Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1998-6-11
pubmed:abstractText
We studied the mechanisms of MHC class II-restricted bacterial Ag processing of the surface fibrillar M5 protein from viable Streptococcus pyogenes in murine macrophages. Two previously defined T cell epitopes were studied using T cell hybridomas specific for 308-319/Ad, associated with the cell wall on the surface of streptococci, and 17-31/Ed, located at the protruding amino terminus of M5. Studies with metabolic inhibitors showed that slow (1 h) processing of M5 308-319 occurred in late endosomes and was dependent on newly synthesized MHC class II molecules and microtubules and on communications between early and late endosomes, consistent with engagement of the classical MHC class II processing pathway. In contrast, fast (15 min) bacterial Ag processing of 17-31 occurred in early endosomes independently of newly synthesized MHC class II molecules and microtubules and of trafficking between early and late endosomes, consistent with the recycling MHC class II processing pathway. Finally, bacterial Ag processing of the epitopes exhibited differential sensitivity to blocking with anti-MHC class II Abs. Thus, two T cell epitopes of a single protective Ag from the surface of whole bacteria are routed to distinct MHC class II processing pathways.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
160
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5267-72
pubmed:dateRevised
2010-8-25
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Two T cell epitopes from the M5 protein of viable Streptococcus pyogenes engage different pathways of bacterial antigen processing in mouse macrophages.
pubmed:affiliation
Department of Immunology, The Medical School, Newcastle University, Newcastle upon Tyne, United Kingdom.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't