Identification and characterization of a novel cathelicidin from ayu, Plecoglossus altivelis

Fish and Shellfish Immunology

Volumn 31, Issue 1, 2011, Pages 52-57

  Lu, X J ^a   Chen, J ^a   Huang, Z A ^a   Shi, Y H ^a   Lr J N ^a  

^a NINGBO UNIVERSITY   (China)

Author keywords

Antimicrobial activity; Cathelicidin; Cleavage site; MRNA expression; Plecoglossus altivelis

Indexed keywords

ANIMALIA; BACTERIA (MICROORGANISMS); PLECOGLOSSUS ALTIVELIS; PROKARYOTA;

EID: 79957855736     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2011.03.005     Document Type: Article

References (27)

1. Ganz T., Selsted M.E., Szklarek D., Harwig S.S., Daher K., Bainton D.F., et al. Defensins. Natural peptide antibiotics of human neutrophils. J Clin Invest 1985, 76:1427-1435.
2. Zasloff M. Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc Natl Acad Sci USA 1987, 84:5449-5453.
3. Zanetti M. Cathelicidins, multifunctional peptides of the innate immunity. J Leukoc Biol 2004, 75:39-48.
4. Bals R., Wilson J.M. Cathelicidins - a family of multifunctional antimicrobial peptides. Cell Mol Life Sci 2003, 60:711-720.
5. Zanetti M., Gennaro R., Skerlavaj B., Tomasinsig L., Circo R. Cathelicidin peptides as candidates for a novel class of antimicrobials. Curr Pharm Des 2002, 8:779-793.
6. Lai Y., Gallo R.L. AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense. Trends Immunol 2009, 30:131-141.
7. Chang C.I., Pleguezuelos O., Zhang Y.A., Zou J., Secombes C.J. Identification of a novel cathelicidin gene in the rainbow trout, Oncorhynchus mykiss. Infect Immun 2005, 73:5053-5064.
8. Chang C.I., Zhang Y.A., Zou J., Nie P., Secombes C.J. Two cathelicidin genes are present in both rainbow trout (Oncorhynchus mykiss) and Atlantic salmon (Salmo salar). Antimicrob Agents 2006, 50:185-195.
9. Maier V.H., Dorn K.V., Gudmundsdottir B.K., Gudmundsson G.H. Characterisation of cathelicidin gene family members in divergent fish species. Mol Immunol 2008, 45:3723-3730.
10. Maier V.H., Schmitt C.N., Gudmundsdottir S., Gudmundsson G.H. Bacterial DNA indicated as an important inducer of fish cathelicidins. Mol Immunol 2008, 45:2352-2358.
11. Uzzell T., Stolzenberg E.D., Shinnar A.E., Zasloff M. Hagfish intestinal antimicrobial peptides are ancient cathelicidins. Peptides 2003, 24:1655-1667.
12. Scocchi M., Pallavicini A., Salgaro R., Bociek K., Gennaro R. The salmonid cathelicidins: A gene family with highly varied C-terminal antimicrobial domains. Comp Biochem Physiol B 2009, 152:376-381.
13. Li C.H., Chen J., Shi Y.H., Li M.Y. Characterization of Listonella anguillarum as the aetiological agent of vibriosis occurred in cultured ayu (Plecoglossus altivelis) in Ninghai county, China. Acta Microbiol Sin 2009, 49:931-937.
14. Nishimori E., Kita-Tsukamoto K., Wakabayashi H. Pseudomonas plecoglossicida sp. nov., the causative agent of bacterial haemorrhagic ascites of ayu, Plecoglossus altivelis. Int J Syst Evol Microbiol 2000, 50:83-89.
15. Tamura K., Dudley J., Nei M., Kumar S. MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol Biol Evol 2007, 24:1596-1599.
16. Sambrook J., Fritsch E.F., Maniatis T. Molecular cloning: a laboratory manual 1989, Cold Spring Harbor Laboratory, New York. 2nd ed.
17. Lee J.Y., Yang S.-T., Lee S.K., Jung H.H., Shin S.Y., Hahm K.-S., et al. Salt-resistant homodimeric bactenecin, a cathelicidin-derived antimicrobial peptide. FEBS J 2008, 275:3911-3920.
18. Goldman M.J., Anderson G.M., Stolzenberg E.D., Kari U.P., Zasloff M., Wilson J.M. Human [beta]-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis. Cell 1997, 88:553-560.
19. Shinnar A.E., Butler K.L., Park H.J. Cathelicidin family of antimicrobial peptides: proteolytic processing and protease resistance. Bioorg Chem 2003, 31:425-436.
20. Ramanathan B., Davis E.G., Ross C.R., Blecha F. Cathelicidins: microbicidal activity, mechanisms of action, and roles in innate immunity. Microbes Infect 2002, 4:361-372.
21. Fishelson L. Cytomorphological alterations of the thymus, spleen, head-kidney, and liver in cardinal fish (Apogonidae, Teleostei) as bioindicators of stress. J Morphol 2006, 267:57-69.
22. Cole A.M., Shi J., Ceccarelli A., Kim Y.H., Park A., Ganz T. Inhibition of neutrophil elastase prevents cathelicidin activation and impairs clearance of bacteria from wounds. Blood 2001, 97:297-304.
23. Sorensen O.E., Follin P., Johnsen A.H., Calafat J., Tjabringa G.S., Hiemstra P.S., et al. Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3. Blood 2001, 97:3951-3959.
24. Levy O., Weiss J., Zarember K., Ooi C.E., Elsbach P. Antibacterial 15-kDa protein isoforms (p15s) are members of a novel family of leukocyte proteins. J Biol Chem 1993, 268:6058-6063.
25. Zarember K.A., Katz S.S., Tack B.F., Doukhan L., Weiss J., Elsbach P. Host defense functions of proteolytically processed and parent (unprocessed) cathelicidins of rabbit granulocytes. Infect Immun 2002, 70:569-576.
26. Broekman D.C., Frei D.M., Gylfason G.A., Steinarsson A., Jornvall H., Agerberth B., et al. Cod cathelicidin: Isolation of the mature peptide, cleavage site characterisation and developmental expression. Dev Comp Immunol 2011, 35:296-303.
27. Nijnik A., Hancock R.E.W. The roles of cathelicidin LL-37 in immune defences and novel clinical applications. Curr Opin Hematol 2009, 16:41-47.