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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2002-11-12
pubmed:abstractText
Group B Streptococcus (GBS) is the leading cause of bacterial chorioamnionitis and neonatal pneumonia, sepsis, and meningitis. Deletion of the alpha C protein gene (bca) attenuates the virulence of GBS in an animal model; significant survival differences in the first 24 h of infection suggest a pathogenic role for the alpha C protein early in the infection process. We examined the role of alpha C protein in the association between GBS and mucosal surfaces using a human cervical epithelial cell line, ME180. Fluorescent and confocal microscopy and flow cytometry demonstrated that 9-repeat alpha C protein binds to the surface of ME180 cells. Isolated N-terminal region of this protein also binds to these cells and competitively inhibits binding of the full protein. Wild-type GBS strain A909 and the bca-null isogenic mutant JL2053 bound similarly to the surface of ME180 cells. However, A909 entered these cells threefold more. Internalization of A909 was inhibited with 2- and 9-repeat alpha C and with N-terminal region alone but not by repeat region-specific peptide. Translocation across polarized ME180 membranes was fivefold greater for A909 than for JL2053. These findings suggest a role for the alpha C protein in interaction with epithelial surfaces and initiation of infection.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1462-5814
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
751-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
The alpha C protein mediates internalization of group B Streptococcus within human cervical epithelial cells.
pubmed:affiliation
Channing Laboratory, Boston, MA 02115, USA. gbolduc@rics.bwh.harvard.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.