Leptospira interrogans enolase is secreted extracellularly and interacts with plasminogen

dc.creatorNogueira, Sarah Veloso
dc.creatorBackstedt, Brian T
dc.creatorSmith, Alexis A
dc.creatorQin, Jin-Hong
dc.creatorWunder Junior, Elsio Augusto
dc.creatorKo, Albert Icksang
dc.creatorPal, Utpal
dc.date2017-07-14T14:11:43Z
dc.date2017-07-14T14:11:43Z
dc.date2013
dc.date.accessioned2023-09-27T00:16:03Z
dc.date.available2023-09-27T00:16:03Z
dc.identifierNOGUEIRA, S. V. et al. Leptospira interrogans enolase is secreted extracellularly and interacts with plasminogen. PLoS One, v. 8, n. 10, p. e78150, 2013.
dc.identifier1932-6203
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/20088
dc.identifier10.1371/journal.pone.0078150
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8899123
dc.descriptionKo, Albert Icksang “Documento produzido em parceria ou por autor vinculado à Fiocruz, mas não consta à informação no documento”.
dc.descriptionNational Institutes of Health (AI080615, AI088752 and AI052473)
dc.descriptionLeptospira interrogans is the agent for leptospirosis, an important zoonosis in humans and animals across the globe. Surface proteins of invading pathogens, such as L. interrogans, are thought to be responsible for successful microbial persistence in vivo via interaction with specific host components. In particular, a number of invasive infectious agents exploit host proteolytic pathways, such as one involving plasminogen (Pg), which aid in efficient pathogen dissemination within the host. Here we show that L. interrogans serovar Lai binds host Pg and that the leptospiral gene product LA1951, annotated as enolase, is involved in this interaction. Interestingly, unlike in related pathogenic Spirochetes, such as Borrelia burgdorferi, LA1951 is not readily detectable in the L. interrogans outer membrane. We show that the antigen is indeed secreted extracellularly; however, it can reassociate with the pathogen surface, where it displays Pg-binding and measurable enzymatic activity. Hamsters infected with L. interrogans also develop readily detectable antibody responses against enolase. Taken together, our results suggest that the L. interrogans enolase has evolved to play a role in pathogen interaction with host molecules, which may contribute to the pathogenesis of leptospirosis.
dc.formatapplication/pdf
dc.languageeng
dc.publisherPublic Library of Science
dc.rightsopen access
dc.subjectLeptospira interrogans
dc.subjectProteínas
dc.subjectPlasminogenio
dc.subjectCricetinae
dc.subjectAnimais
dc.subjectLeptospira interrogans
dc.subjectBacterial Proteins
dc.subjectPlasminogen
dc.subjectCricetinae
dc.subjectAnimals
dc.titleLeptospira interrogans enolase is secreted extracellularly and interacts with plasminogen
dc.typeArticle


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