Linked Life Data

10619844

Source:http://linkedlifedata.com/resource/pubmed/id/10619844

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2000-2-23
pubmed:abstractText
Surface expression of the group 1 K30 capsular polysaccharide of Escherichia coli strain E69 (O9a:K30) requires Wza(K30), a member of the outer membrane auxiliary (OMA) protein family. A mutation in wza(K30) severely restricts the formation of the K30 capsular structure on the cell surface, but does not interfere with the biosynthesis or polymerization of the K30 repeat unit. Here we show that Wza(K30) is a surface-exposed outer membrane lipoprotein. Wza(K30) multimers form ring-like structures in the outer membrane that are reminiscent of the secretins of type II and III protein translocation systems. We propose that Wza(K30) forms an outer membrane pore through which the K30-capsular antigen is translocated. This is the first evidence of a potential mechanism for translocation of high molecular weight polysaccharide across the outer membrane. The broad distribution of the OMA protein family suggests a similar process for polysaccharide export in diverse Gram-negative bacteria.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0261-4189
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
57-66
pubmed:dateRevised
2008-11-20
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Translocation of group 1 capsular polysaccharide to the surface of Escherichia coli requires a multimeric complex in the outer membrane.
pubmed:affiliation
Department of Microbiology, University of Guelph, Guelph, Ontario, Canada N1G 2W1.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't