Linked Life Data

11453703

Source:http://linkedlifedata.com/resource/pubmed/id/11453703

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2001-7-16
pubmed:abstractText
CsrR/CsrS (CovR/CovS) is a two-component regulator of extracellular virulence factors in Group A streptococcus, but the full range of regulated exoproteins is unknown. Since CsrR represses expression of regulated factors, culture supernates of wild-type and CsrR(-)mutant strains were compared by two-dimensional gel electrophoresis (2DGE) to identify regulated exoproteins. Supernates of DeltacsrRS(-)mutant, but not wild-type, bacteria contained an abundant 23 kDa protein. The N-terminal sequence of this spot corresponded to a putative open reading frame (ORF) in the streptococcal genome. In a mobility shift assay, phosphorylated CsrR bound to a PCR amplicon that included sequences upstream of this ORF. By primer extension analysis, the ORF (designated mspA, for Mucoidy-associated Secreted Protein) was expressed in mid- and late-exponential phase in a DeltacsrRS(-)mutant. The presence of an in-frame deletion in mspA did not affect colony appearance, mucoidy or in vitro growth, and there was no difference between DeltamspA and wild-type strains in a mouse model of skin infection. MspA is co-regulated with other factors required for dermonecrosis (e.g. capsule, streptolysin S and purogenic exotoxin B); however, deletion of this gene does not affect expression of hyaluronic acid capsule or severity of skin infection in mice.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0882-4010
pubmed:author
pubmed:copyrightInfo
Copyright 2001 Academic Press.
pubmed:issnType
Print
pubmed:volume
31
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
81-9
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Identification of a major, CsrRS-regulated secreted protein of Group A streptococcus.
pubmed:affiliation
Department of Internal Medicine, University of Michigan School of Medicine, Ann Arbor, MI 48109, U.S.A.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.