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Journal of Bacteriology, February 2007, p. 1390-1398, Vol. 189, No. 4
0021-9193/07/$08.00+0     doi:10.1128/JB.00836-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Two Gene Determinants Are Differentially Involved in the Biogenesis of Fap1 Precursors in Streptococcus parasanguis

Departments of Pediatric Dentistry and Microbiology, Schools of Dentistry and Medicine, University of Alabama at Birmingham, Birmingham, Alabama 35294,¹ Department of Microbiology and Molecular Genetics, University of Vermont, Burlington, Vermont, 05405²

Received 12 June 2006/ Accepted 13 September 2006

Mature Fap1, a 200-kDa fimbria-associated adhesin, is required for fimbrial biogenesis and biofilm formation in Streptococcus parasanguis. Fap1-like proteins are found in the genomes of many streptococcal and staphylococcal species. Fap1 is a serine-rich glycoprotein modified by O-linked glycan moieties. In this study, we identified a seven-gene cluster including secY2, orf1, orf2, orf3, secA2, gtf1, and gtf2 that is localized immediately downstream of fap1. The lower G+C contents and the presence of a putative transposase element suggest that this gene cluster was horizontally transferred from other bacteria and represents a genomic island. At least two genes in this island mediated Fap1 biogenesis. Mutation of a glucosyltransferase (Gtf1) gene led to accumulation of a Fap1 precursor, which had no detectable glycan moieties. Inactivation of a gene coding for an accessory Sec protein (SecY2) resulted in expression of a distinct Fap1 precursor, which reacted with one glycan-specific Fap1 antibody but not with another glycan-specific antibody. Furthermore, partially glycosylated Fap1 was detected on the cell surface and in the culture supernatant. These data suggest that SecY2 has a role in complete glycosylation of Fap1 and imply that SecY2 is not the only translocation channel for the Fap1 precursor and that alternative secretion machinery exists. Together, Gtf1 and SecY2 are involved in biogenesis of two distinct Fap1 precursors in S. parasanguis. Discovery of the effect of an accessory Sec protein on Fap1 glycosylation suggests that Fap1 secretion and glycosylation are coupled during Fap1 biogenesis.

Published ahead of print on 22 September 2006.

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• Bu, S., Li, Y., Zhou, M., Azadin, P., Zeng, M., Fives-Taylor, P., Wu, H. (2008). Interaction between Two Putative Glycosyltransferases Is Required for Glycosylation of a Serine-Rich Streptococcal Adhesin. J. Bacteriol. 190: 1256-1266 [Abstract] [Full Text]  
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