The C-terminal variable domain of LigB fromLeptospiramediates binding to fibronectin

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The C-terminal variable domain of LigB from Leptospira mediates binding to fibronectin

Adhesion through microbial surface components that recognize adhesive matrix molecules is an essential step in infection for most pathogenic bacteria. In this study, we report that LigB interacts with fibronectin (Fn) through its variable region. A possible role for LigB in bacterial attachment to host cells during the course of infection is supported by the following observations: (i) binding ...

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Leptospira spp. are pathogenic spirochetes that cause the zoonotic disease leptospirosis. Leptospiral immunoglobulin (Ig)-like protein B (LigB) contributes to the binding of Leptospira to extracellular matrix proteins such as fibronectin, fibrinogen, laminin, elastin, tropoelastin and collagen. A high-affinity Fn-binding region of LigB has been localized to LigBCen2, which contains the partial ...

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ژورنال

عنوان ژورنال: Journal of Veterinary Science

سال: 2008

ISSN: 1229-845X

DOI: 10.4142/jvs.2008.9.2.133