Inactivation of the antimicrobial peptide LL-37 by pathogenic Leptospira

dc.creatorOLIVEIRA, PRISCILA N.
dc.creatorCOURROL, DANIELLA S.
dc.creatorCHURA-CHAMBI, ROSA M.
dc.creatorMORGANTI, LIGIA
dc.creatorSOUZA, GISELE O.
dc.creatorFRANZOLIN, MARCIA R.
dc.creatorWUNDER JUNIOR, ELSIO A.
dc.creatorHEINEMANN, MARCOS B.
dc.creatorBARBOSA, ANGELA S.
dc.date2021
dc.date2021-01-21T19:54:17Z
dc.date2021-01-21T19:54:17Z
dc.date.accessioned2023-09-28T14:17:41Z
dc.date.available2023-09-28T14:17:41Z
dc.identifier0882-4010
dc.identifierhttp://200.136.52.105/handle/123456789/31771
dc.identifier150
dc.identifier10.1016/j.micpath.2020.104704
dc.identifier40.78
dc.identifier72.50
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/9001994
dc.descriptionLeptospires 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.
dc.descriptionFunda????o de Amparo ?? Pesquisa do Estado de S??o Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Cient??fico e Tecnol??gico (CNPq)
dc.descriptionFAPESP: 18/12896-2
dc.descriptionCNPq: 131434/2018-7; 309145/2017-8; 305114/2017-4
dc.format1-7
dc.relationMicrobial Pathogenesis
dc.rightsopenAccess
dc.subjectbacteria
dc.subjectantimicrobial agents
dc.subjectinactivation
dc.subjectpeptides
dc.subjectelectrophoresis
dc.subjectproteolysis
dc.titleInactivation of the antimicrobial peptide LL-37 by pathogenic Leptospira
dc.typeArtigo de peri??dico
dc.coverageI


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