Pore-forming peptides from spiders

Toxin Reviews

Volumn 24, Issue 3-4, 2005, Pages 345-357

  Villegas, E ^a   Corzo, G ^b  

^a UNIVERSIDAD AUTÓNOMA DEL ESTADO DE MORELOS   (Mexico)

^b INSTITUTO DE BIOTECNOLOGÍA   (Mexico)

Author keywords

Charge distribution; Phospholipid composition; Pore forming peptides

Indexed keywords

CUPIENNIN; GOMESIN; LYCOCITIN; LYCOCITIN 1; LYCOCITIN 2; LYCOCITIN 3; LYCOTOXIN; MAGAININ DERIVATIVE; OXYOPININ; PEPTIDE; PEXIGANAN ACETATE; SPIDER VENOM; UNCLASSIFIED DRUG;

CELL MEMBRANE; CHANNEL GATING; CYTOLYSIS; DEPOLARIZATION; FOOT ULCER; LIPID MEMBRANE; MEMBRANE PERMEABILITY; NONHUMAN; REVIEW; SKIN INFECTION; SPIDER;

ARANEAE;

EID: 27544512987     PISSN: 07313837     EISSN: 15256057     Source Type: Journal    
DOI: 10.1080/07313830500237117     Document Type: Review

References (34)

1. Andres, E., Dimarcq, J. L. (2004). Cationic anti-microbial peptides: from innate immunity study to drug development. Rev. Med. Interne 25:629-635.
2. Andren, D., Rivas, L. (1998). Animal antimicrobial peptides: an overview. Biopolymers 47:415-433.
3. Belokoneva, O. S., Satake, H., Mal'tseva, E. L., Pal'mina, N. P., Villegas, E., Nakajima, T., Corzo, G. (2004). Pore formation of phospholipid membranes by the action of two hemolytic arachnid peptides of different size. Biochim. Biophys. Acta 1664:182-188.
4. Belokoneva, O. S., Villegas, E., Corzo, G., Dai, L., Nakajima, T. (2003). The hemolytic activity of six arachnid cationic peptides is affected by the phosphatidylcholine-to-sphingomyelin ratio in lipid bilayers. Biochim. Biophys. Acta 1617:22-30.
5. Bjellqvist, B., Basse, B., Olsen, E., Celis, J. E. (1994). Reference points for comparisons of two-dimensional maps of proteins from different human cell types defined in a pH scale where isoelectric points correlate with polypeptide compositions. Electrophoresis 15:529-539.
6. Bjellqvist, B., Hughes, G. J., Pasquali, C., Paquet, N., Ravier, F., Sanchez, J. C., Frutiger, S., Hochstrasser, D. (1993). The focusing positions of polypeptides in immobilized pH gradients can be predicted from their amino acid sequences. Electrophoresis 14:1023-1031.
7. Budnik, B. A., Olsen, J. V., Egorov, T. A., Anisimova, V. E., Galkina, T. G., Musolyamov, A. K., Grishin, E. V. Zubarev, R. A. (2004). De novo sequencing of antimicrobial peptides isolated from the venom glands of the wolf spider Lycosa singoriensis. J. Mass Spectrom. 39:193-201.
8. Cirioni, O., Giacometti, A., Ghiselli, R., Dell'Acqua, G., Gov, Y., Kamysz, W., Lukasiak, J., Mocchegiani, F., Orlando, F., D'Amato, G., Balaban, N., Saba, V., Scalise, G. (2003). Prophylactic efficacy of topical temporin A and RNAIII-inhibiting peptide in a subcutaneous rat Pouch model of graft infection attributable to staphylococci with intermediate resistance to glycopeptides. Circulation 108:767-771.
9. Cohen, E., Quistad, G. B. (1998). Cytotoxic effects of arthropod venoms on various cultured cells. Toxicon 36:353-358.
10. Concannon, S. P., Crowe, T. D., Abercrombie, J. J., Molina, C. M., Hou, P., Sukumaran, D. K., Raj, P. A., Leung, K. P. (2003). Susceptibility of oral bacteria to an antimicrobial decapeptide. J. Med. Microbiol. 52:1083-1093.
11. Corzo, G., Villegas, E., Gomez-Lagunas, F., Possani, L. D., Belokoneva, O. S., Nakajima, T. (2002). Oxyopinins, large amphipathic peptides isolated from the venom of the wolf spider Oxyopes kitabensis with cytolytic properties and positive insecticidal cooperativity with spider neurotoxins. J. Biol. Chem. 277:23627-23637.
12. Haeberli, S., Kuhn-Nentwig, L., Schaller, J., Nentwig, W. (2000). Characterisation of antibacterial activity of peptides isolated from the venom of the spider Cupiennius salei (Araneae: Ctenidae). Toxicon 38:373-380.
13. He, K., Ludtke, S. J., Huang, H. W., Worcester, D. L. (1995). Antimicrobial peptide pores in membranes detected by neutron in-plane scattering. Biochemistry 34:15614-15618.
14. He, K., Ludtke, S. J., Worcester, D. L., Huang, H. W. (1996). Neutron scattering in the plane of membranes: structure of alamethicin pores. Biophys. J. 70:2659-2666.
15. Huang, H. W. (2000). Action of antimicrobial peptides: two-stale model. Biochemistry 39:8347-8352.
16. Kazakov, I., Nenilin, A. B., Usmanov, P. B., Tashmukhamedov, B. A. (1985). Channel-forming action-a general property of venoms of spiders in the family Theridiidae (Aranei). Nauchuye Doki Vyss Shkoly Biol Nauki 2:30-33.
17. Kuhn-Nentwig, L. (2003). Antimicrobial and cytolytic peptides of venomous arthropods. Cell Mol. Life Sci. 60:2651-2668.
18. Kuhn-Nentwig, L., Dathe, M., Walz, A., Schaller, J., Nentwig, W. (2002a). Cupiennin 1d*: the cytolytic activity depends on the hydrophobic N-terminus and is modulated by the polar C-terminus. FEBS Lett. 527:193-198.
19. Kuhn-Nentwig, L., Muller, J., Schaller, J., Walz, A., Dathe, M., Nentwig, W. (2002b). Cupiennin 1, a new family of highly basic antimicrobial peptides in the venom of the spider Cupiennius salei (Ctenidae). J. Biol. Chem. 277:11208-11216.
20. Ludtke, S., He, K., Heller, W. T., Harroun, T. A., Yang, L., Huang, H. W. (1996). Membrane pores induced by magainin. Biochemistry 35:13723-13728.
21. Mandard, N., Bulet, P., Caille, A., Daffre, S., Vovelle, F. (2002). The solution structure of gomesin, an antimicrobial cysteine-rich peptide from the spider. Eur. J. Biochem. 269:1190-1198.
22. Matsuzaki, K. (1999). Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes. Biochim. Biophys. Acta 1462:1-10.
23. Matsuzaki, K., Murase, O., Fujii, N., Miyajima, K. (1996). An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation. Biochemistry 35:11361-11368.
24. Nomura, K., Corzo, G., Nakajima, T., Iwashita, T. (2004). Orientation and pore-forming mechanism of a scorpion pore-forming peptide bound to magnetically oriented lipid bilayers. Biophys. J. 87:2497-2507.
25. Ponti, D., Mangoni, M. L., Mignogna, G., Simmaco, M., Barra, D. (2003). An amphibian antimicrobial peptide variant expressed in Nicotiana tabacum confers resistance to phytopathogens. Biochem. J. 370:121-127.
26. Sansom, M. S. (1991). The biophysics of peptide models of ion channels. Prog. Biophys. Mol. Biol. 55:139-235.
27. Silva, P. I., Jr., Daffre, S., Bulet, P. (2000). Isolation and characterization of gomesin, an 18-residue cysteine-rich defense peptide from the spider Acanthoscurria gomesiana hemocytes with sequence similarities to horseshoe crab antimicrobial peptides of the tachyplesin family. J. Biol. Chem. 275:33464-33470.
28. Ulvatne, H. (2003). Antimicrobial peptides: potential use in skin infections. Am. J. Clin. Dermatol. 4:591-595.
29. Wilkins, M. R., Gasteiger, E., Bairoch, A., Sanchez, J.-C., Williams, K. L., Appel, R. D., Hochstrasse, D. F. (1998). Protein Identification and Analysis Tools in the ExPASy Server. In Link, A. J., Ed. 2-D Proteome Analysis Protocols, New Jersey: Humana Press.
30. Wu, M., Maier, E., Benz, R., Hancock, R. E. W. (1999). Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli. Biochemistry 38:7235-7242.
31. Xu, K., Ji, Y., Qu, X. (1989). Purification and characterisation of an antibacterial peptide from venom of Lycosa singoriensis. Acta Zool. Sinica. 35:300-305.
32. Yan, L., Adams, M. E. (1998). Lycotoxins, antimicrobial peptides from venom of the wolf spider Lycosa carolinensis. J. Biol. Chem. 273:2059-2066.
33. Yang, L., Harroun, T. A., Weiss, T. M., Ding, L., Huang, H. W. (2001). Barrel-stave model or toroidal model? A case study on melittin pores. Biophys. J. 81:1475-1485.
34. Zasloff, M. (2002). Antimicrobial peptides of multicellular organisms. Nature 415:389-395.