Lsa21, a novel leptospiral protein binding adhesive matrix molecules and present during human infection

It has been well documented over past decades that interaction of pathogens with the extracellular matrix (ECM) plays a primary role in host cell attachment and invasion. Adherence to host tissues is mediated by surface-exposed proteins expressed by the microorganisms during infection. The mechanism...

Full description

Saved in:

Bibliographic Details
Published in:	BMC microbiology Vol. 8; no. 1; p. 70
Main Authors:	Atzingen, Marina V, Barbosa, Angela S, De Brito, Thales, Vasconcellos, Silvio A, de Morais, Zenáide M, Lima, Dirce Mc, Abreu, Patricia Ae, Nascimento, Ana Lto
Format:	Journal Article
Language:	English
Published:	England BioMed Central Ltd 29-04-2008 BioMed Central BMC
Subjects:	Adhesins, Bacterial - metabolism Adult Aged Causes of Circular Dichroism Cloning, Molecular Diagnosis Extracellular matrix Extracellular Matrix Proteins - metabolism Female Gene expression Gene Expression Regulation, Bacterial Genetic aspects Humans Laminin - metabolism Leptospira - genetics Leptospira interrogans - classification Leptospira interrogans - genetics Leptospira interrogans - metabolism Leptospirosis Leptospirosis - genetics Leptospirosis - metabolism Male Oxidation-Reduction Phylogeny Physiological aspects Protein Binding Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism RNA, Bacterial - genetics RNA, Bacterial - metabolism Transcription, Genetic Brazil
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

Description
Summary:	It has been well documented over past decades that interaction of pathogens with the extracellular matrix (ECM) plays a primary role in host cell attachment and invasion. Adherence to host tissues is mediated by surface-exposed proteins expressed by the microorganisms during infection. The mechanisms by which pathogenic leptospires invade and colonize the host remain poorly understood since few virulence factors contributing to the pathogenesis of the disease have been identified. Whole-genome sequencing analysis of L. interrogans allowed identification of a repertoire of putative leptospiral surface proteins. Here, we report the identification and characterization of a new leptospiral protein that exhibits extracellular matrix-binding properties, called as Lsa21 (leptospiral surface adhesin, 21 kDa). Compatible with its role in adhesion, the protein was shown to be surface-exposed by indirect immunofluorescence. Attachment of Lsa21 to laminin, collagen IV, and plasma fibronectin was specific and dose dependent. Laminin oxidation by sodium metaperiodate reduced the protein-laminin interaction in a concentration-dependent manner, indicating that laminin sugar moieties are crucial for this interaction. The gene coding for Lsa21 is present in pathogenic strains belonging to the L. interrogans species but was not found in the saprophytic L. biflexa serovar Patoc strain Patoc 1. Loss of gene expression occurs upon culture attenuation of pathogenic strains. Environmental factors such as osmolarity and temperature affect Lsa21 expression at the transcriptional level. Moreover, anti-Lsa21 serum labeled liver and kidney tissues of human fatal cases of leptospirosis. Our data suggest a role of Lsa21 in the pathogenesis of leptospirosis.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1471-2180 1471-2180
DOI:	10.1186/1471-2180-8-70