Publication Date:
1989-09-08
Description:
Heat shock proteins are evolutionarily highly conserved polypeptides that are produced under a variety of stress conditions to preserve cellular functions. A major antigen of tubercle bacilli of 65 kilodaltons is a heat shock protein that has significant sequence similarity and cross-reactivity with antigens of various other microbes. Monoclonal antibodies against this common bacterial heat shock protein were used to identify a molecule of similar size in murine macrophages. Macrophages subjected to various stress stimuli including interferon-gamma activation and viral infection were recognized by class I-restricted CD8 T cells raised against the bacterial heat shock protein. These data suggest that heat shock proteins are processed in stressed host cells and that epitopes shared by heat shock proteins of bacterial and host origin are presented in the context of class I molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koga, T -- Wand-Wurttenberger, A -- DeBruyn, J -- Munk, M E -- Schoel, B -- Kaufmann, S H -- New York, N.Y. -- Science. 1989 Sep 8;245(4922):1112-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Microbiology and Immunology, University of Ulm, Federal Republic of Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2788923" target="_blank"〉PubMed〈/a〉
Keywords:
Animals
;
Antibodies, Bacterial/physiology
;
Antibodies, Monoclonal/physiology
;
Antigens, Differentiation, T-Lymphocyte/immunology
;
Bacterial Proteins/*immunology/pharmacology
;
Binding, Competitive
;
Cross Reactions
;
Cytotoxicity, Immunologic
;
Heat-Shock Proteins/*immunology/pharmacology
;
Macrophages/drug effects/*immunology
;
Mice
;
Mice, Inbred C57BL
;
T-Lymphocytes, Cytotoxic/*immunology
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
