Source:http://linkedlifedata.com/resource/pubmed/id/18048922
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 12
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pubmed:dateCreated |
2007-11-30
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pubmed:abstractText |
Sortase A (SrtA) is required for cell-wall anchoring of LPXTG-containing Gram-positive surface proteins. It was hypothesized, therefore, that disruption of the srtA gene would alter surface anchoring and functions of target LPXTG motif-bearing SspA and SspB proteins of Streptococcus gordonii. Mutant strains in srtA (V288srtA(-), DL1srtA(-)) were constructed in S. gordonii V288 (wtV288) and DL1 (wtDL1). When compared to wtV288, the V288srtA(-) mutant showed decreased biofilm formation on polystyrene, and reduced binding to immobilized purified salivary agglutinin (BIAcore analysis). The wtV288 and V288srtA(-) strains were similar in ultrastructure, but immunogold-labelled SspA/SspB surface expression was reduced on the V288srtA(-) mutant. DL1srtA(-) was also complemented to obtain DL1srtA(+). From the wild-type strains (wtV288, wtDL1), srtA(-) mutants (V288srtA(-), DL1srtA(-)), and the complemented mutant (DL1srtA(+)), cytoplasmic, cell-wall and released extracellular protein fractions were isolated. Each fraction was analysed by SDS-PAGE and immunoblotting with anti-P1. Spent medium from srtA(-) mutant cells contained over-represented proteins, including SspA/SspB (P1 antigen). Mutants showed less P1 on the cell surface than wild-types, as estimated using whole-cell ELISA, and no P1 appeared in the cytoplasmic fractions. Expression of several adhesin genes (sspA/B, cshA/B, fbpA) was generally upregulated in the mutants (V288srtA(-), DL1srtA(-)), but restored to wild-type levels in DL1srtA(+). These data therefore imply that in addition to its role in processing LPXTG-containing adhesins, sortase A has the novel function of contributing to transcriptional regulation of adhesin gene expression.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adhesins, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Agglutinins,
http://linkedlifedata.com/resource/pubmed/chemical/Aminoacyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/SspA protein, bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/salivary agglutinin receptor...,
http://linkedlifedata.com/resource/pubmed/chemical/sortase A
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1350-0872
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
153
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4088-97
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pubmed:dateRevised |
2008-3-24
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pubmed:meshHeading |
pubmed-meshheading:18048922-Adhesins, Bacterial,
pubmed-meshheading:18048922-Agglutinins,
pubmed-meshheading:18048922-Amino Acid Motifs,
pubmed-meshheading:18048922-Aminoacyltransferases,
pubmed-meshheading:18048922-Bacterial Proteins,
pubmed-meshheading:18048922-Biofilms,
pubmed-meshheading:18048922-Cysteine Endopeptidases,
pubmed-meshheading:18048922-Gene Expression Regulation, Bacterial,
pubmed-meshheading:18048922-Humans,
pubmed-meshheading:18048922-Microscopy, Electron, Scanning,
pubmed-meshheading:18048922-Microscopy, Electron, Transmission,
pubmed-meshheading:18048922-Mutation,
pubmed-meshheading:18048922-Saliva,
pubmed-meshheading:18048922-Streptococcus gordonii
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pubmed:year |
2007
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pubmed:articleTitle |
Consequences of a sortase A mutation in Streptococcus gordonii.
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pubmed:affiliation |
Department of Diagnostic and Biological Sciences, School of Dentistry, Medical School, University of Minnesota, Minneapolis, MN 55455, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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