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Journal of Bacteriology, November 2007, p. 7610-7617, Vol. 189, No. 21
0021-9193/07/$08.00+0     doi:10.1128/JB.00748-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Differential Roles of Individual Domains in Selection of Secretion Route of a Streptococcus parasanguinis Serine-Rich Adhesin, Fap1{triangledown}

Qiang Chen,1,{dagger} Baiming Sun,1 Hui Wu,2 Zhixiang Peng,1,3 and Paula M. Fives-Taylor1*

Department of Microbiology and Molecular Genetics, University of Vermont, Burlington, Vermont 05405,1 Departments of Pediatric Dentistry and Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294,2 Center of Stomatology, Tongji Hospital, Tongji Medical Collage, Huazhong University of Science and Technology, Wuhan 430030, China3

Received 11 May 2007/ Accepted 21 August 2007

Fimbria-associated protein 1 (Fap1) is a high-molecular-mass glycosylated surface adhesin required for fimbria biogenesis and biofilm formation in Streptococcus parasanguinis. The secretion of mature Fap1 is dependent on the presence of SecA2, a protein with some homology to, but with a different role from, SecA. The signals that direct the secretion of Fap1 to the SecA2-dependent secretion pathway rather than the SecA-dependent secretion pathway have not yet been identified. In this study, Fap1 variants containing different domains were expressed in both secA2 wild-type and mutant backgrounds and were tested for their ability to be secreted by the SecA- or SecA2-dependent pathway. The presence or absence of the cell wall anchor domain (residues 2531 to 2570) at the C terminus did not alter the selection of the Fap1 secretion route. The Fap1 signal peptide (residues 1 to 68) was sufficient to support the secretion of a heterologous protein via the SecA-dependent pathway, suggesting that the signal peptide was sufficient for recognition by the SecA-dependent pathway. The minimal sequences of Fap1 required for the SecA2-dependent pathway included the N-terminal signal peptide, nonrepetitive region I (residues 69 to 102), and part of nonrepetitive region II (residues 169 to 342). The two serine-rich repeat regions (residues 103 to 168 and 505 to 2530) were not required for Fap1 secretion. However, they were both involved in the specific inhibition of Fap1 secretion via the SecA-dependent pathway.

* Corresponding author. Mailing address: Department of Microbiology and Molecular Genetics, College of Medicine and College of Agriculture and Life Sciences, 116 Stafford Hall, 95 Carrigan Dr., University of Vermont, Burlington, VT 05405. Phone: (802) 656-1121. Fax: (802) 656-8749. E-mail: pfivesta{at}uvm.edu

{triangledown} Published ahead of print on 31 August 2007.

{dagger} Present address: Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, 55 Lake Ave., North, Worcester, MA 01655.

Journal of Bacteriology, November 2007, p. 7610-7617, Vol. 189, No. 21
0021-9193/07/$08.00+0     doi:10.1128/JB.00748-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Turner, L. S., Kanamoto, T., Unoki, T., Munro, C. L., Wu, H., Kitten, T. (2009). Comprehensive Evaluation of Streptococcus sanguinis Cell Wall-Anchored Proteins in Early Infective Endocarditis. Infect. Immun. 77: 4966-4975 [Abstract] [Full Text]  
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  • Zhou, M., Wu, H. (2009). Glycosylation and biogenesis of a family of serine-rich bacterial adhesins. Microbiology 155: 317-327 [Abstract] [Full Text]  
  • Zhou, M., Peng, Z., Fives-Taylor, P., Wu, H. (2008). A Conserved C-Terminal 13-Amino-Acid Motif of Gap1 Is Required for Gap1 Function and Necessary for the Biogenesis of a Serine-Rich Glycoprotein of Streptococcus parasanguinis. Infect. Immun. 76: 5624-5631 [Abstract] [Full Text]  


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