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Infection and Immunity, May 2007, p. 2181-2188, Vol. 75, No. 5
0019-9567/07/$08.00+0     doi:10.1128/IAI.01544-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

The Glycan Moieties and the N-Terminal Polypeptide Backbone of a Fimbria-Associated Adhesin, Fap1, Play Distinct Roles in the Biofilm Development of Streptococcus parasanguinis

Departments of Pediatric Dentistry,¹ Microbiology, Schools of Dentistry and Medicine, University of Alabama at Birmingham, Birmingham, Alabama 35294,² Department of Microbiology and Molecular Genetics, College of Medicine and College of Agriculture and Life Sciences, University of Vermont, Burlington, Vermont 05405³

Received 25 September 2006/ Returned for modification 13 November 2006/ Accepted 4 February 2007

Fap1, a fimbria-associated glycoprotein, is essential for biofilm formation of Streptococcus parasanguinis and mediates bacterial attachment to saliva-coated hydroxylapatite, an in vitro tooth model (E. H. Froeliger and P. M. Fives-Taylor, Infect. Immun. 69:2512-2519, 2001; H. Wu and P. M. Fives-Taylor, Mol. Microbiol. 34:1070-1081, 1999; H. Wu et al., Mol. Microbiol. 28:487-500, 1998). Fap1 belongs to a growing family of high-molecular-weight serine-rich proteins found in streptococcal and staphylococcal species and possesses two serine-rich repeat regions. The glycan moiety of Fap1 appears to be O linked within the repeat regions (A. E. Stephenson et al., Mol. Microbiol. 43:147-157, 2002). In the present study, we identified a gene cluster immediately upstream of fap1 that encodes three putative glycosyltransferases and one nucleotide-sugar synthetase-like protein. Inactivation of one glycosyltransferase gene galT2 abolished the expression of two glycan epitopes; however, it did not alter bacterial ability to adhere to both SHA and saliva-conditioned biofilm surfaces. In contrast, the biofilms formed by the galT2 mutant were shallow and had a 70% decrease in biomass accumulation, suggesting that these glycan moieties mediated by GalT2 are not required for the initial adhesion but are important for biofilm formation. A recombinant N-terminal Fap1 polypeptide was shown to interact with a 53-kDa salivary protein and block and displace bacterial attachment, further demonstrating the role of the Fap1 polypeptide in bacterial adhesion. Taken together, these results suggest that Fap1 glycosylation plays an important role in bacterial biofilm formation, whereas the nonglycosylated Fap1 peptide mediates bacterial initial attachment during the process of biofilm formation.

Published ahead of print on 12 February 2007.

Editor: A. Camilli

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