Novel Cathelicidins from Pigeon Highlights Evolutionary Convergence in Avain Cathelicidins and Functions in Modulation of Innate Immunity

Scientific Reports

Volumn 5, Issue , 2015, Pages

  Yu, Haining ^a   Lu, Yiling ^a   Qiao, Xue ^a   Wei, Lin ^b   Fu, Tingting ^a   Cai, Shasha ^a   Wang, Chen ^a   Liu, Xuelian ^a   Zhong, Shijun ^a   Wang, Yipeng ^b  

^a DALIAN UNIVERSITY OF TECHNOLOGY   (China)

^b SOOCHOW UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIINFECTIVE AGENT; CATHELICIDIN; COMPLEMENTARY DNA; INDUCIBLE NITRIC OXIDE SYNTHASE; TOLL LIKE RECEPTOR 4;

AMINO ACID SEQUENCE; ANIMAL; CELL DEATH; CELL MEMBRANE PERMEABILITY; CHEMISTRY; CIRCULAR DICHROISM; DRUG EFFECTS; EVOLUTION; GENETICS; HEMOLYSIS; HUMAN; IMMUNOLOGY; IMMUNOMODULATION; INNATE IMMUNITY; METABOLISM; MOLECULAR GENETICS; MOUSE; NUCLEOTIDE SEQUENCE; PHYLOGENY; PIGEONS AND DOVES; RAW 264.7 CELL LINE; SIGNAL TRANSDUCTION;

AMINO ACID SEQUENCE; ANIMALS; ANTI-INFECTIVE AGENTS; BASE SEQUENCE; BIOLOGICAL EVOLUTION; CATHELICIDINS; CELL DEATH; CELL MEMBRANE PERMEABILITY; CIRCULAR DICHROISM; COLUMBIDAE; DNA, COMPLEMENTARY; HEMOLYSIS; HUMANS; IMMUNITY, INNATE; IMMUNOMODULATION; MICE; MOLECULAR SEQUENCE DATA; NITRIC OXIDE SYNTHASE TYPE II; PHYLOGENY; RAW 264.7 CELLS; SIGNAL TRANSDUCTION; TOLL-LIKE RECEPTOR 4;

EID: 84937692376     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep11082     Document Type: Article

References (45)

1. Zanetti, M. The role of cathelicidins in the innate host defenses of mammals. Curr. Issues. Mol. Biol. 7, 179-196 (2005).
2. Ramanathan, B., Davis, E. G., Ross, C. R. & Blecha, F. Cathelicidins: microbicidal activity, mechanisms of action, and roles in innate immunity. Microbes. Infect. 4, 361-372 (2002).
3. Zanetti, M. Cathelicidins, multifunctional peptides of the innate immunity. J. Leukoc. Biol. 75, 39-48 (2004).
4. Gennaro, R., and Zanetti, M. Structural features and biological activities of the cathelicidin-derived antimicrobial peptides. Biopolymers. 55, 31-49 (2000).
5. Zanetti, M., Gennaro, R., Scocchi, M. & Skerlavaj, B. Structure and biology of cathelicidins. Adv. Exp. Med. Biol. 479, 203-218 (2000).
6. Carretero, M. et al. In vitro and in vivo wound healing-promoting activities of human cathelicidin LL-37. J. Invest. Dermatol. 128, 223-236 (2008).
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. Durr, U. H., Sudheendra, U. S. & Ramamoorthy, A. LL-37, the only human member of the cathelicidin family of antimicrobial peptides. Biochim. Biophys. Acta. 1758, 1408-1425 (2006).
9. Bals, R., and Wilson, J. M. Cathelicidins-a family of multifunctional antimicrobial peptides. Cell. Mol. Life. Sci. 60, 711-720 (2003).
10. Gennaro, R., Skerlavaj, B. & Romeo, D. Purification, composition, and activity of two bactenecins, antibacterial peptides of bovine neutrophils. Infect. Immun. 57, 3142-3146 (1989).
11. Zanetti, M., Litteri, L., Gennaro, R., Horstmann, H. & Romeo, D. Bactenecins, defense polypeptides of bovine neutrophils, are generated from precursor molecules stored in the large granules. J. Cell. Biol. 111, 1363-1371 (1990).
12. Uzzell, T., Stolzenberg, E. D., Shinnar, A. E. & Zasloff, M. Hagfish intestinal antimicrobial peptides are ancient cathelicidins. Peptides. 24, 1655-1667 (2003).
13. Zhu, S. Did cathelicidins, a family of multifunctional host-defense peptides, arise from a cysteine protease inhibitor? Trends. Microbiol. 16, 353-360 (2008).
14. Zaiou, M. & Gallo, R. L. Cathelicidins, essential gene-encoded mammalian antibiotics. J. Mol. Med (Berl). 80, 549-561 (2002).
15. Tomasinsig, L. & Zanetti, M. The cathelicidins-structure, function and evolution. Curr. Protein. Pept. Sci. 6, 23-34 (2005).
16. Feng, F. et al. Gene cloning, expression and characterization of avian cathelicidin orthologs, Cc-CATHs, from Coturnix coturnix. FEBS. J. 278, 1573-1584 (2011).
17. Finlay, B. B. & Hancock, R. E. Can innate immunity be enhanced to treat microbial infections? Nat. Rev. Microbiol. 2, 497-504 (2004).
18. Bowdish, D. M. et al. Impact of LL-37 on anti-infective immunity. J. Leukoc. Biol. 77, 451-459 (2005).
19. Niyonsaba, F., Ushio, H., Nagaoka, I., Okumura, K. & Ogawa, H. The human beta-defensins (-1, -2, -3, -4) and cathelicidin LL-37 induce IL-18 secretion through p38 and ERK MAPK activation in primary human keratinocytes. J. Immunol. 175, 1776-1784 (2005).
20. Thivierge, K. et al. Cathelicidin-like helminth defence molecules (HDMs): absence of cytotoxic, anti-microbial and anti-protozoan activities imply a specific adaptation to immune modulation. PLoS Neglected Tropical Diseases. 7, e2307 (2013).
21. Li, S. A. et al. Naturally occurring antimicrobial peptide OH-CATH30 selectively regulates the innate immune response to protect against sepsis. J. med. Chem. 56, 9136-9145 (2013).
22. Wei, L. et al. Structure and function of a potent lipopolysaccharide-binding antimicrobial and anti-inflammatory peptide. J. med. chem. 56, 3546-3556 (2013).
23. Bridle, A., Nosworthy, E., Polinski, M. & Nowak, B. Evidence of an antimicrobial-immunomodulatory role of Atlantic salmon cathelicidins during infection with Yersinia ruckeri. PloS one. 6, e23417 (2011).
24. 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).
25. Gao, B., Sherman, P., Luo, L., Bowie, J. & Zhu, S. Structural and functional characterization of two genetically related meucin peptides highlights evolutionary divergence and convergence in antimicrobial peptides. FASEB J. 23, 1230-1245 (2009).
26. Bignami, G. S. A rapid and sensitive hemolysis neutralization assay for palytoxin. Toxicon. 31, 817-820 (1993).
27. Livak, K. J. & Schmittgen, T. D. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods. 25, 402-408 (2001).
28. Bonneau, R. et al. Rosetta in CASP4: progress in ab initio protein structure prediction. Proteins. Suppl. 5, 119-126 (2001).
29. Laskowski, R. A., Rullmannn, J. A., MacArthur, M. W., Kaptein, R. & Thornton, J. M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR. 8, 477-486 (1996).
30. Xiao, Y. et al. Identification and functional characterization of three chicken cathelicidins with potent antimicrobial activity. J. Biol. Chem. 281, 2858-2867 (2006).
31. Brogden, K. A. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 3, 238-250 (2005).
32. Zasloff, M. Antimicrobial peptides of multicellular organisms. Nature. 415, 389-395 (2002).
33. Hancock, R. E., Nijnik, A. & Philpott, D. J. Modulating immunity as a therapy for bacterial infections. Nat. Rev. Microbiol. 10, 243-254 (2012).
34. Scott, M. G. et al. An anti-infective peptide that selectively modulates the innate immune response. Nat. Biotechnol. 25, 465-472 (2007).
35. Shimazu, R. et al. MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4. J. Exp. Med. 189, 1777-1782 (1999).
36. Viriyakosol, S., Tobias, P. S., Kitchens, R. L. & Kirkland, T. N. MD-2 binds to bacterial lipopolysaccharide. J. Biol. Chem. 276, 38044-38051 (2001).
37. Kim, H. M. et al. Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran. Cell. 130, 906-917 (2007).
38. Morris, G. M. et al. AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility. J. Comput. Chem. 30, 2785-2791 (2009).
39. Akira, S., Uematsu, S. & Takeuchi, O. Pathogen recognition and innate immunity. Cell. 124, 783-801 (2006).
40. Nizet, V. et al. Innate antimicrobial peptide protects the skin from invasive bacterial infection. Nature. 414, 454-457 (2001).
41. Dathe, M. & Wieprecht, T. Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells. Biochim. Biophys. Acta. 1462, 71-87 (1999).
42. Yang, L., Harroun, T. A., Weiss, T. M., Ding, L. & Huang, H. W. Barrel-stave model or toroidal model? A case study on melittin pores. Biophys. J. 81, 1475-1485 (2001).
43. Rosenfeld, Y., Papo, N. & Shai, Y. Endotoxin (lipopolysaccharide) neutralization by innate immunity host-defense peptides. Peptide properties and plausible modes of action. J. Biol. Chem. 281, 1636-1643 (2006).
44. Chi, D. S., Qui, M., Krishnaswamy, G., Li, C. & Stone, W. Regulation of nitric oxide production from macrophages by lipopolysaccharide and catecholamines. Nitric. Oxide. 8, 127-132 (2003).
45. Husebye, H. et al. Endocytic pathways regulate Toll-like receptor 4 signaling and link innate and adaptive immunity. EMBO J. 25, 683-692 (2006).