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Article

A novel glucosyltransferase is required for glycosylation of a serine-rich adhesin and biofilm formation by Streptococcus parasanguinis.

The Journal of biological chemistry - 16 Apr 2010

Zhou Meixian, Zhu Fan, Dong Shengli, Pritchard David G, Wu Hui

Abstract excerpt

Fap1-like serine-rich glycoproteins are conserved in streptococci, staphylococci, and lactobacilli, and are required for bacterial biofilm formation and pathogenesis. Glycosylation of Fap1 is mediated by a gene cluster flanking the fap1 locus. The key enzymes responsible for the first step of Fap1 glycosylation are glycosyltransferases Gtf1 and Gtf2. They form a functional enzyme complex that catalyzes the...

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Identifiers

PMID: 20164186
DOI: 10.1074/jbc.M109.066928
PMCID: PMC2852953

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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A novel glucosyltransferase is required for glycosylation of a serine-rich adhesin and biofilm formation by Streptococcus parasanguinis.PMID 20164186Read ↗

Interaction between two putative glycosyltransferases is required for glycosylation of a serine-rich streptococcal adhesin.Semantic proximity Read ↗

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