through dendritic and T cell CCR6,” Science, vol. 286, no. 5439, pp. 525–528, 1999. View at Publisher · View at Google Scholar · View at Scopus
  87. M.-C. Dieu-Nosjean, A. Vicari, S. Lebecque, and C. Caux, “Regulation of dendritic cell trafficking: a process that involves the participation of selective chemokines,” Journal of Leukocyte Biology, vol. 66, no. 2, pp. 252–262, 1999. View at Google Scholar · View at Scopus
  88. J. I. Wheeler and H. R. Irving, “Plant peptide signaling: an evolutionary adaptation,” in Plant Signaling Peptides, pp. 1–23, Springer, 2012. View at Google Scholar
  89. K. A. Lease and J. C. Walker, “The Arabidopsis unannotated secreted peptide database, a resource for plant peptidomics,” Plant Physiology, vol. 142, no. 3, pp. 831–838, 2006. View at Publisher · View at Google Scholar · View at Scopus
  90. R. Hammami, J. Ben Hamida, G. Vergoten, and I. Fliss, “PhytAMP: a database dedicated to antimicrobial plant peptides,” Nucleic Acids Research, vol. 37, no. 1, pp. D963–D968, 2009. View at Publisher · View at Google Scholar · View at Scopus
  91. A. Niarchou, A. Alexandridou, E. Athanasiadis, G. Spyrou, and J. Vadivelu, “C-PAmP: large scale analysis and database construction containing high scoring,” PLoS ONE, vol. 8, no. 11, Article ID e79728, 2013. View at Publisher · View at Google Scholar
  92. K. Oelkers, N. Goffard, G. F. Weiller, P. M. Gresshoff, U. Mathesius, and T. Frickey, “Bioinformatic analysis of the CLE signaling peptide family,” BMC Plant Biology, vol. 8, article 1, 2008. View at Publisher · View at Google Scholar · View at Scopus
  93. T. Billington, M. Pharmawati, and C. A. Gehring, “Isolation and immunoaffinity purification of biologically active plant natriuretic peptide,” Biochemical and Biophysical Research Communications, vol. 235, no. 3, pp. 722–725, 1997. View at Publisher · View at Google Scholar · View at Scopus
  94. M. M. Maryani, G. Bradley, D. M. Cahill, and C. A. Gehring, “Natriuretic peptides and immunoreactants modify osmoticum-dependent volume changes in Solanum tuberosum L. mesophyll cell protoplasts,” Plant Science, vol. 161, no. 3, pp. 443–452, 2001. View at Publisher · View at Google Scholar · View at Scopus
  95. S. Rafudeen, G. Gxaba, G. Makgoke et al., “A role for plant natriuretic peptide immuno-analogues in NaCl- and drought-stress responses,” Physiologia Plantarum, vol. 119, no. 4, pp. 554–562, 2003. View at Publisher · View at Google Scholar · View at Scopus
  96. M. Pharmawati, T. Billington, and C. A. Gehring, “Stomatal guard cell responses to kinetin and natriuretic peptides are cGMP-dependent,” Cellular and Molecular Life Sciences, vol. 54, no. 3, pp. 272–276, 1998. View at Publisher · View at Google Scholar · View at Scopus
  97. I. N. Suwastika and C. A. Gehring, “Natriuretic peptide hormones promote radial water movements from the xylem of Tradescantia shoots,” Cellular and Molecular Life Sciences, vol. 54, no. 10, pp. 1161–1167, 1998. View at Publisher · View at Google Scholar · View at Scopus
  98. M. Morse, G. Pironcheva, and C. Gehring, “AtPNP-A is a systemically mobile natriuretic peptide immunoanalogue with a role in Arabidopsis thaliana cell volume regulation,” FEBS Letters, vol. 556, no. 1–3, pp. 99–103, 2004. View at Publisher · View at Google Scholar · View at Scopus
  99. L. Kwezi, S. Meier, L. Mungur, O. Ruzvidzo, H. Irving, and C. Gehring, “The Arabidopsis thaliana brassinosteroid receptor (AtBRI1) contains a domain that functions as a Guanylyl cyclase In Vitro,” PLoS ONE, vol. 2, no. 5, article e449, 2007. View at Publisher · View at Google Scholar · View at Scopus
  100. Y. Matsubayashi, M. Ogawa, A. Morita, and Y. Sakagami, “An LRR receptor kinase involved in perception of a peptide plant hormone, phytosulfokine,” Science, vol. 296, no. 5572, pp. 1470–1472, 2002. View at Publisher · View at Google Scholar · View at Scopus
  101. G. Pearce, G. Munske, Y. Yamaguchi, and C. A. Ryan, “Structure-activity studies of GmSubPep, a soybean peptide defense signal derived from an extracellular protease,” Peptides, vol. 31, no. 12, pp. 2159–2164, 2010. View at Publisher · View at Google Scholar · View at Scopus
  102. L. Yu, M. Moshelion, and N. Moran, “Extracellular protons inhibit the activity of inward-rectifying potassium channels in the motor cells of Samanea saman pulvini,” Plant Physiology, vol. 127, no. 3, pp. 1310–1322, 2001. View at Publisher · View at Google Scholar · View at Scopus
  103. M. R. Blatt and F. Armstrong, “K+ channels of stomatal guard cells: abscisic-acid-evoked control of the outward rectifier mediated by cytoplasmic pH,” Planta, vol. 191, no. 3, pp. 330–341, 1993. View at Publisher · View at Google Scholar · View at Scopus
  104. J. C. Fletcher, “Signaling of cell fate decisions by CLAVATA3 in Arabidopsis shoot meristems,” Science, vol. 283, no. 5409, pp. 1911–1914, 1999. View at Publisher · View at Google Scholar · View at Scopus
  105. M. Ogawa, H. Shinohara, Y. Sakagami, and Y. Matsubayash, “Arabidopsis CLV3 peptide directly binds CLV1 ectodomain,” Science, vol. 319, no. 5861, p. 294, 2008. View at Publisher · View at Google Scholar · View at Scopus
  106. T. J. Strabala, P. J. O'Donnell, A.-M. Smit et al., “Gain-of-function phenotypes of many CLAVATA3/ESR genes, including four new family members, correlate with tandem variations in the conserved CLAVATA3/ESR domain,” Plant Physiology, vol. 140, no. 4, pp. 1331–1344, 2006. View at Publisher · View at Google Scholar · View at Scopus
  107. T.-T. Xu, X.-F. Song, S.-C. Ren, and C.-M. Liu, “The sequence flanking the N-terminus of the CLV3 peptide is critical for its cleavage and activity in stem cell regulation in Arabidopsis,” BMC Plant Biology, vol. 13, article 225, 2013. View at Publisher · View at Google Scholar · View at Scopus
  108. S. E. Clark, M. P. Running, and E. M. Meyerowitz, “CLAVATA1, a regulator of meristem and flower development in Arabidopsis,” Development, vol. 119, no. 2, pp. 397–418, 1993. View at Google Scholar · View at Scopus
  109. A. Bleckmann, S. Weidtkamp-Peters, C. A. M. Seidel, and R. Simon, “Stem cell signaling in Arabidopsis requires CRN to localize CLV2 to the plasma membrane,” Plant Physiology, vol. 152, no. 1, pp. 166–176, 2010. View at Publisher · View at Google Scholar · View at Scopus
  110. R. Müller, A. Bleckmann, and R. Simon, “The receptor kinase CORYNE of Arabidopsis transmits the stem cell-limiting signal CLAVATA3 independently of CLAVATA1,” The Plant Cell, vol. 20, no. 4, pp. 934–946, 2008. View at Publisher · View at Google Scholar · View at Scopus
  111. R. W. Williams, J. M. Wilson, and E. M. Meyerowitz, “A possible role for kinase-associated protein phosphatase in the Arabidopsis CLAVATA1 signaling pathway,” Proceedings of the National Academy of Sciences of the United States of America, vol. 94, no. 19, pp. 10467–10472, 1997. View at Publisher · View at Google Scholar · View at Scopus
  112. L. P. Yu, E. J. Simon, A. E. Trotochaud, and S. E. Clark, “POLTERGEIST functions to regulate meristem development downstream of the CLAVATA loci,” Development, vol. 127, no. 8, pp. 1661–1670, 2000. View at Google Scholar · View at Scopus
  113. H. Yue, S. Nie, and D. Xing, “Over-expression of Arabidopsis Bax inhibitor-1 delays methyl jasmonate-induced leaf senescence by suppressing the activation of MAP kinase 6,” Journal of Experimental Botany, vol. 63, no. 12, pp. 4463–4474, 2012. View at Publisher · View at Google Scholar · View at Scopus
  114. Y. Ito, I. Nakanomyo, H. Motose et al., “Dodeca-CLE as peptides as suppressors of plant stem cell differentiation,” Science, vol. 313, no. 5788, pp. 842–845, 2006. View at Publisher · View at Google Scholar · View at Scopus
  115. Y. Hirakawa, Y. Kondo, and H. Fukuda, “TDIF peptide signaling regulates vascular stem cell proliferation via the WOX4 homeobox gene in Arabidopsis,” The Plant Cell, vol. 22, no. 8, pp. 2618–2629, 2010. View at Publisher · View at Google Scholar · View at Scopus
  116. G. Suzuki, N. Kai, T. Hirose et al., “Genomic organization of the S locus: Identification and characterization of genes in SLG/SRK region of S9 haplotype of Brassica campestris (syn. rapa),” Genetics, vol. 153, no. 1, pp. 391–400, 1999. View at Google Scholar · View at Scopus
  117. J. B. Nasrallah, T. Nishio, and M. E. Nasrallah, “The self-incompatibility genes of Brassica: expression and use in genetic ablation of floral tissues,” Annual Review of Plant Physiology and Plant Molecular Biology, vol. 42, no. 1, pp. 393–422, 1991. View at Publisher · View at Google Scholar · View at Scopus
  118. A. Kachroo, C. R. Schopfer, M. E. Nasrallah, and J. B. Nasrallah, “Allele-specific receptor-ligand interactions in Brassica self-incompatibility,” Science, vol. 293, no. 5536, pp. 1824–1826, 2001. View at Publisher · View at Google Scholar · View at Scopus
  119. L. Hunt and J. E. Gray, “The signaling peptide EPF2 controls asymmetric cell divisions during stomatal development,” Current Biology, vol. 19, no. 10, pp. 864–869, 2009. View at Publisher · View at Google Scholar · View at Scopus
  120. S. S. Sugano, T. Shimada, Y. Imai et al., “Stomagen positively regulates stomatal density in Arabidopsis,” Nature, vol. 463, no. 7278, pp. 241–244, 2010. View at Publisher · View at Google Scholar · View at Scopus
  121. T. Niwa, T. Kondo, M. Nishizawa, R. Kajita, T. Kakimoto, and S. Ishiguro, “Epidermal Patterning factor like 5 peptide represses stomatal development by inhibiting meristemoid maintenance in Arabidopsis thaliana,” Bioscience, Biotechnology and Biochemistry, vol. 77, no. 6, pp. 1287–1295, 2013. View at Publisher · View at Google Scholar · View at Scopus
  122. E. D. Shpak, J. M. McAbee, L. J. Pillitteri, and K. U. Torii, “Stomatal patterning and differentiation by synergistic interactions of receptor kinases,” Science, vol. 309, no. 5732, pp. 290–293, 2005. View at Publisher · View at Google Scholar · View at Scopus
  123. T.-H. Kim, M. Böhmer, H. Hu, N. Nishimura, and J. I. Schroeder, “Guard cell signal transduction network: advances in understanding abscisic acid, CO2, and Ca2+ signaling,” Annual Review of Plant Biology, vol. 61, pp. 561–591, 2010. View at Publisher · View at Google Scholar · View at Scopus
  124. L. J. Pillitteri and J. Dong, “Stomatal development in arabidopsis,” in The Arabidopsis Book, vol. 11, American Society of Plant Biologists, 2013. View at Google Scholar
  125. A. Mannheim and M. Cheryan, “Continuous hydrolysis of milk protein in a membrane reactor,” Journal of Food Science, vol. 55, no. 2, pp. 381–385, 1990. View at Google Scholar
  126. D. A. Clare and H. E. Swaisgood, “Bioactive milk peptides: a prospectus,” Journal of Dairy Science, vol. 83, no. 6, pp. 1187–1195, 2000. View at Publisher · View at Google Scholar · View at Scopus
  127. P. K. Singh, M. R. Parsek, E. P. Greenberg, and M. J. Welsh, “A component of innate immunity prevents bacterial biofilm development,” Nature, vol. 417, no. 6888, pp. 552–555, 2002. View at Publisher · View at Google Scholar · View at Scopus
  128. J. Overhage, A. Campisano, M. Bains, E. C. W. Torfs, B. H. A. Rehm, and R. E. W. Hancock, “Human host defense peptide LL-37 prevents bacterial biofilm formation,” Infection and Immunity, vol. 76, no. 9, pp. 4176–4182, 2008. View at Publisher · View at Google Scholar · View at Scopus
  129. K. Lewis, “Persister cells,” Annual Review of Microbiology, vol. 64, pp. 357–372, 2010. View at Publisher · View at Google Scholar · View at Scopus
  130. X. Chen, M. Zhang, C. Zhou, N. R. Kallenbach, and D. Ren, “Control of bacterial persister cells by Trp/Arg-containing antimicrobial peptides,” Applied and Environmental Microbiology, vol. 77, no. 14, pp. 4878–4885, 2011. View at Publisher · View at Google Scholar · View at Scopus