A domain of the Leptospira LigB contributes to high affinity binding of fibronectin.

A domain of the Leptospira LigB contributes to high affinity binding of fibronectin. Research Abstract Details 

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A domain of the Leptospira LigB contributes to high affinity binding of fibronectin. Abstract Text:

Yi-Pin Lin,Yung-Fu Chang,

Adhesion of pathogenic Leptospira spp. to mammalian cells is mediated by their adhesins interacting with host cell receptors. In a previous study, we have identified two potential fibronectin (Fn) binding sites in central variable region (LigBCen) and C-terminal variable region (LigBCtv) of LigB, an adhesin of pathogenic Leptospira spp. In this study, we have further localized the Fn-binding site on LigBCen and found a domain of LigB (LigBCen2) (amino acids 1014-1165) strongly bound to Fn. LigBCen2 bound to a 70kDa domain of Fn including N-terminal domain (NTD) and gelatin binding domain (GBD), but with a higher binding affinity to NTD (K(d)=272nM) than to GBD (K(d)=1200nM). Except Fn, LigBCen2 also bound laminin and fibrinogen. LigBCen2 could bind MDCK cells, and blocked the binding of Leptospira on MDCK cells by 45%. These results suggest that LigBCen2 contributed to high affinity binding on NTD or GBD of Fn, laminin, and fibrinogen and mediated Leptospira binding on host cells.

A domain of the Leptospira LigB contributes to high affinity binding of fibronectin. Publishing Authors By Initials

YP Lin,YF Chang,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: protein binding research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: protein binding research

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A domain of the Leptospira LigB contributes to high affinity binding of fibronectin. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Biochemical and biophysical research communication

VOLUME: 362

Page Numbers: 443-8

Journal Abbreviation: Biochem. Biophys. Res. Commun.

ISSN: 0006-291X

DAY: 13

MONTH: 08

YEAR: 2007

A domain of the Leptospira LigB contributes to high affinity binding of fibronectin. Information

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LANGUAGE: eng

NlmUniqueID: 372516

A domain of the Leptospira LigB contributes to high affinity binding of fibronectin. Keywords Mesh Terms:

KEYWORDS: Protein Binding

MESH TERMS: metabolism

Chemical & Substance for Abstract: A domain of the Leptospira LigB contributes to high affinity binding of fibronectin. Information

Substance Name: Gelatin

Registry Number: 9000-70-8

Grant and Affiliation Information for A domain of the Leptospira LigB contributes to high affinity binding of fibronectin.

AFFILIATION: Department of Population Medicine and Diagnostic Sciences, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA.

Country: United States

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MEDLINETA: Biochem Biophys Res Commun

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