Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1994-8-4
pubmed:abstractText
The outer membrane protein PhoE of Escherichia coli can be used for the expression of foreign antigenic determinants. Previously, a T-cell epitope of the 65 kDa heat shock protein (hsp65) of Mycobacterium tuberculosis, comprising amino acids 180 to 188, was expressed in PhoE. The hybrid protein induced proliferation of epitope-specific T-cell clones in vitro. In this report, the potential of the hybrid protein to induce an in vivo T-cell response against the 180-188 T-cell epitope was assessed. Popliteal lymph node cells, isolated from rats immunized with PhoE containing the hsp65 epitope, showed high proliferative responses to a synthetic peptide consisting of amino acids 180 to 188 of hsp65, indicating that the epitope is immunogenic in the PhoE-associated conformation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Bacterial, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Chaperonin 60, http://linkedlifedata.com/resource/pubmed/chemical/Chaperonins, http://linkedlifedata.com/resource/pubmed/chemical/Epitopes, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments, http://linkedlifedata.com/resource/pubmed/chemical/PhoE protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/Porins, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/heat-shock protein 65, Mycobacterium
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0264-410X
pubmed:author
pubmed:issnType
Print
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
406-9
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:7517602-Animals, pubmed-meshheading:7517602-Antigens, Bacterial, pubmed-meshheading:7517602-Bacterial Proteins, pubmed-meshheading:7517602-Chaperonin 60, pubmed-meshheading:7517602-Chaperonins, pubmed-meshheading:7517602-Epitopes, pubmed-meshheading:7517602-Escherichia coli, pubmed-meshheading:7517602-Escherichia coli Proteins, pubmed-meshheading:7517602-Heat-Shock Proteins, pubmed-meshheading:7517602-Immunization, pubmed-meshheading:7517602-Lymph Nodes, pubmed-meshheading:7517602-Lymphocyte Activation, pubmed-meshheading:7517602-Male, pubmed-meshheading:7517602-Mycobacterium tuberculosis, pubmed-meshheading:7517602-Peptide Fragments, pubmed-meshheading:7517602-Porins, pubmed-meshheading:7517602-Rats, pubmed-meshheading:7517602-Rats, Inbred Lew, pubmed-meshheading:7517602-Recombinant Fusion Proteins, pubmed-meshheading:7517602-T-Lymphocyte Subsets
pubmed:year
1994
pubmed:articleTitle
Immunogenicity of a mycobacterial T-cell epitope expressed in outer membrane protein PhoE of Escherichia coli.
pubmed:affiliation
Institute of Molecular Biology and Medical Biotechnology, University of Utrecht, The Netherlands.
pubmed:publicationType
Journal Article