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

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...

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Autores principales:	Takahashi MB, Teixeira AF, Nascimento ALTO
Formato:	article
Lenguaje:	EN
Publicado:	Taylor & Francis Group 2021
Materias:	leptospira spp leptospirosis pathogenesis lipl21 lipl41 Infectious and parasitic diseases RC109-216
Acceso en línea:	https://doaj.org/article/e69ab9b9303e4c7382e9f7090c87a695
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spelling	oai:doaj.org-article:e69ab9b9303e4c7382e9f7090c87a6952021-11-26T11:19:49ZThe leptospiral LipL21 and LipL41 proteins exhibit a broad spectrum of interactions with host cell components2150-55942150-560810.1080/21505594.2021.1993427https://doaj.org/article/e69ab9b9303e4c7382e9f7090c87a6952021-12-01T00:00:00Zhttp://dx.doi.org/10.1080/21505594.2021.1993427https://doaj.org/toc/2150-5594https://doaj.org/toc/2150-5608Leptospirosis 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.Takahashi MBTeixeira AFNascimento ALTOTaylor & Francis Grouparticleleptospira sppleptospirosispathogenesislipl21lipl41Infectious and parasitic diseasesRC109-216ENVirulence, Vol 12, Iss 1, Pp 2798-2813 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	leptospira spp leptospirosis pathogenesis lipl21 lipl41 Infectious and parasitic diseases RC109-216
spellingShingle	leptospira spp leptospirosis pathogenesis lipl21 lipl41 Infectious and parasitic diseases RC109-216 Takahashi MB Teixeira AF Nascimento ALTO The leptospiral LipL21 and LipL41 proteins exhibit a broad spectrum of interactions with host cell components
description	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.
format	article
author	Takahashi MB Teixeira AF Nascimento ALTO
author_facet	Takahashi MB Teixeira AF Nascimento ALTO
author_sort	Takahashi MB
title	The leptospiral LipL21 and LipL41 proteins exhibit a broad spectrum of interactions with host cell components
title_short	The leptospiral LipL21 and LipL41 proteins exhibit a broad spectrum of interactions with host cell components
title_full	The leptospiral LipL21 and LipL41 proteins exhibit a broad spectrum of interactions with host cell components
title_fullStr	The leptospiral LipL21 and LipL41 proteins exhibit a broad spectrum of interactions with host cell components
title_full_unstemmed	The leptospiral LipL21 and LipL41 proteins exhibit a broad spectrum of interactions with host cell components
title_sort	leptospiral lipl21 and lipl41 proteins exhibit a broad spectrum of interactions with host cell components
publisher	Taylor & Francis Group
publishDate	2021
url	https://doaj.org/article/e69ab9b9303e4c7382e9f7090c87a695
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The leptospiral LipL21 and LipL41 proteins exhibit a broad spectrum of interactions with host cell components

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