Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
1987-6-19
pubmed:abstractText
Attachment of bacteria to the host tissue is considered a first step in the development of many infections. Previous studies have shown that fibronectin, a protein shown to mediate substrate adhesion of eukaryotic cells, also binds to some pathogenic bacteria and mediates the tissue adherence of these prokaryotes. In the present communication, we report on the isolation and characterization of a fibronectin receptor from Staphylococcus aureus strain Newman. A 210-kDa fibronectin binding protein was isolated from a bacterial lysate by affinity chromatography followed by gel chromatography. Additional smaller peptides with fibronectin binding properties were also obtained. These peptides seem to represent degradation products of the large receptor protein since the former dominated when the purification was carried out in the absence of protease inhibitors. Furthermore, degradation of the purified receptor protein by staphylococcal V8 protease generated a large number of peptides that retained fibronectin binding activity. This observation also suggests that the large receptor protein contains several binding sites for fibronectin, and analysis of the binding of the 29-kDa amino-terminal fibronectin fragment to the 210-kDa receptor adsorbed in microtiter wells suggests that one receptor molecule can bind six to nine fibronectin molecules.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
262
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6564-71
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Isolation and characterization of a fibronectin receptor from Staphylococcus aureus.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't