Document Detail

Chaperone-usher pathways: diversity and pilus assembly mechanism.
MedLine Citation:
PMID:  22411982     Owner:  NLM     Status:  MEDLINE    
Up to eight different types of secretion systems, and several more subtypes, have been described in Gram-negative bacteria. Here, we focus on the diversity and assembly mechanism of one of the best-studied secretion systems, the widespread chaperone-usher pathway known to assemble and secrete adhesive surface structures, called pili or fimbriae, which play essential roles in targeting bacterial pathogens to the host.
Andreas Busch; Gabriel Waksman
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review    
Journal Detail:
Title:  Philosophical transactions of the Royal Society of London. Series B, Biological sciences     Volume:  367     ISSN:  1471-2970     ISO Abbreviation:  Philos. Trans. R. Soc. Lond., B, Biol. Sci.     Publication Date:  2012 Apr 
Date Detail:
Created Date:  2012-03-13     Completed Date:  2012-06-26     Revised Date:  2014-02-20    
Medline Journal Info:
Nlm Unique ID:  7503623     Medline TA:  Philos Trans R Soc Lond B Biol Sci     Country:  England    
Other Details:
Languages:  eng     Pagination:  1112-22     Citation Subset:  IM    
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MeSH Terms
Adhesins, Escherichia coli / chemistry
Bacterial Secretion Systems*
Fimbriae Proteins / chemistry
Fimbriae, Bacterial / chemistry*,  genetics,  physiology
Genetic Complementation Test
Genetic Variation
Gram-Negative Bacteria / chemistry,  genetics,  physiology*
Host-Pathogen Interactions
Molecular Chaperones / chemistry*,  classification
Multigene Family
Multiprotein Complexes / chemistry
Protein Structure, Tertiary
Receptors, Immunologic / chemistry
Grant Support
082227//Wellcome Trust; G0800002//Medical Research Council
Reg. No./Substance:
0/Adhesins, Escherichia coli; 0/Molecular Chaperones; 0/Multiprotein Complexes; 0/Receptors, Immunologic; 0/bacterial adhesin receptor; 0/fimD protein, bacteria; 0/fimH protein, E coli; 147680-16-8/Fimbriae Proteins

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