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Volumn 26, Issue 1, 2014, Pages 115-122

HLA-DM and HLA-DO, key regulators of MHC-II processing and presentation

Author keywords

[No Author keywords available]

Indexed keywords

HLA DM ANTIGEN; HLA DO ANTIGEN; IMMUNOGLOBULIN G; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2;

EID: 84890050541     PISSN: 09527915     EISSN: 18790372     Source Type: Journal    
DOI: 10.1016/j.coi.2013.11.005     Document Type: Review
Times cited : (100)

References (55)
  • 1
    • 84875513590 scopus 로고    scopus 로고
    • The adaptable major histocompatibility complex (MHC) fold: structure and function of nonclassical and MHC class I-like molecules
    • Adams E.J., Luoma A.M. The adaptable major histocompatibility complex (MHC) fold: structure and function of nonclassical and MHC class I-like molecules. Annu Rev Immunol 2013, 31:529-561.
    • (2013) Annu Rev Immunol , vol.31 , pp. 529-561
    • Adams, E.J.1    Luoma, A.M.2
  • 2
    • 84871595445 scopus 로고    scopus 로고
    • Crystal structure of the HLA-DM-HLA-DR1 complex defines mechanisms for rapid peptide selection
    • Pos W., Sethi D.K., Call M.J., Schulze M.S., Anders A.K., Pyrdol J., Wucherpfennig K.W. Crystal structure of the HLA-DM-HLA-DR1 complex defines mechanisms for rapid peptide selection. Cell 2012, 151:1557-1568.
    • (2012) Cell , vol.151 , pp. 1557-1568
    • Pos, W.1    Sethi, D.K.2    Call, M.J.3    Schulze, M.S.4    Anders, A.K.5    Pyrdol, J.6    Wucherpfennig, K.W.7
  • 7
    • 82755181500 scopus 로고    scopus 로고
    • Conformational lability in the class II MHC 310 helix and adjacent extended strand dictate HLA-DM susceptibility and peptide exchange
    • Painter C.A., Negroni M.P., Kellersberger K.A., Zavala-Ruiz Z., Evans J.E., Stern L.J. Conformational lability in the class II MHC 310 helix and adjacent extended strand dictate HLA-DM susceptibility and peptide exchange. Proc Natl Acad Sci U S A 2011, 108:19329-19334.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 19329-19334
    • Painter, C.A.1    Negroni, M.P.2    Kellersberger, K.A.3    Zavala-Ruiz, Z.4    Evans, J.E.5    Stern, L.J.6
  • 8
    • 0030978530 scopus 로고    scopus 로고
    • HLA-DM acts as a molecular chaperone and rescues empty HLA-DR molecules at lysosomal pH
    • Kropshofer H., Arndt S.O., Moldenhauer G., Hammerling G.J., Vogt A.B. HLA-DM acts as a molecular chaperone and rescues empty HLA-DR molecules at lysosomal pH. Immunity 1997, 6:293-302.
    • (1997) Immunity , vol.6 , pp. 293-302
    • Kropshofer, H.1    Arndt, S.O.2    Moldenhauer, G.3    Hammerling, G.J.4    Vogt, A.B.5
  • 9
    • 0030458137 scopus 로고    scopus 로고
    • HLA-DM interactions with intermediates in HLA-DR maturation and a role for HLA-DM in stabilizing empty HLA-DR molecules
    • Denzin L.K., Hammond C., Cresswell P. HLA-DM interactions with intermediates in HLA-DR maturation and a role for HLA-DM in stabilizing empty HLA-DR molecules. J Exp Med 1996, 184:2153-2165.
    • (1996) J Exp Med , vol.184 , pp. 2153-2165
    • Denzin, L.K.1    Hammond, C.2    Cresswell, P.3
  • 11
    • 0034603779 scopus 로고    scopus 로고
    • A three-step kinetic mechanism for peptide binding to MHC class II proteins
    • Joshi R.V., Zarutskie J.A., Stern L.J. A three-step kinetic mechanism for peptide binding to MHC class II proteins. Biochemistry 2000, 39:3751-3762.
    • (2000) Biochemistry , vol.39 , pp. 3751-3762
    • Joshi, R.V.1    Zarutskie, J.A.2    Stern, L.J.3
  • 12
    • 0033084056 scopus 로고    scopus 로고
    • Empty and peptide-loaded class II major histocompatibility complex proteins produced by expression in Escherichia coli and folding in vitro
    • Frayser M., Sato A.K., Xu L., Stern L.J. Empty and peptide-loaded class II major histocompatibility complex proteins produced by expression in Escherichia coli and folding in vitro. Protein Expr Purif 1999, 15:105-114.
    • (1999) Protein Expr Purif , vol.15 , pp. 105-114
    • Frayser, M.1    Sato, A.K.2    Xu, L.3    Stern, L.J.4
  • 13
    • 0034684671 scopus 로고    scopus 로고
    • HLA-DM recognizes the flexible conformation of major histocompatibility complex class II
    • Chou C.L., Sadegh-Nasseri S. HLA-DM recognizes the flexible conformation of major histocompatibility complex class II. J Exp Med 2000, 192:1697-1706.
    • (2000) J Exp Med , vol.192 , pp. 1697-1706
    • Chou, C.L.1    Sadegh-Nasseri, S.2
  • 16
    • 0033713296 scopus 로고    scopus 로고
    • Determination of the HLA-DM interaction site on HLA-DR molecules
    • Doebele R.C., Busch R., Scott H.M., Pashine A., Mellins E.D. Determination of the HLA-DM interaction site on HLA-DR molecules. Immunity 2000, 13:517-527.
    • (2000) Immunity , vol.13 , pp. 517-527
    • Doebele, R.C.1    Busch, R.2    Scott, H.M.3    Pashine, A.4    Mellins, E.D.5
  • 17
    • 0032168861 scopus 로고    scopus 로고
    • The structure of HLA-DM, the peptide exchange catalyst that loads antigen onto class II MHC molecules during antigen presentation
    • Mosyak L., Zaller D.M., Wiley D.C. The structure of HLA-DM, the peptide exchange catalyst that loads antigen onto class II MHC molecules during antigen presentation. Immunity 1998, 9:377-383.
    • (1998) Immunity , vol.9 , pp. 377-383
    • Mosyak, L.1    Zaller, D.M.2    Wiley, D.C.3
  • 20
    • 84867325424 scopus 로고    scopus 로고
    • HLA-DM constrains epitope selection in the human CD4 T cell response to vaccinia virus by favoring the presentation of peptides with longer HLA-DM-mediated half-lives
    • Yin L., Calvo-Calle J.M., Dominguez-Amorocho O., Stern L.J. HLA-DM constrains epitope selection in the human CD4 T cell response to vaccinia virus by favoring the presentation of peptides with longer HLA-DM-mediated half-lives. J Immunol 2012, 189:3983-3994.
    • (2012) J Immunol , vol.189 , pp. 3983-3994
    • Yin, L.1    Calvo-Calle, J.M.2    Dominguez-Amorocho, O.3    Stern, L.J.4
  • 21
    • 84860320829 scopus 로고    scopus 로고
    • The utility and limitations of current Web-available algorithms to predict peptides recognized by CD4 T cells in response to pathogen infection
    • Chaves F.A., Lee A.H., Nayak J.L., Richards K.A., Sant A.J. The utility and limitations of current Web-available algorithms to predict peptides recognized by CD4 T cells in response to pathogen infection. J Immunol 2012, 188:4235-4248.
    • (2012) J Immunol , vol.188 , pp. 4235-4248
    • Chaves, F.A.1    Lee, A.H.2    Nayak, J.L.3    Richards, K.A.4    Sant, A.J.5
  • 22
    • 84880790787 scopus 로고    scopus 로고
    • Disruption of hydrogen bonds between major histocompatibility complex class II and the peptide N-terminus is not sufficient to form a human leukocyte antigen-DM receptive state of major histocompatibility complex class II
    • Schulze M.S., Anders A.K., Sethi D.K., Call M.J. Disruption of hydrogen bonds between major histocompatibility complex class II and the peptide N-terminus is not sufficient to form a human leukocyte antigen-DM receptive state of major histocompatibility complex class II. PLoS ONE 2013, 8:e69228.
    • (2013) PLoS ONE , vol.8
    • Schulze, M.S.1    Anders, A.K.2    Sethi, D.K.3    Call, M.J.4
  • 23
    • 84883684287 scopus 로고    scopus 로고
    • Mechanisms of peptide repertoire selection by HLA-DM
    • Pos W., Sethi D.K., Wucherpfennig K.W. Mechanisms of peptide repertoire selection by HLA-DM. Trends Immunol 2013, 34:495-501.
    • (2013) Trends Immunol , vol.34 , pp. 495-501
    • Pos, W.1    Sethi, D.K.2    Wucherpfennig, K.W.3
  • 24
    • 77958128035 scopus 로고    scopus 로고
    • Divergent motifs but overlapping binding repertoires of six HLA-DQ molecules frequently expressed in the worldwide human population
    • Sidney J., Steen A., Moore C., Ngo S., Chung J., Peters B., Sette A. Divergent motifs but overlapping binding repertoires of six HLA-DQ molecules frequently expressed in the worldwide human population. J Immunol 2010, 185:4189-4198.
    • (2010) J Immunol , vol.185 , pp. 4189-4198
    • Sidney, J.1    Steen, A.2    Moore, C.3    Ngo, S.4    Chung, J.5    Peters, B.6    Sette, A.7
  • 25
    • 80052679493 scopus 로고    scopus 로고
    • An insertion mutant in DQA1*0501 restores susceptibility to HLA-DM: implications for disease associations
    • Hou T., Macmillan H., Chen Z., Keech C.L., Jin X., Sidney J., Strohman M., Yoon T., Mellins E.D. An insertion mutant in DQA1*0501 restores susceptibility to HLA-DM: implications for disease associations. J Immunol 2011, 187:2442-2452.
    • (2011) J Immunol , vol.187 , pp. 2442-2452
    • Hou, T.1    Macmillan, H.2    Chen, Z.3    Keech, C.L.4    Jin, X.5    Sidney, J.6    Strohman, M.7    Yoon, T.8    Mellins, E.D.9
  • 26
    • 1642447710 scopus 로고    scopus 로고
    • Structural basis for HLA-DQ2-mediated presentation of gluten epitopes in celiac disease
    • Kim C.Y., Quarsten H., Bergseng E., Khosla C., Sollid L.M. Structural basis for HLA-DQ2-mediated presentation of gluten epitopes in celiac disease. Proc Natl Acad Sci U S A 2004, 101:4175-4179.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 4175-4179
    • Kim, C.Y.1    Quarsten, H.2    Bergseng, E.3    Khosla, C.4    Sollid, L.M.5
  • 27
    • 84860431793 scopus 로고    scopus 로고
    • A Peptide/MHCII conformer generated in the presence of exchange peptide is substrate for HLA-DM editing
    • Ferrante A., Gorski J. A Peptide/MHCII conformer generated in the presence of exchange peptide is substrate for HLA-DM editing. Sci Rep 2012, 2:386.
    • (2012) Sci Rep , vol.2 , pp. 386
    • Ferrante, A.1    Gorski, J.2
  • 28
    • 56649109618 scopus 로고    scopus 로고
    • HLA-DM mediates epitope selection by a "compare-exchange" mechanism when a potential peptide pool is available
    • Ferrante A., Anderson M.W., Klug C.S., Gorski J. HLA-DM mediates epitope selection by a "compare-exchange" mechanism when a potential peptide pool is available. PLoS ONE 2008, 3:e3722.
    • (2008) PLoS ONE , vol.3
    • Ferrante, A.1    Anderson, M.W.2    Klug, C.S.3    Gorski, J.4
  • 29
    • 0026007230 scopus 로고
    • Energy transfer between two peptides bound to one MHC class II molecule
    • Tampe R., Clark B.R., McConnell H.M. Energy transfer between two peptides bound to one MHC class II molecule. Science 1991, 254:87-89.
    • (1991) Science , vol.254 , pp. 87-89
    • Tampe, R.1    Clark, B.R.2    McConnell, H.M.3
  • 31
    • 10944263783 scopus 로고    scopus 로고
    • "Chemical analogues" of HLA-DM can induce a peptide-receptive state in HLA-DR molecules
    • Marin-Esteban V., Falk K., Rotzschke O. "Chemical analogues" of HLA-DM can induce a peptide-receptive state in HLA-DR molecules. J Biol Chem 2004, 279:50684-50690.
    • (2004) J Biol Chem , vol.279 , pp. 50684-50690
    • Marin-Esteban, V.1    Falk, K.2    Rotzschke, O.3
  • 35
    • 0027265394 scopus 로고
    • Ligand-induced accelerated dissociation of (+)-cis-diltiazem from L-type Ca2+ channels is simply explained by competition for individual attachment points
    • Prinz H., Striessnig J. Ligand-induced accelerated dissociation of (+)-cis-diltiazem from L-type Ca2+ channels is simply explained by competition for individual attachment points. J Biol Chem 1993, 268:18580-18585.
    • (1993) J Biol Chem , vol.268 , pp. 18580-18585
    • Prinz, H.1    Striessnig, J.2
  • 36
    • 84869880199 scopus 로고    scopus 로고
    • Accelerated disassembly of IgE-receptor complexes by a disruptive macromolecular inhibitor
    • Kim B., Eggel A., Tarchevskaya S.S., Vogel M., Prinz H., Jardetzky T.S. Accelerated disassembly of IgE-receptor complexes by a disruptive macromolecular inhibitor. Nature 2012, 491:613-617.
    • (2012) Nature , vol.491 , pp. 613-617
    • Kim, B.1    Eggel, A.2    Tarchevskaya, S.S.3    Vogel, M.4    Prinz, H.5    Jardetzky, T.S.6
  • 37
    • 84871834366 scopus 로고    scopus 로고
    • Immunodeficiency and autoimmunity in H2-O-deficient mice
    • Gu Y., Jensen P.E., Chen X. Immunodeficiency and autoimmunity in H2-O-deficient mice. J Immunol 2013, 190:126-137.
    • (2013) J Immunol , vol.190 , pp. 126-137
    • Gu, Y.1    Jensen, P.E.2    Chen, X.3
  • 39
    • 0041466079 scopus 로고    scopus 로고
    • H2-O influence on antigen presentation in H2-E-expressing mice
    • Alfonso C., Williams G.S., Karlsson L. H2-O influence on antigen presentation in H2-E-expressing mice. Eur J Immunol 2003, 33:2014-2021.
    • (2003) Eur J Immunol , vol.33 , pp. 2014-2021
    • Alfonso, C.1    Williams, G.S.2    Karlsson, L.3
  • 43
    • 77950193442 scopus 로고    scopus 로고
    • Targeted regulation of self-peptide presentation prevents type I diabetes in mice without disrupting general immunocompetence
    • Yi W., Seth N.P., Martillotti T., Wucherpfennig K.W., Sant'Angelo D.B., Denzin L.K. Targeted regulation of self-peptide presentation prevents type I diabetes in mice without disrupting general immunocompetence. J Clin Invest 2010, 120:1324-1336.
    • (2010) J Clin Invest , vol.120 , pp. 1324-1336
    • Yi, W.1    Seth, N.P.2    Martillotti, T.3    Wucherpfennig, K.W.4    Sant'Angelo, D.B.5    Denzin, L.K.6
  • 44
    • 84868139454 scopus 로고    scopus 로고
    • Endogenous HLA class II epitopes that are immunogenic in vivo show distinct behavior toward HLA-DM and its natural inhibitor HLA-DO
    • Kremer A.N., van der Meijden E.D., Honders M.W., Goeman J.J., Wiertz E.J., Falkenburg J.H., Griffioen M. Endogenous HLA class II epitopes that are immunogenic in vivo show distinct behavior toward HLA-DM and its natural inhibitor HLA-DO. Blood 2012, 120:3246-3255.
    • (2012) Blood , vol.120 , pp. 3246-3255
    • Kremer, A.N.1    van der Meijden, E.D.2    Honders, M.W.3    Goeman, J.J.4    Wiertz, E.J.5    Falkenburg, J.H.6    Griffioen, M.7
  • 45
    • 84883825805 scopus 로고    scopus 로고
    • HLA-DO increases bacterial superantigen binding to human MHC molecules by inhibiting dissociation of class II-associated invariant chain peptides
    • Pezeshki A.M., Azar G.A., Mourad W., Routy J.P., Boulassel M.R., Denzin L.K., Thibodeau J. HLA-DO increases bacterial superantigen binding to human MHC molecules by inhibiting dissociation of class II-associated invariant chain peptides. Hum Immunol 2013, 74:1280-1287.
    • (2013) Hum Immunol , vol.74 , pp. 1280-1287
    • Pezeshki, A.M.1    Azar, G.A.2    Mourad, W.3    Routy, J.P.4    Boulassel, M.R.5    Denzin, L.K.6    Thibodeau, J.7
  • 46
    • 84881319397 scopus 로고    scopus 로고
    • HLA-DO as the optimizer of epitope selection for MHC class II antigen presentation
    • Poluektov Y.O., Kim A., Hartman I.Z., Sadegh-Nasseri S. HLA-DO as the optimizer of epitope selection for MHC class II antigen presentation. PLoS ONE 2013, 8:e71228.
    • (2013) PLoS ONE , vol.8
    • Poluektov, Y.O.1    Kim, A.2    Hartman, I.Z.3    Sadegh-Nasseri, S.4
  • 47
    • 18144397513 scopus 로고    scopus 로고
    • A point mutation in the groove of HLA-DO allows egress from the endoplasmic reticulum independent of HLA-DM
    • Deshaies F., Brunet A., Diallo D.A., Denzin L.K., Samaan A., Thibodeau J. A point mutation in the groove of HLA-DO allows egress from the endoplasmic reticulum independent of HLA-DM. Proc Natl Acad Sci U S A 2005, 102:6443-6448.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 6443-6448
    • Deshaies, F.1    Brunet, A.2    Diallo, D.A.3    Denzin, L.K.4    Samaan, A.5    Thibodeau, J.6
  • 48
    • 17544401516 scopus 로고    scopus 로고
    • Prolonged antigen persistence within nonterminal late endocytic compartments of antigen-specific B lymphocytes
    • Gondre-Lewis T.A., Moquin A.E., Drake J.R. Prolonged antigen persistence within nonterminal late endocytic compartments of antigen-specific B lymphocytes. J Immunol 2001, 166:6657-6664.
    • (2001) J Immunol , vol.166 , pp. 6657-6664
    • Gondre-Lewis, T.A.1    Moquin, A.E.2    Drake, J.R.3
  • 51
    • 84876858943 scopus 로고    scopus 로고
    • Ubiquitination of HLA-DO by MARCH family E3 ligases
    • Jahnke M., Trowsdale J., Kelly A.P. Ubiquitination of HLA-DO by MARCH family E3 ligases. Eur J Immunol 2013, 43:1153-1161.
    • (2013) Eur J Immunol , vol.43 , pp. 1153-1161
    • Jahnke, M.1    Trowsdale, J.2    Kelly, A.P.3
  • 53
    • 84866740799 scopus 로고    scopus 로고
    • Antigen presentation events in autoimmune diabetes
    • Mohan J.F., Unanue E.R. Antigen presentation events in autoimmune diabetes. Nat Rev Immunol 2012, 12:721-728.
    • (2012) Nat Rev Immunol , vol.12 , pp. 721-728
    • Mohan, J.F.1    Unanue, E.R.2
  • 54
    • 77949872804 scopus 로고    scopus 로고
    • Unique autoreactive T cells recognize insulin peptides generated within the islets of Langerhans in autoimmune diabetes
    • Mohan J.F., Levisetti M.G., Calderon B., Herzog J.W., Petzold S.J., Unanue E.R. Unique autoreactive T cells recognize insulin peptides generated within the islets of Langerhans in autoimmune diabetes. Nat Immunol 2010, 11:350-354.
    • (2010) Nat Immunol , vol.11 , pp. 350-354
    • Mohan, J.F.1    Levisetti, M.G.2    Calderon, B.3    Herzog, J.W.4    Petzold, S.J.5    Unanue, E.R.6


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