Inactivation of the antimicrobial peptide LL-37 by pathogenic Leptospira
Carregando...
Data
Data de publicação
Autores IPEN
Orientador
Título da Revista
ISSN da Revista
Título do Volume
É parte de
É parte de
É parte de
Microbial Pathogenesis
Exportar
Resumo
Leptospires are aerobic, Gram-negative spirochetes with a high invasive capacity. Pathogenic leptospires secrete
proteases that inactivate a variety of host’s proteins including molecules of the extracellular matrix and of the
human complement system. This strategy, used by several pathogens of medical importance, contributes to
bacterial invasion and immune evasion. In the current work we present evidence that Leptospira proteases also
target human cathelicidin (LL-37), an antimicrobial peptide that plays an important role in the innate immune
response. By using six Leptospira strains, four pathogenic and two saprophytic, we demonstrated that proteases
present in the supernatants of pathogenic strains were capable of degrading LL-37 in a time-dependent manner,
whereas proteolytic degradation was not observed with the supernatants of the two saprophytic strains. Inactivation
of LL-37 was prevented by using the 1,10-phenanthroline inhibitor, thus suggesting the involvement of
metalloproteinases in this process. In addition, the antibacterial activity of LL-37 against two Leptospira strains
was evaluated. Compared to the saprophytic strain, a greater resistance of the pathogenic strain to the action of
the peptide was observed. Our data suggest that the capacity to inactivate the host defense peptide LL-37 may be
part of the virulence arsenal of pathogenic Leptospira, and we hypothesize that its inactivation by the bacteria
may influence the outcome of the disease.
Como referenciar
OLIVEIRA, PRISCILA N.; COURROL, DANIELLA S.; CHURA-CHAMBI, ROSA M.; MORGANTI, LIGIA; SOUZA, GISELE O.; FRANZOLIN, MARCIA R.; WUNDER JUNIOR, ELSIO A.; HEINEMANN, MARCOS B.; BARBOSA, ANGELA S. Inactivation of the antimicrobial peptide LL-37 by pathogenic Leptospira. Microbial Pathogenesis, v. 150, p. 1-7, 2021. DOI: 10.1016/j.micpath.2020.104704. Disponível em: http://200.136.52.105/handle/123456789/31771. Acesso em: 30 Dec 2025.
Esta referência é gerada automaticamente de acordo com as normas do estilo IPEN/SP (ABNT NBR 6023) e recomenda-se uma verificação final e ajustes caso necessário.