Interaction between Two Putative Glycosyltransferases Is Required for Glycosylation of a Serine-Rich Streptococcal Adhesin

Nucleotide sugar
DOI: 10.1128/jb.01078-07 Publication Date: 2007-12-15T01:53:31Z
ABSTRACT
Fap1, a serine-rich glycoprotein, is essential for fimbrial biogenesis and biofilm formation of Streptococcus parasanguinis (formerly S. parasanguis). Fap1-like proteins are conserved in many streptococci staphylococci have been implicated bacterial virulence. Fap1 contains two repeat regions that modified by O-linked glycosylation. A seven-gene cluster has identified, this biogenesis. In study, we investigated the initial step glycosylation using recombinant as model. This molecule same monosaccharide composition profile native protein. Glycosyl linkage analyses indicated N-acetylglucosamine (GlcNAc) among first group sugar residues transferred to peptide. Two putative glycosyltransferases, Gtf1 Gtf2, were with GlcNAc-containing oligosaccharide(s) both well system Escherichia coli. Yeast two-hybrid analysis vitro vivo glutathione S-transferase pull-down assays demonstrated glycosyltransferases interacted each other. The interaction domain was mapped an N-terminal region required data study suggested Gtf2 complex initiation necessary.
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