Characterization and functional analysis of cathelicidin-MH, a novel frog-derived peptide with anti-septicemic properties.
Characterization and functional analysis of cathelicidin-MH, a novel frog-derived peptide with anti-septicemic properties.
复制标题
具有抗败血症特性的新型青蛙衍生肽 cathelicidin-MH 的表征和功能分析
作者:
Chai J;Chen X;Ye T;Zeng B;Zeng Q;Wu J;Kascakova B;Martins LA;Prudnikova T;Smatanova IK;Kotsyfakis M;Xu X
Antimicrobial peptides form part of the innate immune response and play a vital role in host defense against pathogens. Here we report a new antimicrobial peptide belonging to the cathelicidin family, cathelicidin-MH (cath-MH), from the skin of Microhyla heymonsivogt frog. Cath-MH has a single α-helical structure in membrane-mimetic environments and is antimicrobial against fungi and bacteria, especially Gram-negative bacteria. In contrast to other cathelicidins, cath-MH suppresses coagulation by affecting the enzymatic activities of tissue plasminogen activator, plasmin, β-tryptase, elastase, thrombin, and chymase. Cath-MH protects against lipopolysaccharide (LPS)- and cecal ligation and puncture-induced sepsis, effectively ameliorating multiorgan pathology and inflammatory cytokine through its antimicrobial, LPS-neutralizing, coagulation suppressing effects as well as suppression of MAPK signaling. Taken together, these data suggest that cath-MH is an attractive candidate therapeutic agent for the treatment of septic shock.