Streptococcus pyogenes antigen I/II-family polypeptide AspA shows differential ligand-binding properties and mediates biofilm formation
Author
Maddocks, Sarah
Wright, Christopher
Nobbs, Angela
Brittan, Jane
Franklin, Linda
Strömberg, Nicklas
Jepson, Mark
Kadioglu, Aras
Jenkinson, Howard
Date
2011Type
Article
Publisher
Wiley
ISSN
0950-382X
Metadata
Show full item recordAbstract
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
Description
The definitive version is available at www3.interscience.wiley.com
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