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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
9
|
| pubmed:dateCreated |
1995-12-14
|
| pubmed:abstractText |
We demonstrate conclusively that the bacterial exotoxin listeriolysin O (LLO) is a target Ag for eliciting CD4+ T cell responses following infection with Listeria monocytogenes. The minimal I-Ek-restricted immunodominant CD4+ T cell epitope was identified as peptide 215-226 (p215-226). Most LLO-specific T cell hybridomas recognized p203-226, p208-226, p215-226, and p215-234, although each exhibited a characteristic pattern of preferential reactivity. One hybridoma (IIIC5) reacted to p203-226 but not to p208-226 or any other LLO peptide tested. With APCs from B10 congenic mice and cells transfected with either I-Ak or I-Ek, IIIC5 recognized p203-216 with I-Ak, while a different hybridoma (IB5) recognized p215-226 with I-Ek. Competitive binding studies demonstrated that of 15 LLO peptides tested, only p203-226, p215-226, and p215-234 had high affinity for I-Ek, while p203-226 could also bind to isolated I-Ak. Of nine LLO peptides tested, only p215-234 bound multiple class II MHC alleles. These findings suggest that the immunodominance of p203-226 may be due in part to the presence of multiple T cell epitopes with I-Ek- and I-Ak-binding capability. Many of the rules of immunodominance observed with model Ags are also operative in our murine model of bacterial infectious disease. Furthermore, a novel mechanism of immunodominance based on newly defined structural features of MHC molecules is implicated. This information is crucial for rational vaccine development.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
AIM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hemolysin Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Histocompatibility Antigens Class II,
http://linkedlifedata.com/resource/pubmed/chemical/Immunodominant Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/hlyA protein, Listeria monocytogenes
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0022-1767
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
1
|
| pubmed:volume |
155
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
4355-66
|
| pubmed:dateRevised |
2010-11-18
|
| pubmed:meshHeading |
pubmed-meshheading:7594595-Amino Acid Sequence,
pubmed-meshheading:7594595-Animals,
pubmed-meshheading:7594595-Antigens, Bacterial,
pubmed-meshheading:7594595-Bacterial Proteins,
pubmed-meshheading:7594595-Bacterial Toxins,
pubmed-meshheading:7594595-CD4-Positive T-Lymphocytes,
pubmed-meshheading:7594595-Epitopes,
pubmed-meshheading:7594595-Female,
pubmed-meshheading:7594595-Heat-Shock Proteins,
pubmed-meshheading:7594595-Hemolysin Proteins,
pubmed-meshheading:7594595-Histocompatibility Antigens Class II,
pubmed-meshheading:7594595-Hybridomas,
pubmed-meshheading:7594595-Immunodominant Epitopes,
pubmed-meshheading:7594595-Listeriosis,
pubmed-meshheading:7594595-Mice,
pubmed-meshheading:7594595-Mice, Inbred C3H,
pubmed-meshheading:7594595-Molecular Sequence Data,
pubmed-meshheading:7594595-Protein Binding
|
| pubmed:year |
1995
|
| pubmed:articleTitle |
Mechanisms of T cell epitope immunodominance analyzed in murine listeriosis.
|
| pubmed:affiliation |
Department of Microbiology and Immunology, Emory University School of Medicine, Atlanta, GA 30322, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|