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Streptococcus pyogenes antigen I/II-family polypeptide AspA shows differential ligand-binding properties and mediates biofilm formation

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Author
Maddocks, Sarah
Wright, Christopher
Nobbs, Angela
Brittan, Jane
Franklin, Linda
Strömberg, Nicklas
Jepson, Mark
Kadioglu, Aras
Jenkinson, Howard
Date
2011
Type
Article
Publisher
Wiley
ISSN
0950-382X
Metadata
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Abstract
The streptococcal antigen I/II (AgI/II)-family polypeptides are cell wall-anchored adhesins expressed by most indigenous oral streptococci. Proteins sharing 30–40% overall amino acid sequence similarities with AgI/II-family proteins are also expressed by Streptococcus pyogenes. The S. pyogenes M28_Spy1325 polypeptide (designated AspA) displays an AgI/II primary structure, with alanine-rich (A) and prolinerich (P) repeats flanking a V region that is projected distal from the cell. In this study it is shown that AspA from serotype M28 S. pyogenes, when expressed on surrogate host Lactococcus lactis, confers binding to immobilized salivary agglutinin gp-340. This binding was blocked by antibodies to the AspA-VP region. In contrast, the N-terminal region of AspA was deficient in binding fluid-phase gp-340, and L. lactis cells expressing AspA were not agglutinated by gp-340. Deletion of the aspA gene from two different M28 strains of S. pyogenes abrogated their abilities to form biofilms on saliva-coated surfaces. In each mutant strain, biofilm formation was restored by trans complementation of the aspA deletion. In addition, expression of AspA protein on the surface of L. lactis conferred biofilm-forming ability. Taken collectively, the results provide evidence that AspA is a biofilmassociated adhesin that may function in host colonization by S. pyogenes.
Journal/conference proceeding
Molecular Microbiology;
Citation
Molecular Microbiology (2011) 81(4), 1034–1049
URI
http://hdl.handle.net/10369/5314
http://dx.doi.org/10.1111/j.1365-2958.2011.07749.x
Description
The definitive version is available at www3.interscience.wiley.com
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  • Un-themed [116]

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