Source:http://linkedlifedata.com/resource/pubmed/id/12427097
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
2002-11-12
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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.
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pubmed:grant |
http://linkedlifedata.com/resource/pubmed/grant/AI01388,
http://linkedlifedata.com/resource/pubmed/grant/AI07061,
http://linkedlifedata.com/resource/pubmed/grant/AI38424,
http://linkedlifedata.com/resource/pubmed/grant/AI75326,
http://linkedlifedata.com/resource/pubmed/grant/T32AI07061,
http://linkedlifedata.com/resource/pubmed/grant/T32HD07466
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1462-5814
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
751-8
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:12427097-Animals,
pubmed-meshheading:12427097-Antigens, Surface,
pubmed-meshheading:12427097-Bacterial Proteins,
pubmed-meshheading:12427097-Biological Transport,
pubmed-meshheading:12427097-Cell Line,
pubmed-meshheading:12427097-Cell Polarity,
pubmed-meshheading:12427097-Cervix Uteri,
pubmed-meshheading:12427097-Epithelial Cells,
pubmed-meshheading:12427097-Female,
pubmed-meshheading:12427097-Flow Cytometry,
pubmed-meshheading:12427097-Fluorescent Dyes,
pubmed-meshheading:12427097-Humans,
pubmed-meshheading:12427097-Protein Binding,
pubmed-meshheading:12427097-Streptococcal Infections,
pubmed-meshheading:12427097-Streptococcus agalactiae
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pubmed:year |
2002
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pubmed:articleTitle |
The alpha C protein mediates internalization of group B Streptococcus within human cervical epithelial cells.
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pubmed:affiliation |
Channing Laboratory, Boston, MA 02115, USA. gbolduc@rics.bwh.harvard.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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