rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
9
|
pubmed:dateCreated |
1990-9-27
|
pubmed:abstractText |
Toxic shock syndrome toxin 1 (TSST-1), a 22-kilodalton protein made by strains of Staphylococcus aureus harboring the chromosomal toxin gene, may elicit toxic shock syndrome in humans. In vitro, TSST-1 induces T cells to proliferate and macrophages to secrete interleukin-1. To conduct a structure-function analysis, point mutations on the TSST-1 gene were generated by site-directed mutagenesis to identify amino acids critical for activity of the toxin. Specific tyrosine and histidine residues were replaced by alanines. Wild-type and mutant TSST-1 gene constructs were expressed in Escherichia coli, and the products were tested for their mitogenic potential and reactivity with a TSST-1 neutralizing monoclonal antibody (MAb 8-5-7). Four of the mutants were similar to the wild type; i.e., the mutant toxins stimulated murine T cells and reacted with MAb 8-5-7 equally as well as the wild type. Two mutants exhibited a decrease in mitogenic activity, but one of these retained the capacity to bind with MAb 8-5-7 while the other was no longer recognized by the same antibody. One double mutant demonstrated minimal mitogenic activity and did not react in enzyme-linked immunosorbent and immunoblot assays with MAb 8-5-7. The data show that specific residues near the carboxy terminus of TSST-1 are essential for mitogenic activity and in forming the epitope recognized by neutralizing MAb 8-5-7.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696937-2313089,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696937-2457635,
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pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Sep
|
pubmed:issn |
0019-9567
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
58
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
3020-8
|
pubmed:dateRevised |
2009-11-18
|
pubmed:meshHeading |
pubmed-meshheading:1696937-Animals,
pubmed-meshheading:1696937-Antibodies, Monoclonal,
pubmed-meshheading:1696937-Bacterial Toxins,
pubmed-meshheading:1696937-Base Sequence,
pubmed-meshheading:1696937-Binding, Competitive,
pubmed-meshheading:1696937-Blotting, Western,
pubmed-meshheading:1696937-Cloning, Molecular,
pubmed-meshheading:1696937-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1696937-Enterotoxins,
pubmed-meshheading:1696937-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:1696937-Epitopes,
pubmed-meshheading:1696937-Escherichia coli,
pubmed-meshheading:1696937-Mice,
pubmed-meshheading:1696937-Mitogens,
pubmed-meshheading:1696937-Molecular Sequence Data,
pubmed-meshheading:1696937-Mutation,
pubmed-meshheading:1696937-Neutralization Tests,
pubmed-meshheading:1696937-Spleen,
pubmed-meshheading:1696937-Superantigens
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pubmed:year |
1990
|
pubmed:articleTitle |
Mutants of staphylococcal toxic shock syndrome toxin 1: mitogenicity and recognition by a neutralizing monoclonal antibody.
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pubmed:affiliation |
Department of Molecular Genetics, Biochemistry and Microbiology, University of Cincinnati Medical Center, Ohio 45267-0524.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|