Identification of a novel cathelicidin antimicrobial peptide from ducks and determination of its functional activity and antibacterial mechanism

Scientific Reports

Volumn 5, Issue , 2015, Pages

  Gao, Wei ^a   Xing, Liwei ^a   Qu, Pei ^a   Tan, Tingting ^a   Yang, Na ^a   Li, Dan ^a   Chen, Huixian ^a   Feng, Xingjun ^a  

^a NORTHEAST AGRICULTURAL UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIINFECTIVE AGENT; CATHELICIDIN; CATHELICIDIN ANTIMICROBIAL PEPTIDE;

AMINO ACID SEQUENCE; ANIMAL; CELL DEATH; CELL LINE; CELL MEMBRANE PERMEABILITY; CHEMISTRY; DRUG EFFECTS; DUCK; ESCHERICHIA COLI; GENETICS; HEMOLYSIS; HUMAN; MEMBRANE POTENTIAL; METABOLISM; MICROBIAL SENSITIVITY TEST; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PHYLOGENY; SEQUENCE ALIGNMENT; STAPHYLOCOCCUS AUREUS; ULTRASTRUCTURE;

AMINO ACID SEQUENCE; ANIMALS; ANTI-BACTERIAL AGENTS; BASE SEQUENCE; CATHELICIDINS; CELL DEATH; CELL LINE; CELL MEMBRANE PERMEABILITY; DUCKS; ESCHERICHIA COLI; HEMOLYSIS; HUMANS; MEMBRANE POTENTIALS; MICROBIAL SENSITIVITY TESTS; MOLECULAR SEQUENCE DATA; PHYLOGENY; SEQUENCE ALIGNMENT; STAPHYLOCOCCUS AUREUS;

EID: 84948394409     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep17260     Document Type: Article

References (43)

1. Blair, J. M., Webber, M. A., Baylay, A. J., Ogbolu, D. O. & Piddock, L. J. Molecular mechanisms of antibiotic resistance. Nat. Rev. Microbiol. 13, 42-51 (2015).
2. Teixeira, V., Feio, M. J. & Bastos, M. Role of lipids in the interaction of antimicrobial peptides with membranes. Prog. Lipid Res. 51, 149-177 (2012).
3. Zhang, G. & Sunkara, L. T. Avian antimicrobial host defense peptides: from biology to therapeutic applications. Pharmaceuticals. 7, 220-247 (2014).
4. Zanetti, M., Gennaro, R. & Romeo, D. Cathelicidins: a novel protein family with a common proregion and a variable C-terminal antimicrobial domain. FEBS Lett. 374, 1-5 (1995).
5. Nakamichi, Y., Horibe, K., Takahashi, N. & Udagawa, N. Roles of cathelicidins in inflammation and bone loss. Odontology. 102, 137-146 (2014).
6. Zanetti, M. The role of cathelicidins in the innate host defenses of mammals. Curr. Issues Mol. Biol. 7, 179-196 (2005).
7. Zanetti, M., Del Sal, G., Storici, P., Schneider, C. & Romeo, D. The cDNA of the neutrophil antibiotic Bac5 predicts a prosequence homologous to a cysteine proteinase inhibitor that is common to other neutrophil antibiotics. J. Biol. Chem. 268, 522-526 (1993).
8. Wassing, G. M., Bergman, P., Lindbom, L. & Van Der Does, A. M. Complexity of antimicrobial peptide regulation during pathogen-host interactions. Int. J. Antimicrob Ag. 45, 447-454 (2015).
9. Xiao, Y. et al. Identification and functional characterization of three chicken cathelicidins with potent antimicrobial activity. J. Biol. Chem. 281, 2858-2867 (2006).
10. Goitsuka, R. et al. Chicken cathelicidin-B1, an antimicrobial guardian at the mucosal M cell gateway. PNAS. 38, 15063-15068 (2007).
11. van Dijk, A., Veldhuizen, E. J., van Asten, A. J. & Haagsman, H. P. CMAP27, a novel chicken cathelicidin-like antimicrobial protein. Vet. Immunol. Immunopathol. 106, 321-327 (2005).
12. Wang, Y. et al. Molecular cloning and characterization of novel cathelicidin-derived myeloid antimicrobial peptide from Phasianus colchicus. Dev. Comp. Immunol. 35, 314-322 (2011).
13. Feng, F. et al. Gene cloning, expression and characterization of avian cathelicidin orthologs, Cc-CATHs, from Coturnix coturnix. FEBS J. 278, 1573-1584 (2011).
14. Yu, H. et al. Novel cathelicidins from pigeon highlights evolutionary convergence in avian cathelicidins and functions in modulation of innate immunity. Sci. Rep. 5, 11082, doi: 10.1038/srep11082 (2015).
15. Huang, Y. et al. The duck genome and transcriptome provide insight into an avian influenza virus reservoir species. Nat. Genet. 45, 776-783 (2013).
16. Scocchi, M., Skerlavaj, B., Romeo, D. & Gennaro, R. Proteolytic cleavage by neutrophil elastase converts inactive storage proforms to antibacterial bactenecins. Eur. J. Biochem. 209, 589-595 (1992).
17. Panyutich, A., Shi, J., Boutz, P. L., Zhao, C. & Ganz, T. Porcine polymorphonuclear leukocytes generate extracellular microbicidal activity by elastase-mediated activation of secreted proprotegrins. Infect. Immun. 65, 978-985 (1997).
18. Burgess, D. J. Microbial genetics: amplified origins of antibiotic resistance. Nat. Rev. Genet. 15, 362 (2014).
19. Maroti, G., Kereszt, A., Kondorosi, E. & Mergaert, P. Natural roles of antimicrobial peptides in microbes, plants and animals. Res. Microbiol. 162, 363-374 (2012).
20. Ramanathan, B., Davis, E. G., Ross, C. R. & Blecha, F. Cathelicidins: microbiocidal activity, mechanisms of action, and roles in innate immunity. Microbes Infect. 4, 361-372 (2002).
21. Wuerth, K. & Hancock, R. E. W. New insights into cathelicidin modulation of adaptive immunity. Eur. J. Immunol. 41, 2817-2819 (2011).
22. Tomasinsig, L. & Zanetti, M. The cathelicidins-structure, function and evolution. Curr. Protein Pept. Sci. 6, 23-34 (2005).
23. Cole, A. M. et al. Inhibition of neutrophil elastase prevents cathelicidin activation and impairs clearance of bacteria from wounds. Blood. 97, 297-304 (2001).
24. Sorensen, O. E. et al. Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3. Blood. 97, 3951-3519 (2001).
25. 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. 268, 6058-6063 (1993).
26. Zarember, K. A. et al. Host defense functions of proteolytically processed and parent (unprocessed) cathelicidins of rabbit granulocytes. Infect. Immun. 70, 569-576 (2002).
27. Shinnar, A. E., Butler, K. L. & Park, H. J. Cathelicidin family of antimicrobial peptides: proteolytic processing and protease resistance. Bioorg Chem. 31, 425-436 (2003).
28. Travis, S. M. et al. Bactericidal activity of mammalian cathelicidin-derived peptides. Infect. Immun. 68, 2748-2755 (2000).
29. Takahashi, D., Shukla, S. K., Prakash, O. & Zhang, G. Structural determinants of host defense peptides for antimicrobial activity and target cell selectivity. Biochimie. 92, 1236-1241 (2010).
30. Sivertsen, A. et al. Synthetic cationic antimicrobial peptides bind with their hydrophobic parts to drug site II of human serum albumin. BMC. Struct. Biol. 14, 4 (2014).
31. Even, M., Sandusky, C. & Barnard, N. Serum-free hybridoma culture: ethical, scientific and safety considerations. Trends Biotechnol. 24, 105-108 (2006).
32. Sato, H. & Feix, J. B. Peptide-membrane interactions and mechanisms of membrane destruction by amphipathic alpha-helical antimicrobial peptides. Biochim. Biophys. Acta. 1758, 1245-1256 (2006).
33. Brogden, K. A. Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 3, 238-250 (2005).
34. Teixeira, V., Feio, M. J. & Bastos, M. Role of lipids in the interaction of antimicrobial peptides with membranes. Prog. Lipid Res. 51, 149-177 (2012).
35. Sieprawska-Lupa, M. et al. Degradation of human antimicrobial peptide LL-37 by Staphylococcus aureus-derived proteinases. Antimicrob. Agents Chemother. 48, 4673-4679 (2004).
36. Subbalakshmi, C. & Sitaram, N. Mechanism of antimicrobial action of indolicidin. FEMS Microbiol. Lett. 160, 91-96 (1998).
37. Park, C. B., Kim, H. S. & 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, 253-257 (1998).
38. Zhu, X. et al. Design of imperfectly amphipathic α -helical antimicrobial peptides with enhanced cell selectivity. Acta. Biomater. 10, 244-257 (2014).
39. Xiao, Y. et al. The central kink region of fowlicidin-2, an α -helical host defense peptide, is critically involved in bacterial killing and endotoxin neutralization. J. Innate Immun. 1, 268-280 (2009).
40. Jin, X. et al. Apoptosis-inducing activity of the antimicrobial peptide cecropin of Musca domestica in human hepatocellular carcinoma cell line BEL-7402 and the possible mechanism. Acta. Biochim. Biophys. Sin. (Shanghai). 42, 259-265 (2010).
41. Dong, N. et al. Antimicrobial potency and selectivity of simplified symmetric-end peptides. Biomaterials. 35, 8028-8039 (2014).
42. Han, F. F. et al. Y.Z. Comparing bacterial membrane interactions and antimicrobial activity of porcine lactoferricin-derived peptides. J. Dairy Sci. 96, 3471-3487 (2013).
43. Ma, Z. et al. Characterization of cell selectivity, physiological stability and endotoxin neutralization capabilities of α -helix-based peptide amphiphiles. Biomaterials. 52, 517-530 (2015).