Please use this identifier to cite or link to this item: https://www.arca.fiocruz.br/handle/icict/7561
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dc.contributor.authorMatsunaga, James
dc.contributor.authorBarocchi, Michele A
dc.contributor.authorCroda, Julio Henrique Rosa
dc.contributor.authorYoung, Tracy A
dc.contributor.authorSanchez, Yolanda
dc.contributor.authorSiqueira, Isadora Cristina de
dc.contributor.authorBolin, Carole A
dc.contributor.authorReis, Mitermayer Galvão dos
dc.contributor.authorRiley, Lee Woodland
dc.contributor.authorHaake, David A
dc.contributor.authorKo, Albert Icksang
dc.date.accessioned2014-04-30T17:19:56Z
dc.date.available2014-04-30T17:19:56Z
dc.date.issued2003
dc.identifier.citationMATSUNAGA, J. et al. Pathogenic Leptospira species express surface-exposed proteins belonging to the bacterial immunoglobulin superfamily. Molecular Microbiology, v. 49, n. 4, p. 929-945, 2003.
dc.identifier.issn0950-382X
dc.identifier.urihttps://www.arca.fiocruz.br/handle/icict/7561
dc.language.isoeng
dc.publisherNational Institute of Health
dc.rightsopen access
dc.titlePathogenic Leptospira species express surface-exposed proteins belonging to the bacterial immunoglobulin superfamily
dc.typeArticle
dc.description.abstractenProteins with bacterial immunoglobulin-like (Big) domains, such as the Yersinia pseudotuberculosis invasin and Escherichia coli intimin, are surface-expressed proteins that mediate host mammalian cell invasion or attachment. Here, we report the identification and characterization of a new family of Big domain proteins, referred to as Lig (leptospiral Ig-like) proteins, in pathogenic Leptospira. Screening of L. interrogans and L. kirschneri expression libraries with sera from leptospirosis patients identified 13 lambda phage clones that encode tandem repeats of the 90 amino acid Big domain. Two lig genes, designated ligA and ligB, and one pseudogene, ligC, were identified. The ligA and ligB genes encode amino-terminal lipoprotein signal peptides followed by 10 or 11 Big domain repeats and, in the case of ligB, a unique carboxy-terminal non-repeat domain. The organization of ligC is similar to that of ligB but contains mutations that disrupt the reading frame. The lig sequences are present in pathogenic but not saprophytic Leptospira species. LigA and LigB are expressed by a variety of virulent leptospiral strains. Loss of Lig protein and RNA transcript expression is correlated with the observed loss of virulence during culture attenuation of pathogenic strains. High-pressure freeze substitution followed by immunocytochemical electron microscopy confirmed that the Lig proteins were localized to the bacterial surface. Immunoblot studies with patient sera found that the Lig proteins are a major antigen recognized during the acute host infection. These observations demonstrate that the Lig proteins are a newly identified surface protein of pathogenic Leptospira, which by analogy to other bacterial immunoglobulin superfamily virulence factors, may play a role in host cell attachment and invasion during leptospiral pathogenesis.
dc.creator.affilliationVeterans Affairs Greater Los Angeles Healthcare System. Los Angeles, CA, USA / Department of Medicine. UCLA School of Medicine. Los Angeles, CA, USA.
dc.creator.affilliationDivision of Infectious Diseases and Immunity. School of Public Health. University of California. Berkeley Berkeley, CA, USA.
dc.creator.affilliationFundação Oswaldo Cruz. Centro de Pesquisa Gonçalo Moniz. Salvador, BA, Brasil.
dc.creator.affilliationVeterans Affairs Greater Los Angeles Healthcare System. Los Angeles, CA, USA.
dc.creator.affilliationVeterans Affairs Greater Los Angeles Healthcare System. Los Angeles, CA, USA / Department of Medicine. UCLA School of Medicine. Los Angeles, CA, USA.
dc.creator.affilliationFundação Oswaldo Cruz. Centro de Pesquisa Gonçalo Moniz. Salvador, BA, Brasil.
dc.creator.affilliationCollege of Veterinary Medicine. Michigan State University. East Lansing, MI, USA.
dc.creator.affilliationFundação Oswaldo Cruz. Centro de Pesquisa Gonçalo Moniz. Salvador, BA, Brasil.
dc.creator.affilliationDivision of Infectious Diseases and Immunity. School of Public Health. University of California. Berkeley Berkeley, CA, USA.
dc.creator.affilliationVeterans Affairs Greater Los Angeles Healthcare System. Los Angeles, CA, USA / Department of Medicine. UCLA School of Medicine. Los Angeles, CA, USA.
dc.creator.affilliationFundação Oswaldo Cruz. Centro de Pesquisa Gonçalo Moniz. Salvador, BA, Brasil / Division of International Medicine and Infectious Diseases. Weill Medical College of Cornell University. New York, NY, USA.
dc.subject.decsAnticorpos Antibacterianos/genética
dc.subject.decsProteínas de Bactérias/metabolismo
dc.subject.decsLeptospira/genética
dc.subject.decsLeptospira/metabolismo
dc.subject.decsProteínas de Membrana/metabolismo
dc.subject.decsSequência de Aminoácidos
dc.subject.decsAnimais
dc.subject.decsAnticorpos Antibacterianos/química
dc.subject.decsProteínas de Bactérias/química
dc.subject.decsRegulação Bacteriana da Expressão Gênica
dc.subject.decsHumanos
dc.subject.decsImunoglobulinas/genética
dc.subject.decsLeptospira/imunologia
dc.subject.decsProteínas de Membrana/química
dc.subject.decsModelos Moleculares
dc.subject.decsDados de Sequência Molecular
dc.subject.decsEstrutura Terciária de Proteína
Appears in Collections:BA - IGM - Artigos de Periódicos

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