The Journal of Experimental Medicine · 1993 · 625 citations · 25 references
Life SciencesImmunologyOncologyCancer ImmunologyTumor ImmunologyVaccinologyAntigen PresentationCancer ImmunotherapyCancer VaccinesTumor AntigensTumor-associated AntigensVaccine-based ImmunotherapyMolecular Mass DeterminationPeptide Binding AffinityPeptide EpitopesPeptide VaccinationPeptide-based ImmunotherapyProtein-based Cancer VaccinesTumor Antigen RecognitionTumor Rejection Antigens
Vaccination of mice with heat shock protein 70 (hsp70) preparations derived from the Meth A sarcoma, but not from normal tissues, renders the mice immune to a substantial challenge with Meth A sarcoma. The immunogenicity is dose dependent and tumor specific. Treatment of an antigenically active hsp70 preparation with ATP followed by removal of low-molecular weight material leaves hsp70 intact, as judged by SDS-PAGE but results in loss of antigenicity, as judged by tumor rejection assays. Separation of this low-molecular weight material on a C18 reverse-phase column shows a diverse array of peptides with molecular mass between 1,000 and 5,000 daltons. Our data indicate that antigenicity of hsp70 preparations derives, not from hsp70 per se, but from associated peptides. These observations may suggest a novel method of using the peptide-binding property of hsp70 for specific vaccination against cancer and infectious diseases.
25
Peptide-binding specificity of the molecular chaperone BiP
Gregory C. Flynn, Jan Pohl, Mark T. Flocco et al. · Nature · 1991 · 773 citations
Alterations in Signal Transduction Molecules in T Lymphocytes from Tumor-Bearing Mice
Hiromoto Mizoguchi, John J. O’Shea, Dan L. Longo et al. · Science · 1992 · 639 citations
Life Sciences, Immunology, Oncology +17
Phagocytic processing of bacterial antigens for class I MHC presentation to T cells
John D. Pfeifer, Mary Jo Wick, Richard Roberts et al. · Nature · 1993 · 615 citations