Identification of critical residues in Gap3 of <Emphasis Type="Italic">Streptococcus parasanguinis</Emphasis> involved in Fap1 glycosylation,fimbrial formation and <Emphasis Type="Italic">in vitro</Emphasis>adhesion |
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| Authors: | Zhixiang Peng Paula Fives-Taylor Teresa Ruiz Meixian Zhou Baiming Sun Qiang Chen Hui Wu |
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| Institution: | (1) Departments of Pediatric Dentistry and Microbiology, University of Alabama at Birmingham Schools of Dentistry and Medicine, 35294 Birmingham, AL, USA;(2) Department of Microbiology and Molecular Genetics, University of Vermont, 05405 Burlington, VT, USA;(3) Department of Endodontics, Guanghua College of Stomatology, Sun Yat-Sen University, 510055, Guangzhou, China;(4) Molecular Physiology and Biophysics, University of Vermont, 05405 Burlington, VT, USA |
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| Abstract: | Background
Streptococcus parasanguinis is a primary colonizer of human tooth surfaces and plays an important role in dental plaque formation. Bacterial adhesion
and biofilm formation are mediated by long peritrichous fimbriae that are composed of a 200 kDa serine rich glycoprotein named
Fap1 (fimbriae-associated protein). Glycosylation and biogenesis of Fap1 are modulated by a gene cluster downstream of the
fap1 locus. A gene encoding a glycosylation-associated protein, Gap3, was found to be important for Fap1 glycosylation, long fimbrial
formation and Fap1-mediated biofilm formation. |
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