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

Bu, Su; Li, Yirong; Zhou, Mingjun; Azadin, Parastoo; Zeng, Meiqin; Fives-Taylor, Paula; Wu, Hui

doi:10.1128/jb.01078-07

Cited by 54 publications

(87 citation statements)

References 36 publications

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“…31 and 32) predicts that interface I is significantly more stable than interface II. This interface is consistent with previous mutational analysis (28,33).…”

Section: Resultssupporting

confidence: 81%

Mechanism of a cytosolic O -glycosyltransferase essential for the synthesis of a bacterial adhesion protein

Chen

Seepersaud

Bensing

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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O-glycosylation of Ser and Thr residues is an important process in all organisms, which is only poorly understood. Such modification is required for the export and function of adhesin proteins that mediate the attachment of pathogenic Gram-positive bacteria to host cells. Here, we have analyzed the mechanism by which the cytosolic O-glycosyltransferase GtfA/B of Streptococcus gordonii modifies the Ser/Thr-rich repeats of adhesin. The enzyme is a tetramer containing two molecules each of GtfA and GtfB. The two subunits have the same fold, but only GtfA contains an active site, whereas GtfB provides the primary binding site for adhesin. During a first phase of glycosylation, the conformation of GtfB is restrained by GtfA to bind substrate with unmodified Ser/Thr residues. In a slow second phase, GtfB recognizes residues that are already modified with N-acetylglucosamine, likely by converting into a relaxed conformation in which one interface with GtfA is broken. These results explain how the glycosyltransferase modifies a progressively changing substrate molecule.

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“…31 and 32) predicts that interface I is significantly more stable than interface II. This interface is consistent with previous mutational analysis (28,33).…”

Section: Resultssupporting

confidence: 81%

Mechanism of a cytosolic O -glycosyltransferase essential for the synthesis of a bacterial adhesion protein

Chen

Seepersaud

Bensing

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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show abstract

“…An 11-gene cluster has been identified and implicated in the biogenesis of Fap1 (Zhou and Wu 2009). Among them, 6 genes (gtf1, gtf2, gly, gtf3, galT1, and galT2) encode putative glycosyltransferases, which mediate the glycosylation of Fap1 (Wu, Bu, et al 2007;Wu, Zeng, et al 2007;Bu et al 2008;Zhou and Wu 2009;Wu et al 2010;Zhou et al 2010;Zhu et al 2011;Zhang et al 2013;Zhang et al 2014) (Fig. 2).…”

Section: Glycosyltransferases Important For the Glycosylation Of Srrpsmentioning

confidence: 99%

“…However, Gtf1 alone only exhibits minimal enzymatic activity, while Gtf2 alone does not have any activity . Gtf2 enhances the enzymatic activity of Gtf1 by its chaperone-like property (Bu et al 2008;Wu et al 2010). Gtf1 and Gtf2 work in concert to form a fully activated protein complex.…”

Section: Glycosyltransferases Important For the Glycosylation Of Srrpsmentioning

confidence: 99%

“…Gtf1 and Gtf2 initiate the first step of the glycosylation by transferring a GlcNAc reside to Fap1 (Wu, Bu, et al 2007;Bu et al 2008). Gtf1 is a typical glycosyltransferase that belongs to the GT-B family of GTs.…”

Section: Glycosyltransferases Important For the Glycosylation Of Srrpsmentioning

confidence: 99%

“…The glycosidic bond formation catalyzed by glycosyltransferases occurs between carbohydrate and acceptor. The acceptor is diverse, containing a variety of biomolecules such as serine-rich repeats or partially glycosylated serine-rich repeat proteins (Wu, Zeng, et al 2007;Bu et al 2008;Zhou and Wu 2009;Zhou et al 2010;Zhu et al 2011;Lizcano et al 2012), glucan matrix synthesized by cariogenic Streptococcus mutans (Lemos et al 2013), glycolipids (Ito et al 2011), and receptor polysaccharide (Xu et al 2003).…”

Section: Introductionmentioning

confidence: 99%

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Glycosyltransferase-mediated Sweet Modification in Oral Streptococci

Zhu

Zhang

2015

J Dent Res

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Bacterial glycosyltransferases play important roles in bacterial fitness and virulence. Oral streptococci have evolved diverse strategies to survive and thrive in the carbohydrate-rich oral cavity. In this review, we discuss 2 important biological processes mediated by 2 distinct groups of glycosyltransferases in oral streptococci that are important for bacterial colonization and virulence. The first process is the glycosylation of highly conserved serine-rich repeat adhesins by a series of glycosyltransferases. Using Streptococcus parasanguinis as a model, we highlight new features of several glycosyltransferases that sequentially modify the serine-rich glycoprotein Fap1. Distinct features of a novel glycosyltransferase fold from a domain of unknown function 1792 are contrasted with common properties of canonical glycosyltransferases. The second biological process we cover is involved in building sticky glucan matrix to establish cariogenic biofilms by an important opportunistic pathogen Streptococcus mutans through the action of a family of 3 glucosyltransferases. We focus on discussing the structural feature of this family as a glycoside hydrolase family of enzymes. While the 2 processes are distinct, they all produce carbohydrate-coated biomolecules, which enable bacteria to stick better in the complex oral microbiome. Understanding the making of the sweet modification presents a unique opportunity to develop novel antiadhesion and antibiofilm strategies to fight infections by oral streptococci and beyond.

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Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2007–2008

Harvey

2011

Mass Spectrometry Reviews

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This review is the fifth update of the original review, published in 1999, on the application of MALDI mass spectrometry to the analysis of carbohydrates and glycoconjugates and brings coverage of the literature to the end of 2008. The first section of the review covers fundamental studies, fragmentation of carbohydrate ions, use of derivatives and new software developments for analysis of carbohydrate spectra. Among newer areas of method development are glycan arrays, MALDI imaging and the use of ion mobility spectrometry. The second section of the review discusses applications of MALDI MS to the analysis of different types of carbohydrate. Specific compound classes that are covered include carbohydrate polymers from plants, N- and O-linked glycans from glycoproteins, biopharmaceuticals, glycated proteins, glycolipids, glycosides and various other natural products. There is a short section on the use of MALDI mass spectrometry for the study of enzymes involved in glycan processing and a section on the use of MALDI MS to monitor products of the chemical synthesis of carbohydrates with emphasis on carbohydrate-protein complexes and glycodendrimers. Corresponding analyses by electrospray ionization now appear to outnumber those performed by MALDI and the amount of literature makes a comprehensive review on this technique impractical. However, most of the work relating to sample preparation and glycan synthesis is equally relevant to electrospray and, consequently, those proposing analyses by electrospray should also find material in this review of interest.

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

Cited by 54 publications

References 36 publications

Mechanism of a cytosolic O -glycosyltransferase essential for the synthesis of a bacterial adhesion protein

Mechanism of a cytosolic O -glycosyltransferase essential for the synthesis of a bacterial adhesion protein

Glycosyltransferase-mediated Sweet Modification in Oral Streptococci

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2007–2008

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