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(The FASEB Journal. 2008;22:320.11)
© 2008 FASEB
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(The FASEB Journal. 2008;22:320.11.)
© 2008 FASEB

320.11

Specificity of epithelial cell adhesion by Group A Streptococcus pilus proteins in the M1 serotype SF370 strain

Emily Louise Abbot1, Wendy D. Smith1, Jonathan A. Pointon1, Carlos Chiriboga1, Janet A. Wilson2, Barry H. Hirst1 and Michael A. Kehoe1

1 Institute for Cell and Molecular Biosciences
2 School of Surgical and Reproductive Sciences, University of Newcastle upon Tyne, Newcastle upon Tyne, United Kingdom

ABSTRACT

Group A Streptococcus (GAS) express long polymeric pili which are encoded in the hypervarible FCT-region. In the serotype M1 strain SF370 these pili are composed of a major subunit (Spy128) and two ancillary proteins (Spy130 and Spy125). Deletion mutants of each of the individual subunit genes failed to adhere to human tonsil epithelium or human keratinocytes (HaCATs), suggesting that pili are essential in promoting the initial stages of GAS infection. However, which of the subunits is functioning as the primary adhesin in this pilus-dependent interaction remains undetermined. Each of the three pilus subunits were expressed as a recombinant protein and their ability to interact with various epithelial models was examined by immunofluorescence using subunit specific antisera. Both r130 and r125 proteins adhered to the surface of tonsil epithelium and HaCAT cells, however r128 failed to bind to either model. The ability of subunit-specific antisera to reduce parent strain (WT) bacterial adherence to human tonsil or HaCAT cells was examined. Incubation of WT GAS with anti-Spy125 sera inhibited the ability of GAS to adhere to either cell model. In contrast, anti-Spy 128 and anti-Spy 130 sera had no affect on bacterial binding. These results suggest that although both Spy130 and Spy125 proteins have the ability to bind host cells, pilus adhesion specificity resides in the Spy125 subunit.

Sponsored by MRC.





This Article
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Right arrow Articles by Kehoe, M. A.