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

• DOI: 10.1128/jb.01078-07
• Publication Date: 2007-12-15T01:53:31Z
• Authors: Su Bu; Yirong Li; Meixian Zhou; Parastoo Azadin; Meiqin Zeng; Paula Fives-Taylor; Hui Wu
• Keywords: Nucleotide sugar

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.