Source:http://linkedlifedata.com/resource/pubmed/id/12622825
Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6
|
| pubmed:dateCreated |
2003-3-7
|
| pubmed:databankReference | |
| pubmed:abstractText |
A collagen-binding adhesin of Enterococcus faecium, Acm, was identified. Acm shows 62% similarity to the Staphylococcus aureus collagen adhesin Cna over the entire protein and is more similar to Cna (60% and 75% similarity with Cna A and B domains respectively) than to the Enterococcus faecalis collagen-binding adhesin, Ace, which shares homology with Acm only in the A domain. Despite the detection of acm in 32 out of 32 E. faecium isolates, only 11 of these (all clinical isolates, including four vancomycin-resistant endocarditis isolates and seven other isolates) exhibited binding to collagen type I (CI). Although acm from three CI-binding vancomycin-resistant E. faecium clinical isolates showed 100% identity, analysis of acm genes and their promoter regions from six non-CI-binding strains identified deletions or mutations that introduced stop codons and/or IS elements within the gene or the promoter region in five out of six strains, suggesting that the presence of an intact functional acm gene is necessary for binding of E. faecium strains to CI. Recombinant Acm A domain showed specific and concentration-dependent binding to collagen, and this protein competed with E. faecium binding to immobilized CI. Consistent with the adherence phenotype and sequence data, probing with Acm-specific IgGs purified from anti-recombinant Acm A polyclonal rabbit serum confirmed the surface expression of Acm in three out of three collagen-binding clinical isolates of E. faecium tested, but in none of the strains with a non-functional pseudo acm gene. Introduction of a functional acm gene into two non-CI-binding natural acm mutant strains conferred a CI-binding phenotype, further confirming that native Acm is sufficient for the binding of E. faecium to CI. These results demonstrate that acm, which encodes a potential virulence factor, is functional only in certain infection-derived clinical isolates of E. faecium, and suggest that Acm is the primary adhesin responsible for the ability of E. faecium to bind collagen.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Mar
|
| pubmed:issn |
0950-382X
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
47
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1733-47
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:12622825-Adhesins, Bacterial,
pubmed-meshheading:12622825-Amino Acid Sequence,
pubmed-meshheading:12622825-Animals,
pubmed-meshheading:12622825-Bacterial Adhesion,
pubmed-meshheading:12622825-Cell Membrane,
pubmed-meshheading:12622825-Collagen,
pubmed-meshheading:12622825-Collagen Type I,
pubmed-meshheading:12622825-Enterococcus faecium,
pubmed-meshheading:12622825-Genetic Complementation Test,
pubmed-meshheading:12622825-Gram-Positive Bacteria,
pubmed-meshheading:12622825-Humans,
pubmed-meshheading:12622825-Molecular Sequence Data,
pubmed-meshheading:12622825-Mutation,
pubmed-meshheading:12622825-Protein Structure, Tertiary,
pubmed-meshheading:12622825-Pseudogenes,
pubmed-meshheading:12622825-Rabbits,
pubmed-meshheading:12622825-Recombinant Proteins,
pubmed-meshheading:12622825-Sequence Homology, Amino Acid,
pubmed-meshheading:12622825-Species Specificity
|
| pubmed:year |
2003
|
| pubmed:articleTitle |
Clinical isolates of Enterococcus faecium exhibit strain-specific collagen binding mediated by Acm, a new member of the MSCRAMM family.
|
| pubmed:affiliation |
Division of Infectious Diseases, Department of Internal Medicine and Center for the Study of Emerging and Re-emerging Pathogens, University of Texas Medical School at Houston, 6431 Fannin Street, Houston, TX 77030, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|