Structural similarity (molecular mimicry) between viral epitopes and self-peptides can lead to the induction of autoaggressive CD4+ as well as CD8+ T cell responses. Based on the flexibility of T cell receptor/antigen/major histocompatibility complex recognition, it has been proposed that a self-peptide could replace a viral epitope for T cell recognition and therefore participate in pathophysiological processes in which T cells are involved. To address this issue, we used, as a molecular model of viral antigen, the H-2Db-restricted immunodominant epitope nucleoprotein (NP)-(396–404) (FQPQNGQFI) of lymphocytic choriomeningitis virus (LCMV). We identified peptide sequences from murine self-proteins that share structural and functional homology with LCMV NP-(396–404) and that bound to H-2Db with high affinity. One of these self-peptides, derived from tumor necrosis factor receptor I (FGPSNWHFM, amino acids 302–310), maintained LCMV-specific CD8+ T cells in an active state as observed both in vitro in cytotoxic assays and in vivoin a model of virus-induced autoimmune diabetes, the rat insulin promoter-LCMV NP transgenic mouse. The natural occurrence and molecular concentration at the surface of H-2b spleen cells of tumor necrosis factor receptor I-(302–310) were determined by on-line μ-high pressure liquid chromatography/mass spectrometry and supported its biological relevance. Structural similarity (molecular mimicry) between viral epitopes and self-peptides can lead to the induction of autoaggressive CD4+ as well as CD8+ T cell responses. Based on the flexibility of T cell receptor/antigen/major histocompatibility complex recognition, it has been proposed that a self-peptide could replace a viral epitope for T cell recognition and therefore participate in pathophysiological processes in which T cells are involved. To address this issue, we used, as a molecular model of viral antigen, the H-2Db-restricted immunodominant epitope nucleoprotein (NP)-(396–404) (FQPQNGQFI) of lymphocytic choriomeningitis virus (LCMV). We identified peptide sequences from murine self-proteins that share structural and functional homology with LCMV NP-(396–404) and that bound to H-2Db with high affinity. One of these self-peptides, derived from tumor necrosis factor receptor I (FGPSNWHFM, amino acids 302–310), maintained LCMV-specific CD8+ T cells in an active state as observed both in vitro in cytotoxic assays and in vivoin a model of virus-induced autoimmune diabetes, the rat insulin promoter-LCMV NP transgenic mouse. The natural occurrence and molecular concentration at the surface of H-2b spleen cells of tumor necrosis factor receptor I-(302–310) were determined by on-line μ-high pressure liquid chromatography/mass spectrometry and supported its biological relevance. major histocompatibility complex T cell receptor nucleoprotein lymphocytic choriomeningitis virus cytotoxic T lymphocyte rat insulin promoter insulin-dependent diabetes mellitus tumor necrosis factor receptor high pressure liquid chromatography electrospray ionization mass spectrometry interferon-γ Molecular mimicry, a process in which potentially autoreactive T cells are activated in the periphery by major histocompatibility complex (MHC)1-restricted cross-reactive self-peptides, is suspected to be a possible mechanism triggering pathological (versus normal) immunity, particularly virus-induced autoimmune disease (1Oldstone M.B.A. Cell. 1987; 50: 819-820Abstract Full Text PDF PubMed Scopus (798) Google Scholar). Although the recognition of a viral antigenic peptide by the T cell receptor (TCR) is a most specific process, structurally altered antigenic variants or mimicry peptides, which can be unrelated in terms of primary sequence to the viral antigen (2Evavold B.D. Sloan-Lancaster J. Wilson K.J. Rothbard J.B. Allen P.M. Immunity. 1995; 2: 655-663Abstract Full Text PDF PubMed Scopus (202) Google Scholar, 3Hemmer B. Vergelli M. Gran B. Ling N. Conlon P. Pinilla C. Houghten R. McFarland H.F. Martin R. J. Immunol. 1998; 160: 3631-3636PubMed Google Scholar, 4Wucherpfennig K.W. Strominger J.L. Cell. 1995; 80: 695-705Abstract Full Text PDF PubMed Scopus (1277) Google Scholar), can still be recognized by CD4+ or CD8+ T cells (5Jameson S.C. Bevan M.J. Immunity. 1995; 2: 1-11Abstract Full Text PDF PubMed Scopus (246) Google Scholar, 6Kersh G.J. Allen P.M. Nature. 1996; 380: 495-498Crossref PubMed Scopus (292) Google Scholar). The functional properties of these peptides depend on their structure, and their interaction with the TCR can lead to either full or partial T cell activation or antagonism (5Jameson S.C. Bevan M.J. Immunity. 1995; 2: 1-11Abstract Full Text PDF PubMed Scopus (246) Google Scholar). Such cross-reactive peptides are thought to play a role in pathophysiological situations such as T cell selection (7Hu Q. Bazemore Walker C.R. Girao C. Opferman J.T. Sun J. Shabanowitz J. Hunt D.F. Ashton-Rickardt P.G. Immunity. 1997; 7: 221-231Abstract Full Text Full Text PDF PubMed Scopus (85) Google Scholar, 8Hogquist K.A. Tomlinson A.J. Kieper W.C. McGargill M.A. Hart M.C. Naylor S. Jameson S.C. Immunity. 1997; 6: 389-399Abstract Full Text Full Text PDF PubMed Scopus (163) Google Scholar), anergy (9Sloan-Lancaster J. Evavold B.D. Allen P.M. Nature. 1993; 363: 156-159Crossref PubMed Scopus (579) Google Scholar), viral escape (10Klenerman P. Rowland-Jones S. McAdam S. Edwards J. Daenke S. Lalloo D. 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Pye S.J. Silins S.L. Proc. Natl. Acad. Sci. U. S. A. 1999; 96: 2279-2284Crossref PubMed Scopus (62) Google Scholar, 14Vizler C. Bercovici N. Cornet A. Cambouris C. Liblau R.S. Immunol. Rev. 1999; 169: 81-92Crossref PubMed Scopus (40) Google Scholar). However, the molecular mechanisms by which autoreactive CD8+ T cells are activated or maintained in a functional state remain mostly unknown. In this study, we explored the possible role of MHC class I-restricted self-peptides in these mechanisms because of their potential importance in clinical disease. Our aim was (i) to identify putative self-molecular mimics of a viral antigen, (ii) to characterize their structural and functional properties, and (iii) to determine their biological relevance. For this, we used the H-2Db-restricted immunodominant epitope located in nucleoprotein (NP)-(396–404) (FQPQNGQFI) of lymphocytic choriomeningitis virus (LCMV), a model of choice for dissecting the molecular or cellular mechanisms involved in an autoreactive CD8+ T cell response. Indeed, the H-2Db-restricted CD8+ T cell response mounted against the LCMV NP is directed toward the immunodominant epitope sequence NP-(396–404) (15Gairin J.E. Mazarguil H. Hudrisier D. Oldstone M.B.A. J. Virol. 1995; 69: 2297-2305Crossref PubMed Google Scholar, 16Schulz M. Aichele P. Wollenweider M. Bobe F.W. Cardinaux F. Hengartner H. Zinkernagel R.M. Eur. J. Immunol. 1989; 19: 1657-1667Crossref PubMed Scopus (111) Google Scholar, 17Murali-Krishna K. Altman J.D. Suresh M. Sourdive D. Zajac A. Ahmed R. Adv. Exp. Med. Biol. 1998; 452: 123-142Crossref PubMed Scopus (86) Google Scholar). 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Virol. 1993; PubMed Google Scholar). The of on the of NP-(396–404) to cells to by LCMV-specific was with the Oldstone M.B.A. J. Virol. PubMed Google are in The was observed at of for a peptide to cells at the concentration that is the TCR properties were also of at and at that these also play a of as TCR of at and The observed at and were as a of the properties of the were with of from either with LCMV or with NP-(396–404) and and TCR identified in the NP-(396–404) sequence the response against this of MHC and TCR is in specific at the peptide concentration and recognition of the LCMV NP-(396–404) epitope and for H-2Db for specific was observed at the peptide concentration specific at the peptide concentration were by the and by on a and their were by For H-2Db peptides to were in a MHC class I on cells as D. Mazarguil H. Oldstone M.B.A. J.E. 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Bevan M.J. J. Exp. Med. 1993; PubMed Scopus Google Scholar, W. Nature. 1995; PubMed Scopus Google Scholar, S. H. C. J. Immunol. 1996; Google Scholar, D. B. S. C. J. Immunol. 1998; Google Scholar), we determined the self-peptides could as the of the by the murine self-peptides with homology to of cells with of NP-(396–404) was in the of of self-peptides, was at the concentration In antagonism was with the H-2Db-restricted LCMV immunodominant which to H-2Db with a high to that of NP-(396–404) (15Gairin J.E. Mazarguil H. Hudrisier D. Oldstone M.B.A. J. Virol. 1995; 69: 2297-2305Crossref PubMed Google and To determine mimicry peptides could in we used of spleen cells from LCMV Such and particularly K. Altman J.D. Suresh M. Sourdive D. Zajac A. Ahmed R. Adv. Exp. Med. Biol. 1998; 452: 123-142Crossref PubMed Scopus (86) Google Scholar). were with with with or The peptides for this study, and and functional with LCMV in in the of T cells in by cells with LCMV or with the LCMV NP-(396–404) peptide in a of The mimicry peptides the to in in the In in the of MHC with the LCMV immunodominant of LCMV-specific H-2b as of LCMV-specific with LCMV and with LCMV and with LCMV and with and with and with and and were with LCMV a of cells LCMV-specific was in the of from and H-2b as cells with LCMV with the H-2Db-restricted or LCMV epitopes with the self-peptide or in a were with LCMV a of cells LCMV-specific was in the of from and H-2b as cells with LCMV with the H-2Db-restricted or LCMV epitopes with the self-peptide or We determined maintained in in the of a mimicry peptide functional We used the self-peptide for these in with LCMV-infected H-2b However, the was that observed with with LCMV or In H-2b with the NP-(396–404) or peptide were also by with the epitope were vitro cytotoxic of LCMV-specific of LCMV-specific from LCMV-infected and with LCMV-infected or as in the to were to LCMV-infected cells was in a at an of as LCMV-specific been in for at the the was from are and are of in a LCMV-specific from LCMV-infected and with LCMV-infected or as in the to were to LCMV-infected cells was in a at an of as LCMV-specific been in for at the the was from are and are of We determined the cytotoxic in For this such were NP transgenic In such either LCMV or of the of and as by the of and of insulin P. S. K. H. C. B. B. Zinkernagel R.M. Hengartner H. Cell. Full Text PDF PubMed Scopus Google Scholar, M.B.A. M. P. J. H. Cell. Full Text PDF PubMed Scopus Google S. H. Oldstone M.B.A. Immunity. 1995; Full Text PDF PubMed Scopus Google Scholar). in and were observed in of LCMV-specific with for the of these was to or of by or LCMV-infected of LCMV-specific H-2b NP transgenic of LCMV-specific with or NP with with the of these was observed by NP with or transgenic LCMV NP in cells of of the were were with activated as in the to and were and of was as M.B.A. M. P. J. H. Cell. Full Text PDF PubMed Scopus Google Scholar, J. Oldstone M.B.A. Immunity. 1994; Full Text PDF PubMed Scopus Google Scholar, S. H. Oldstone M.B.A. Immunity. 1995; Full Text PDF PubMed Scopus Google the of these was observed by in a H-2b or transgenic LCMV NP in cells of of the were were with activated as in the to and were and of was as M.B.A. M. P. J. H. Cell. Full Text PDF PubMed Scopus Google Scholar, J. Oldstone M.B.A. Immunity. 1994; Full Text PDF PubMed Scopus Google Scholar, S. H. Oldstone M.B.A. Immunity. 1995; Full Text PDF PubMed Scopus Google Scholar). The and was to that such a self-peptide with the to functional was at the cell To peptides were from the surface of by of and by on-line the peptide a its was the and Indeed, as a the peptide in and and by to the of the peptide and to the an as in at we that the of to both and with peptide from and spleen cells were and their were and by on-line mass and were to of the of the peptide was in of H-2b spleen of this natural of was by (i) which a of the natural and the and (ii) which a specific for the peptide as by Based on the the of the peptide from spleen cells was the of the the of on the cell surface was at cells, which an of Structural similarity (molecular mimicry) between viral epitopes and self-peptides can lead to the induction of MHC class autoaggressive CD4+ T cells (4Wucherpfennig K.W. Strominger J.L. Cell. 1995; 80: 695-705Abstract Full Text PDF PubMed Scopus (1277) Google as well as MHC class I CD8+ T cell (13Misko I.S. Cross S.M. Khanna R. Elliott S.L. Schmidt C. Pye S.J. Silins S.L. Proc. Natl. Acad. Sci. U. S. A. 1999; 96: 2279-2284Crossref PubMed Scopus (62) Google Scholar, 14Vizler C. Bercovici N. Cornet A. Cambouris C. Liblau R.S. Immunol. Rev. 1999; 169: 81-92Crossref PubMed Scopus (40) Google Scholar, A. A. E. K. B. Eur. J. Immunol. 1999; PubMed Google Scholar, B. J. A. J. Exp. Med. 1999; PubMed Scopus Google Scholar). clinical and experimental to that that with self-proteins can play a role in molecular mimicry M.B.A. J. 1998; PubMed Google Scholar, H. M. S. Sette A. Conlon P. J. Exp. Med. 1999; PubMed Scopus Google Scholar). for peptides structural homology with a antigen may be to identify potential cross-reactive (1Oldstone M.B.A. Cell. 1987; 50: 819-820Abstract Full Text PDF PubMed Scopus (798) Google Scholar, 4Wucherpfennig K.W. Strominger J.L. 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Immunity. 1997; 6: 389-399Abstract Full Text Full Text PDF PubMed Scopus (163) Google peptides in T selection and identified a for mimicry peptides to with MHC class autoreactive T cell specific for the a (4Wucherpfennig K.W. Strominger J.L. Cell. 1995; 80: 695-705Abstract Full Text PDF PubMed Scopus (1277) Google Scholar). which is by the of of these peptides in the from the of H-2b which molecular can the peptide and the self-peptides potentially autoreactive in a functional to the and the self-peptides identified as altered peptide J. Allen P.M. Rev. Immunol. 1996; PubMed Scopus Google Scholar), with at both functional and structural the functional the in their sequences of the TCR and of of an TCR of the mimicry self-peptides identified were to in as that still with the TCR and that their for the TCR was (7Hu Q. Bazemore Walker C.R. Girao C. Opferman J.T. Sun J. Shabanowitz J. Hunt D.F. Ashton-Rickardt P.G. 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In the is that self-peptides such as and identified in this can potentially autoreactive T cells to their in the of viral antigen a of the mechanisms by which potentially autoreactive CD8+ T cells are maintained or activated a of pathological also for it Immunol. 1999; PubMed Scopus Google Scholar). In this study, we on MHC class I self-peptides and on their possible role in these of the potential importance of these self-peptides in clinical the may particularly in terms of by to or molecular mimics to potentially autoreactive T We Mazarguil for peptide for of peptide and for molecular
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