T Cells Against a Bacterial Heat Shock Protein Recognize Stressed Macrophages

DOI Web Site 被引用文献8件
  • Tetsuya Koga
    Department Medical Microbiology and Immunology, University of Ulm, D-7900 Ulm, Federal Republic of Germany.
  • Angela Wand-Württenberger
    Department Medical Microbiology and Immunology, University of Ulm, D-7900 Ulm, Federal Republic of Germany.
  • Jacqueline DeBruyn
    Institut Pasteur du Brabant, B-1180 Bruxelles, Belgium.
  • Martin E. Munk
    Department Medical Microbiology and Immunology, University of Ulm, D-7900 Ulm, Federal Republic of Germany.
  • Bernd Schoel
    Department Medical Microbiology and Immunology, University of Ulm, D-7900 Ulm, Federal Republic of Germany.
  • Stefan H. E. Kaufmann
    Department Medical Microbiology and Immunology, University of Ulm, D-7900 Ulm, Federal Republic of Germany.

抄録

<jats:p>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-γ 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.</jats:p>

収録刊行物

  • Science

    Science 245 (4922), 1112-1115, 1989-09-08

    American Association for the Advancement of Science (AAAS)

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