{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T08:33:32Z","timestamp":1791189212392,"version":"4.1.0"},"reference-count":29,"publisher":"Rockefeller University Press","issue":"5","content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1998,3,2]]},"abstract":"<jats:p>Heat shock proteins (hsp's) isolated from murine cancer cells can elicit protective immunity and specific cytotoxic T lymphocytes (CTLs) by channeling tumor-derived peptides bound to hsp's to the major histocompatibility class I antigen presentation pathway. Here we have investigated if hsp70 can be used in a novel peptide vaccine for the induction of protective antiviral immunity and memory CTLs. A CTL epitope from the well-defined lymphocytic choriomeningitis virus (LCMV) system was mixed with recombinant hsp70 in vitro under conditions that optimize peptide binding to hsp70. Mice were immunized with the hsp70\u2013peptide mixture and challenged with LCMV. Virus titers were reduced 10\u2013100-fold in these mice compared to control mice. Immunization with the hsp70\u2013peptide mixture resulted in the development of CTL memory cells that could be reactivated during LCMV infection, and that in a 51Cr-release assay could lyse cells pulsed with the same peptide, but not cells pulsed with another LCMV peptide. These results show that hsp70 can be used with CTL epitopes to induce efficient protective antiviral immunity and the generation of peptide-specific CTLs. The results also demonstrate the usefulness of hsp70 as an alternative to adjuvants and DNA vectors for the delivery of CTL epitopes to antigen-presenting cells.<\/jats:p>","DOI":"10.1084\/jem.187.5.685","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T16:49:30Z","timestamp":1027702170000},"page":"685-691","update-policy":"https:\/\/doi.org\/10.1084\/jem.crossmarkpolicy","source":"Crossref","is-referenced-by-count":128,"title":["Immunization with a Lymphocytic Choriomeningitis Virus Peptide Mixed with Heat Shock Protein 70 Results in Protective Antiviral Immunity and Specific Cytotoxic T Lymphocytes"],"prefix":"10.1084","volume":"187","author":[{"given":"Anne-Marie T.","family":"Ciupitu","sequence":"first","affiliation":[{"name":"From the *Microbiology and Tumor Biology Center, Karolinska Institute, Stockholm, Sweden S-171 77; the \u2021Department of Pathology, University of Massachusetts Medical Center, Worcester, Massachusetts 01655; \u00a7Biogen, Inc., Cambridge, Massachusetts 02142; \u2016NeoGenesis, Inc., Cambridge, Massachusetts 02142; and the \u00b6Department of Experimental Oncology, Radiumhemmet, Karolinska Hospital, Stockholm, Sweden S-171 77"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Max","family":"Petersson","sequence":"additional","affiliation":[{"name":"From the *Microbiology and Tumor Biology Center, Karolinska Institute, Stockholm, Sweden S-171 77; the \u2021Department of Pathology, University of Massachusetts Medical Center, Worcester, Massachusetts 01655; \u00a7Biogen, Inc., Cambridge, Massachusetts 02142; \u2016NeoGenesis, Inc., Cambridge, Massachusetts 02142; and the \u00b6Department of Experimental Oncology, Radiumhemmet, Karolinska Hospital, Stockholm, Sweden S-171 77"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carey L.","family":"O'Donnell","sequence":"additional","affiliation":[{"name":"From the *Microbiology and Tumor Biology Center, Karolinska Institute, Stockholm, Sweden S-171 77; the \u2021Department of Pathology, University of Massachusetts Medical Center, Worcester, Massachusetts 01655; \u00a7Biogen, Inc., Cambridge, Massachusetts 02142; \u2016NeoGenesis, Inc., Cambridge, Massachusetts 02142; and the \u00b6Department of Experimental Oncology, Radiumhemmet, Karolinska Hospital, Stockholm, Sweden S-171 77"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kevin","family":"Williams","sequence":"additional","affiliation":[{"name":"From the *Microbiology and Tumor Biology Center, Karolinska Institute, Stockholm, Sweden S-171 77; the \u2021Department of Pathology, University of Massachusetts Medical Center, Worcester, Massachusetts 01655; \u00a7Biogen, Inc., Cambridge, Massachusetts 02142; \u2016NeoGenesis, Inc., Cambridge, Massachusetts 02142; and the \u00b6Department of Experimental Oncology, Radiumhemmet, Karolinska Hospital, Stockholm, Sweden S-171 77"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Satish","family":"Jindal","sequence":"additional","affiliation":[{"name":"From the *Microbiology and Tumor Biology Center, Karolinska Institute, Stockholm, Sweden S-171 77; the \u2021Department of Pathology, University of Massachusetts Medical Center, Worcester, Massachusetts 01655; \u00a7Biogen, Inc., Cambridge, Massachusetts 02142; \u2016NeoGenesis, Inc., Cambridge, Massachusetts 02142; and the \u00b6Department of Experimental Oncology, Radiumhemmet, Karolinska Hospital, Stockholm, Sweden S-171 77"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rolf","family":"Kiessling","sequence":"additional","affiliation":[{"name":"From the *Microbiology and Tumor Biology Center, Karolinska Institute, Stockholm, Sweden S-171 77; the \u2021Department of Pathology, University of Massachusetts Medical Center, Worcester, Massachusetts 01655; \u00a7Biogen, Inc., Cambridge, Massachusetts 02142; \u2016NeoGenesis, Inc., Cambridge, Massachusetts 02142; and the \u00b6Department of Experimental Oncology, Radiumhemmet, Karolinska Hospital, Stockholm, Sweden S-171 77"},{"name":"From the *Microbiology and Tumor Biology Center, Karolinska Institute, Stockholm, Sweden S-171 77; the \u2021Department of Pathology, University of Massachusetts Medical Center, Worcester, Massachusetts 01655; \u00a7Biogen, Inc., Cambridge, Massachusetts 02142; \u2016NeoGenesis, Inc., Cambridge, Massachusetts 02142; and the \u00b6Department of Experimental Oncology, Radiumhemmet, Karolinska Hospital, Stockholm, Sweden S-171 77"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Raymond M.","family":"Welsh","sequence":"additional","affiliation":[{"name":"From the *Microbiology and Tumor Biology Center, Karolinska Institute, Stockholm, Sweden S-171 77; the \u2021Department of Pathology, University of Massachusetts Medical Center, Worcester, Massachusetts 01655; \u00a7Biogen, Inc., Cambridge, Massachusetts 02142; \u2016NeoGenesis, Inc., Cambridge, Massachusetts 02142; and the \u00b6Department of Experimental Oncology, Radiumhemmet, Karolinska Hospital, Stockholm, Sweden S-171 77"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"291","published-online":{"date-parts":[[1998,3,2]]},"reference":[{"key":"2023072507574560300_B1","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1038\/355033a0","article-title":"Protein folding in the cell","volume":"355","author":"Gething","year":"1992","journal-title":"Nature"},{"key":"2023072507574560300_B2","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1016\/0968-0004(94)90169-4","article-title":"Molecular chaperones in protein folding: the art of avoiding sticky situations","volume":"19","author":"Hartl","year":"1994","journal-title":"TIBS (Trends Biochem Sci)"},{"key":"2023072507574560300_B3","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1016\/0092-8674(93)90492-9","article-title":"Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP","volume":"75","author":"Blond-Elguindi","year":"1993","journal-title":"Cell"},{"key":"2023072507574560300_B4","doi-asserted-by":"crossref","first-page":"30470","DOI":"10.1016\/S0021-9258(18)43837-9","article-title":"Common and divergent peptide binding specificities of hsp70 molecular chaperones","volume":"269","author":"Fourie","year":"1994","journal-title":"J Biol Chem"},{"key":"2023072507574560300_B5","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1016\/0092-8674(94)90416-2","article-title":"Heat shock proteins and molecular chaperones: mediators of protein conformation and turnover in the cell","volume":"78","author":"Craig","year":"1994","journal-title":"Cell"},{"key":"2023072507574560300_B6","doi-asserted-by":"crossref","first-page":"873","DOI":"10.4049\/jimmunol.156.2.873","article-title":"Adjuvant-free hsp70 fusion protein system elicits humoral and cellular immune responses to HIV-1 p24","volume":"156","author":"Suzuke","year":"1996","journal-title":"J Immunol"},{"key":"2023072507574560300_B7","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1046\/j.1365-2567.1996.d01-697.x","article-title":"Synthetic peptides noncovalently bound to bacterial hsp70 elicit peptide-specific T-cell responses in vivo.","volume":"88","author":"Rom\u00e1n","year":"1996","journal-title":"Immunology"},{"key":"2023072507574560300_B8","doi-asserted-by":"crossref","first-page":"1391","DOI":"10.1084\/jem.178.4.1391","article-title":"Heat shock protein 70\u2013associated peptides elicit specific cancer immunity","volume":"178","author":"Udono","year":"1993","journal-title":"J Exp Med"},{"key":"2023072507574560300_B9","doi-asserted-by":"crossref","first-page":"5398","DOI":"10.4049\/jimmunol.152.11.5398","article-title":"Comparison of tumor-specific immunogenicities of stress-induced proteins gp96, hsp90 and hsp70","volume":"152","author":"Udono","year":"1994","journal-title":"J Immunol"},{"key":"2023072507574560300_B10","doi-asserted-by":"crossref","first-page":"1585","DOI":"10.1126\/science.7545313","article-title":"A mechanism for the specific immunogenicity of heat shock protein\u2013chaperoned peptides","volume":"269","author":"Suto","year":"1995","journal-title":"Science"},{"key":"2023072507574560300_B11","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1111\/j.1600-065X.1993.tb01517.x","article-title":"Effector T-cell induction and T-cell memory versus peripheral deletion of T cells","volume":"131","author":"Zinkernagel","year":"1993","journal-title":"Immunol Rev"},{"key":"2023072507574560300_B12","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1006\/viro.1995.1314","article-title":"CTL escape viral variants. 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