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LIC12254 Is a Leptospiral Protein That Interacts with Integrins via the RGD Motif.
Cavenague, Maria F; Teixeira, Aline F; Fernandes, Luis G V; Nascimento, Ana L T O.
Afiliação
  • Cavenague MF; Laboratório de Desenvolvimento de Vacinas, Instituto Butantan, São Paulo 05503-000, SP, Brazil.
  • Teixeira AF; Programa de Pós-Graduação Interunidades em Biotecnologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, São Paulo 05508-900, SP, Brazil.
  • Fernandes LGV; Laboratório de Desenvolvimento de Vacinas, Instituto Butantan, São Paulo 05503-000, SP, Brazil.
  • Nascimento ALTO; Laboratório de Desenvolvimento de Vacinas, Instituto Butantan, São Paulo 05503-000, SP, Brazil.
Trop Med Infect Dis ; 8(5)2023 Apr 26.
Article em En | MEDLINE | ID: mdl-37235297
Pathogenic leptospires can bind to receptors on mammalian cells such as cadherins and integrins. Leptospira effectively adheres to cells, overcomes host barriers and spreads into the bloodstream, reaching internal target organs such as the lungs, liver and kidneys. Several microorganisms produce proteins that act as ligands of integrins through the RGD motif. Here, we characterized a leptospiral RGD-containing protein encoded by the gene lic12254. In silico analysis of pathogenic, intermediate and saprophytic species showed that LIC12254 is highly conserved among pathogenic species, and is unique in presenting the RGD motif. The LIC12254-coding sequence is greatly expressed in the virulent Leptospira interrogans L1-130 strain compared with the culture-attenuated L. interrogans M20 strain. We also showed that the recombinant protein rLIC12254 binds to αVß8 and α8 human integrins most likely via the RGD motif. These interactions are dose-dependent and saturable, a typical property of receptor-ligand interactions. The binding of the recombinant protein lacking this motif-rLIC12254 ΔRAA-to αVß8 was almost totally abolished, while that with the α8 human integrin was decreased by 65%. Taken together, these results suggest that this putative outer membrane protein interacts with integrins via the RGD domain and may play a key role in leptospirosis pathogenesis.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Revista: Trop Med Infect Dis Ano de publicação: 2023 Tipo de documento: Article País de afiliação: Brasil País de publicação: Suíça

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Revista: Trop Med Infect Dis Ano de publicação: 2023 Tipo de documento: Article País de afiliação: Brasil País de publicação: Suíça