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dc.contributor.authorMaddocks, Sarah
dc.contributor.authorWright, Christopher
dc.contributor.authorNobbs, Angela
dc.contributor.authorBrittan, Jane
dc.contributor.authorFranklin, Linda
dc.contributor.authorStrömberg, Nicklas
dc.contributor.authorJepson, Mark
dc.contributor.authorKadioglu, Aras
dc.contributor.authorJenkinson, Howard
dc.date.accessioned2014-02-11T16:54:54Z
dc.date.available2014-02-11T16:54:54Z
dc.date.issued2011
dc.identifier.citationMolecular Microbiology (2011) 81(4), 1034–1049en_US
dc.identifier.issn0950-382X
dc.identifier.urihttp://hdl.handle.net/10369/5314
dc.identifier.urihttp://dx.doi.org/10.1111/j.1365-2958.2011.07749.x
dc.descriptionThe definitive version is available at www3.interscience.wiley.comen_US
dc.description.abstractThe 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.en_US
dc.language.isoenen_US
dc.publisherWileyen_US
dc.relation.ispartofseriesMolecular Microbiology;
dc.titleStreptococcus pyogenes antigen I/II-family polypeptide AspA shows differential ligand-binding properties and mediates biofilm formationen_US
dc.typeArticleen_US


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