Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2011-2-28
pubmed:abstractText
Oligocomponent pilus structures, recently discovered in many important Gram-positive pathogens, represent a new class of virulence factors with adhesive and matrix protein-binding activity. Some of these proteins have emerged as very promising lead components of protein-based vaccines against Streptococci. These extended surface structures play key roles in host cell and tissue adherence, paracellular translocation, and biofilm formation of major Gram-positive pathogens such as Streptococcus pyogenes, S. agalactiae, S. pneumoniae as well as in opportunistic and nosocomial pathogens like Enterococci. Here, we discuss the similarities and differences of: (1) the genomic organization of the various regions encoding pilus proteins, (2) the number, type, and assembly of the proteins constituting the pili, (3) their expression and regulation mechanisms, (4) their role in bacterial virulence, and (5) their potential as vaccine candidate antigens.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1618-0607
pubmed:author
pubmed:copyrightInfo
Copyright © 2010 Elsevier GmbH. All rights reserved.
pubmed:issnType
Electronic
pubmed:volume
301
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
240-51
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Genomic organization, structure, regulation and pathogenic role of pilus constituents in major pathogenic Streptococci and Enterococci.
pubmed:affiliation
Institute of Medical Microbiology, Virology and Hygiene, University of Rostock, D-18057 Rostock, Germany. Bernd.Kreikemeyer@med.uni-rostock.de
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't