The leptospiral LipL21 and LipL41 proteins exhibit a broad spectrum of interactions with host cell components

Autor(es)

Takahashi, M. B. ^{[1, 2]} ; Teixeira, A. F. ^[1] ; Alto, Nascimento ^[1]

Afiliação do(s) autor(es)

^[1] Inst Butantan, Lab Desenvolvimento Vacinas, Sao Paulo - Brazil

^[2] Univ Sao Paulo, Inst Ciencias Biomed, Programa Posgrad Interunidades Biotecnol, Sao Paulo - Brazil

• Tipo de documento: Artigo Científico
• Fonte: VIRULENCE; v. 12, n. 1, p. 2798-2813, DEC 31 2021.
• Citações Web of Science: 0

Resumo

Leptospirosis is a globally prevalent zoonotic disease, and is caused by pathogenic spirochetes from the genus Leptospira. LipL21 and LipL41 are lipoproteins expressed strongly on the outer membrane of pathogenic Leptospira spp. Many studies have shown that both proteins are interesting targets for vaccines and diagnosis. However, their role in host-pathogen interactions remains underexplored. Therefore, we evaluated the capacity of LipL21 and LipL41 to bind with glycosaminoglycans (GAGs), the cell receptors and extracellular matrix, and plasma components by ELISA. Both proteins interacted with collagen IV, laminin, E-cadherin, and elastin dose-dependently. A broad-spectrum binding to plasma components was also observed. Only LipL21 interacted with all the GAG components tested, whereas LipL41 presented a concentration-dependent binding only for chondroitin 4 sulfate. Although, both proteins have the ability to interact with fibrinogen, only LipL21 inhibited fibrin clot formation partially. Both proteins exhibited a decrease in plasminogen binding in the presence of amino caproic acid (ACA), a competitive inhibitor of lysine residues, suggesting that their binding occurs via the kringle domains of plasminogen. LipL41, but not LipL21, was able to convert plasminogen to plasmin, and recruit plasminogen from normal human serum, suggesting that the interaction of this protein with plasminogen may occur in physiological conditions. This work provides the first report demonstrating the capacity of LipL21 and LipL41 to interact with a broad range of host components, highlighting their importance in host-Leptospira interactions. (AU)

• Processo FAPESP: 17/26223-7 - Avaliação do papel funcional de proteínas de superfície de Leptospira interrogans como receptores de células endoteliais e epiteliais do hospedeiro
• Beneficiário: Maria Beatriz Takahashi
• Modalidade de apoio: Bolsas no Brasil - Doutorado Direto
• Processo FAPESP: 19/17488-2 - Avançando no entendimento da patogenicidade e virulência da Leptospira interrogans através de análises proteômicas, estruturais, mutagênicas e imunológicas
• Beneficiário: Ana Lucia Tabet Oller do Nascimento
• Modalidade de apoio: Auxílio à Pesquisa - Temático
• Processo FAPESP: 17/00236-5 - As plaquetas na interface da modulação da imunidade, inflamação e hemostasia na leptospirose
• Beneficiário: Mônica Larucci Vieira
• Modalidade de apoio: Auxílio à Pesquisa - Jovens Pesquisadores