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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
13
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pubmed:dateCreated |
1992-8-14
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pubmed:abstractText |
Binding to fibronectin has been suggested to play an important role in adherence of the group A streptococcus Streptococcus pyrogenes to host epithelial cells; however, the identity of the streptococcal fibronectin receptor has been elusive. Here we demonstrate that the fibronectin-binding property of S. pyogenes is mediated by protein F, a bacterial surface protein that binds fibronectin at high affinity. The gene encoding protein F (prtF) produced a functional fibronectin-binding protein in Escherichia coli. Insertional mutagenesis of the cloned gene generated a mutation that resulted in the loss of fibronectin-binding activity. When this mutation was introduced into the S. pyrogenes chromosome by homologous recombination with the wild-type allele, the resulting strains no longer produced protein F and lost their ability to bind fibronectin. The mutation could be complemented by prtF introduced on a plasmid. Mutants lacking protein F had a much lower capacity to adhere to respiratory epithelial cells. These results demonstrate that protein F is an important adhesin of S. pyogenes.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-1252248,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-14097352,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-1658571,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-1834912,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-1849511,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-1965958,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-2019444,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-2188957,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-2201955,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-2497953,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-2521391,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-2522418,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-2533933,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-2553613,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-2649795,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-2670192,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-2822388,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-2972252,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-3326132,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-3327753,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-3519458,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-3534131,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-4284300,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-4610991,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-46620,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-4896022,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-4905440,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-6299959,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-6319358,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-6337097,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-6368734,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-6411621,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-6772544,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-7014727,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-7035430,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-732875,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-7403857,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385871-783118
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
89
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6172-6
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pubmed:dateRevised |
2010-9-7
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pubmed:meshHeading |
pubmed-meshheading:1385871-Animals,
pubmed-meshheading:1385871-Bacterial Adhesion,
pubmed-meshheading:1385871-Cells, Cultured,
pubmed-meshheading:1385871-Cricetinae,
pubmed-meshheading:1385871-Epithelium,
pubmed-meshheading:1385871-Fibronectins,
pubmed-meshheading:1385871-Genes, Bacterial,
pubmed-meshheading:1385871-Receptors, Fibronectin,
pubmed-meshheading:1385871-Receptors, Immunologic,
pubmed-meshheading:1385871-Respiratory System,
pubmed-meshheading:1385871-Restriction Mapping,
pubmed-meshheading:1385871-Streptococcus pyogenes
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pubmed:year |
1992
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pubmed:articleTitle |
Protein F, a fibronectin-binding protein, is an adhesin of the group A streptococcus Streptococcus pyogenes.
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pubmed:affiliation |
Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, MO 63110-1093.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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