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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1995-2-3
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pubmed:abstractText |
In this report we have analyzed the binding of collagen to Streptococcus pyogenes strain 6414. This binding was rapid, specific, and involved a limited number of receptor molecules (11,600 copies per cell). When the proteins in a streptococcal lysate were blotted onto a nitrocellulose filter and probed with 125I-labeled collagen, a prominent collagen-binding protein of 57 kDa was identified as well as minor 130-150-kDa components. The major 57-kDa protein was isolated by affinity chromatography on collagen-Sepharose followed by gel filtration chromatography. The 57-kDa protein purified from S. pyogenes was used to raise a monospecific antibody which also reacted with a collagen-binding protein of similar molecular size isolated from Streptococcus zooepidemicus. The two collagen-binding proteins from streptococci have a similar amino acid composition and isoelectric points. Isolated collagen-binding protein was specifically recognized by 125I-collagen in a solid-phase binding assay and displayed an affinity for the ligand quite similar to that exhibited by intact bacteria (Kd = 3.1 versus 3.5 x 10(-9) M, respectively). Surface-labeled bacteria attached to microtiter wells coated with different collagen types and the 57-kDa protein blocked the adhesion to collagen substrate. We propose that the 57-kDa protein is an adhesin involved in the attachment of streptococci to host tissues.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
347-53
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7814395-Amino Acid Sequence,
pubmed-meshheading:7814395-Animals,
pubmed-meshheading:7814395-Carrier Proteins,
pubmed-meshheading:7814395-Cattle,
pubmed-meshheading:7814395-Chromatography, Affinity,
pubmed-meshheading:7814395-Chromatography, Gel,
pubmed-meshheading:7814395-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:7814395-Integrins,
pubmed-meshheading:7814395-Mice,
pubmed-meshheading:7814395-Mice, Inbred BALB C,
pubmed-meshheading:7814395-Molecular Sequence Data,
pubmed-meshheading:7814395-Protein Binding,
pubmed-meshheading:7814395-Receptors, Collagen,
pubmed-meshheading:7814395-Streptococcus equi,
pubmed-meshheading:7814395-Streptococcus pyogenes
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pubmed:year |
1995
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pubmed:articleTitle |
Isolation and characterization of a novel collagen-binding protein from Streptococcus pyogenes strain 6414.
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pubmed:affiliation |
Department of Biochemistry, University of Pavia, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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