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Article

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

Journal of bacteriology - 1 Feb 2008

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

Abstract excerpt

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 and staphylococci and have been implicated in bacterial virulence. Fap1 contains two serine-rich repeat regions that are modified by O-linked glycosylation. A seven-gene cluster has been identified, and this...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

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Identifiers

PMID: 18083807
DOI: 10.1128/JB.01078-07
PMCID: PMC2238222

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Interaction between two putative glycosyltransferases is required for glycosylation of a serine-rich streptococcal adhesin.PMID 18083807Read ↗

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