Isopeptide bond in collagen- and fibrinogen-binding MSCRAMMs
نویسندگان
چکیده
منابع مشابه
A family of fibrinogen-binding MSCRAMMs from Enterococcus faecalis.
We report that three (EF0089, EF2505 and EF1896, renamed here Fss1, Fss2 and Fss3, respectively, for Enterococcus faecalis surface protein) of the recently predicted MSCRAMMs (microbial surface components recognizing adhesive matrix molecules) in E. faecalis strain V583 bind fibrinogen (Fg). Despite an absence of extensive primary sequence homology, the three proteins appear to be related struc...
متن کاملIdentification and biochemical characterization of two novel collagen binding MSCRAMMs of Bacillus anthracis.
Cell wall-anchored proteins play critical roles in the pathogenesis of infections caused by Gram-positive bacteria. Through the analysis of the genome of Bacillus anthracis Ames strain, we identified two novel putative cell wall-anchored proteins, BA0871 and BA5258, which have sequence homology to CNA, a cell wall-anchored collagen adhesin of Staphylococcus aureus. The two proteins have similar...
متن کاملCalcium-dependent proteolysis and isopeptide bond formation: Calpains and transglutaminases
The mechanisms of action and physiological functions of two calcium-activated enzyme families, the calpains and transglutaminases, are discussed: 1. Both enzymes work via a covalent acylenzyme intermediate. Calpains, as other papain-like proteases, have a Cys and His residue in the active site, which in the ground state tend to form a thiolate-imidazolium ion pair. In the active site of tranglu...
متن کاملA Novel Fibronectin Binding Motif in MSCRAMMs Targets F3 Modules
BACKGROUND BBK32 is a surface expressed lipoprotein and fibronectin (Fn)-binding microbial surface component recognizing adhesive matrix molecule (MSCRAMM) of Borrelia burgdorferi, the causative agent of Lyme disease. Previous studies from our group showed that BBK32 is a virulence factor in experimental Lyme disease and located the Fn-binding region to residues 21-205 of the lipoprotein. MET...
متن کاملMolecular Characterization of the Interaction of Staphylococcal Mscramms Clfa and Fbl with Fibrinogen
The ligand binding domain of the fibrinogen binding protein from Staphylococcus lugdunensis (Fbl) shares 60% sequence identity with clumping factor A (ClfA) of Staphylococcus aureus. Recombinant Fbl corresponding to the minimum fibrinogen-binding region (subdomains N2N3) was compared to ClfA for binding to fibrinogen. Fbl and ClfA had very similar affinities for fibrinogen by surface plasmon re...
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ژورنال
عنوان ژورنال: Biophysical Reviews
سال: 2016
ISSN: 1867-2450,1867-2469
DOI: 10.1007/s12551-015-0191-5