Antimicrobial peptide from the skin secretion of the frog Leptodactylus syphax

Toxicon

Volumn 50, Issue 4, 2007, Pages 572-580

  Dourado, Flávio S ^a,b   Leite, José Roberto S A ^b,c   Silva, Luciano P ^b   Melo, Jorge A T ^b   Bloch Jr , Carlos ^b   Schwartz, Elisabeth F ^a  

^a UNIVERSITY OF BRASILIA   (Brazil)

^b EMBRAPA RECURSOS GENÉTICOS E BIOTECNOLOGIA   (Brazil)

^c FEDERAL UNIVERSITY OF PIAUÍ   (Brazil)

Author keywords

Antimicrobial peptides; Frog skin; Leptodactylus syphax; Syphaxin

Indexed keywords

POLYPEPTIDE ANTIBIOTIC AGENT; SYPHAXIN; SYPHAXIN[1-16]; SYPHAXIN[1-22]; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; CYTOTOXICITY TEST; ELECTROSTIMULATION; ERYTHROCYTE; ESCHERICHIA COLI; FROG; HUMAN; HUMAN CELL; INNATE IMMUNITY; LEPTODACTYLUS SYPHAX; LEUKOCYTE; MINIMUM INHIBITORY CONCENTRATION; NONHUMAN; PEPTIDE ANALYSIS; PRIORITY JOURNAL; REVERSED PHASE LIQUID CHROMATOGRAPHY; SKIN SECRETION; STAPHYLOCOCCUS AUREUS;

AMINO ACID SEQUENCE; ANIMALS; ANTIMICROBIAL CATIONIC PEPTIDES; ANURA; HUMANS; MASS SPECTROMETRY; MICROBIAL SENSITIVITY TESTS; MOLECULAR SEQUENCE DATA; SKIN;

ANURA; ESCHERICHIA COLI; LEPTODACTYLIDAE; LEPTODACTYLUS SYPHAX; STAPHYLOCOCCUS AUREUS;

EID: 34548503200     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2007.04.027     Document Type: Article

References (34)

1. Andreu D., and Rivas L. Animal antimicrobial peptides: an overview. Biopolymers (Pept. Sci.) 47 (1999) 415-433
2. Boman H.G. Peptide antibiotics and their role in innate immunity. Ann. Rev. Immunol. 13 (1995) 61-92
3. Brand G.D., Leite J.R.S.A., Silva L.P., Albuquerque S., Prates M.V., Azevedo R.B., Carregaro V., Silva J.S., Sá V.C.L., Brandão R.A., and Bloch Jr. C. Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta: anti-Trypanosoma cruzi activity without cytotoxicity to mammalian cells. J. Biol. Chem. 277 51 (2002) 49332-49340
4. Cao W., Zhou Y., Ma Y., Luo Q., and Wei D. Expression and purification of antimicrobial peptide adenoregulin with C-amidated terminus in Escherichia coli. Protein Express. Purif. 40 (2005) 404-410
5. Conlon J.M., Al-Ghaferi N., Abraham B., Sonnevend A., King J.D., and Nielsen P.F. Purification and properties of laticeptins, an antimicrobial peptide from skin secretions of the South American frog Leptodactylus laticeps. Protein Peptide Lett. 13 (2006) 411-415
6. Frost, D.R., 2006. Amphibian Species of the World: An Online Reference. Version 4 (17 August 2006). Electronic Database accessible at 〈http://research.amnh.org/herpetology/amphibia/index.php〉. American Museum of Natural History, New York, USA.
7. Gibson B.W., Poulter L., Williams D.H., and Maggio J.E. Novel peptide fragments originating from PGLa and the caerulein and xenopsin precursors from Xenopus laevis. J. Biol. Chem. 261 12 (1986) 5341-5349
8. Giovannini M.G., Poulter L., Gibson B.W., and Williams D.H. Biosynthesis and degradation of peptides derived from Xenopus laevis prohormones. Biochem. J. 243 (1987) 113-120
9. Gogichaeva N.V., Williams T., and Alterman M.A. MALDI-TOF/TOF tandem mass spectrometry as a new tool for amino acid analysis. J. Am. Soc. Mass Spectrom. 18 (2007) 279-284
10. + ions of peptides. Side chain specific sequence ions. Int. J. Mass Spectrom. Ion Proc. 86 (1988) 137-154
11. King J.D., Al-Ghaferi N., Abraham B., Sonnevend A., Leprince J., Nielsen P.F., and Conlon J.M. Pentadactylin: an antimicrobial peptide from the skin secretions of the South American bullfrog Leptodactylus pentadactylus. Comp. Biochem. Physiol. C 141 4 (2005) 393-397
12. Lai R., Liu H., Lee W.H., and Zhang Y. A novel bradykinin-related peptide from skin secretions of toad Bombina maxima and its precursor containing six identical copies of the final product. Biochem. Biophys. Res. Commun. 286 2 (2001) 259-263
13. Mangoni M.L., Fiocco D., Mignogna G., Barra D., and Simmaco M. Functional characterization of the 1-18 fragment of esculetin-1b, an antimicrobial peptide from Rana esculenta. Peptides 24 11 (2003) 1771-1777
14. Mor A., and Nicolas P. Isolation and structure of novel defensive peptides from frog skin. Eur. J. Biochem. 219 (1994) 145-154
15. Nascimento A.C.C., Zanotta L.C., Kyaw C.M., Schwartz E.N., Schwartz C.A., Sebben A., Sousa M.V., Fontes W., and Castro M.S. Ocellatins: new antimicrobial peptides from the skin secretion of the South American frog Leptodactylus ocellatus (Anura: Leptodactylidae). Protein J. 23 8 (2004) 501-508
16. National Committee for Clinical Laboratory Standards. Performance Standards for Antimicrobial Susceptibility Testing, NCCLS-approved Standard M100-S9 (1999), National Committee for Clinical Laboratorial Standards, Wayne, PA
17. Nicolas P., and Mor A. Peptides as weapons against microorganisms in the chemical defense system of vertebrates. Ann. Rev. Microbiol. 49 (1995) 277-304
18. Nicolas P., Vanhoye D., and Amiche M. Molecular strategies in biological evolution of antimicrobial peptides. Peptides 24 (2003) 1669-1680
19. Oren Z., and Shai Y. Mode of action of linear amphipatic α-helical antimicrobial peptides. Biopolymers (Pept. Sci.) 47 (1999) 451-463
20. Park C.B., Kim H.S., and Kim S.C. Mechanism of action of the antimicrobial peptide buforin II: buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions. Biochem. Biophys. Res. Commun. 244 (1998) 253-257
21. Park C.B., Yi K., Matsuzaki K., Kim M.S., and Kim S.C. Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: the proline hinge is responsible for the cell-penetrating ability of buforin II. Proc. Natl. Acad. Sci. USA 97 15 (2000) 8245-8250
22. Resnick N.M., Maloy W.L., Robert Guy H., and Zasloff M. A novel endopeptidase from Xenopus that recognizes α-helical secondary structure. Cell 66 3 (1991) 541-554
23. Rinaldi A.C. Antimicrobial peptides from amphibian skin: an expanding scenario. Curr. Opin. Chem. Biol. 6 (2002) 799-804
24. Rollins-Smith L.A., Doersam J.K., Longcore J.E., Taylor S.K., Shamblin J.C., Carey C., and Zasloff M.A. Antimicrobial peptide defenses against pathogens associated with global Amphibian declines. Dev. Comp. Immunol. 26 (2002) 63-72
25. Rollins-Smith L.A., King J.D., Nielsen P.F., Sonnevend A., and Conlon J.M. An antimicrobial peptide from the skin secretions of the mountain chicken frog Leptodactylus fallax (Anura: Leptodactylidae). Regul. Pept. (2005) 124173-124178
26. Sachse C., Jahns-Streubel G., and Henkel E. Evaluation of leukocyte differential count information from the CELL-DYN 3200 Hematology Analyzer. Lab. Hematol. 5 3 (1999) 137-148
27. Saitou N., and Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4 (1987) 406-425
28. Shai Y. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim. Biophys. Acta 1642 (1999) 55-70
29. Simmaco M., Mignogna G., and Barra D. Antimicrobial peptides from amphibian skin: what do they tell us?. Biopolymers (Pept. Sci.) 47 (1998) 435-450
30. VanCompernolle S.E., Taylor R.J., Oswald-Richter K., Jiang J., Youree B.E., Bowie J.H., Tyler M.J., Conlon J.M., Wade D., Aiken C., Dermody T.S., KewalRamani V.N., Rollins-Smith L.A., and Unutmaz D. Antimicrobial peptides from amphibian skin potently inhibit human immunodeficiency virus infection and transfer of virus from dendritic cells to T cells. J. Virol. 79 18 (2005) 11598-11606
31. Vanhoye D., Bruston F., Nicolas P., and Amiche M. Antimicrobial peptides from hylid and ranin frogs originated from a 150-million-year-old ancestral precursor with a conserved signal peptide but a hypermutable antimicrobial domain. Eur. J. Biochem. 270 9 (2003) 2068-2081
32. Yeman M.R., and Yount N.Y. Mechanisms of antimicrobial peptide action and resistance. Pharmacol. Rev. 55 (2003) 27-55
33. Yount N.Y., Bayer A.S., Xionq Y.Q., and Yeaman M.R. Advances in antimicrobial peptide immunobiology. Biopolymers 84 5 (2006) 435-458
34. Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 415 6870 (2002) 389-395