rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
3
|
pubmed:dateCreated |
2005-9-21
|
pubmed:abstractText |
The chaperone-usher system determines the biogenesis of surface-exposed adhesive structures responsible for virulence of many Gram-negative bacteria. Investigations of the last 20 years have resolved the mechanism of this pathway on a structural level for different species of pathogenic bacteria. The purpose of this review is to present the molecular mechanisms of the biogenesis of adhesive structures assembled via the chaperone-usher pathway. The obtained mechanistic data allow one to propose potential strategies of anti-bacterial action. Additionally, the specific properties of the polymeric adhesive structures (pili and fimbriae) of the chaperone-usher system allow their use as effective and safe recombinant vaccines carrying foreign epitopes in thousands of copies on bacterial cell surface.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:issn |
0001-527X
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
52
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
639-46
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:16175239-Adhesins, Bacterial,
pubmed-meshheading:16175239-Anti-Bacterial Agents,
pubmed-meshheading:16175239-Bacterial Infections,
pubmed-meshheading:16175239-Bacterial Proteins,
pubmed-meshheading:16175239-Bacterial Vaccines,
pubmed-meshheading:16175239-Biogenesis,
pubmed-meshheading:16175239-Cell Membrane,
pubmed-meshheading:16175239-Drug Design,
pubmed-meshheading:16175239-Epitopes,
pubmed-meshheading:16175239-Fimbriae, Bacterial,
pubmed-meshheading:16175239-Fimbriae Proteins,
pubmed-meshheading:16175239-Microbial Sensitivity Tests,
pubmed-meshheading:16175239-Molecular Chaperones
|
pubmed:year |
2005
|
pubmed:articleTitle |
The chaperone-usher pathway of bacterial adhesin biogenesis -- from molecular mechanism to strategies of anti-bacterial prevention and modern vaccine design.
|
pubmed:affiliation |
Department of Microbiology, Gda?sk University of Technology, Poland.
|
pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
|