Characterization and functional analysis of cathelicidin-MH, a novel frog-derived peptide with anti-septicemic properties.
Elife
; 102021 04 20.
Article
en En
| MEDLINE
| ID: mdl-33875135
ABSTRACT
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, ß-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.
Palabras clave
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Anuros
/
Sepsis
/
Proteínas Anfibias
/
Catelicidinas
/
Antiinfecciosos
Límite:
Animals
Idioma:
En
Año:
2021
Tipo del documento:
Article