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Appendices
Aufgaben
1 6.1 Kurze Antwort
Dendritische Zellen können exogene Antigene effizient aufnehmen und den T-Zellen auf MHC-Klasse-I-Molekülen präsentieren. Wie unterscheiden sie sich dadurch von allen anderen Körperzellen und warum ist das von Bedeutung?
1 6.2 Bitte zuordnen
Welcher Begriff gehört zu welcher Beschreibung?
A. | Proteasom | i. | verdrängt die konstitutiven β-Untereinheiten der katalytischen Kammer als Reaktion auf Interferone |
B. | 20S-Core-Komplex | ii. | besteht aus einem katalytischen Core-Komplex und zwei regulatorischen 19S-Cap-Komplexen |
C. | LMP2, LMP7, MECL-1 | iii. | großer zylindrischer Komplex aus 28 Untereinheiten, die in vier gestapelten Ringen angeordnet sind |
D. | PA28 | iv. | markiert Proteine für den Abbau |
E. | Lysin-48-Ubiquitin | v. | bindet an das Proteasom und erhöht die Freisetzungsrate der Peptide aus dem Proteasom |
1 6.3 Richtig oder falsch
Die Oberflächenexpression von MHC-Klasse-I-Molekülen wird von der Transportkapazität der Zelle für Peptide in das endoplasmatische Reticulum nicht beeinflusst.
1 6.4 Bitte ergänzen
Polypeptide, die für die Zellmembran bestimmt sind, werden in das Lumen des endoplasmatischen Reticulums transloziert, was jedoch verwirrend ist, da die von MHC-Klasse-Molekülen-I präsentierten Peptide im ________ vorkommen. Weitere Untersuchungen zeigten, dass die Präsentation der cytosolischen Peptide von einer Familie von ABC-Transportproteinen (________) ermöglicht wird, die den ATP-abhängigen Transport von Peptiden in das Lumen des ________ bewerkstelligen. Dieser Transporterkomplex besitzt nur eine begrenzte Spezifität für die transportierten Peptide; so sind beispielsweise die Peptide im Allgemeinen ________ Aminosäuren lang und der Transport wird bei ________ Resten im Carboxyterminus begünstigt und bei ________ Resten in den ersten ________ aminoterminalen Aminosäuren gehemmt.
1 6.5 Multiple Choice
Dendritische CD8-Zellen besitzen die besondere Eigenschaft, Antigene sehr effektiv in Form einer Kreuzpräsentation darzubieten. Welche der folgenden Kombinationen beinhaltet einen Transkriptionsfaktor, der für die Entwicklung der dendritischen CD8-Zellen essenziell ist, und einen nur von diesen Zellen exprimierten Oberflächenmarker?
-
A.
CIITA, CD74
-
B.
BATF3, CD4
-
C.
CIITA, CD94
-
D.
BATF3, XCR1
1 6.6 Bitte zuordnen
Welcher Begriff gehört zu welcher Beschreibung?
A. | TRIC | i. | hält die α-Kette der MHC-Klasse-I-Moleküle in einem teilweise gefalteten Zustand |
B. | ERAAP | ii. | schützt Peptide, die im Cytosol erzeugt werden, vor einem vollständigen Abbau |
C. | Calnexin | iii. | bildet eine Brücke zwischen dem MHC-Klasse-I-Molekül und dem TAP-Komplex |
D. | ERp57 | iv. | verkürzt den Aminoterminus von Peptiden, die für eine Bindung durch MHC zu lang sind |
E. | Tapasin | v. | öffnet und schließt während der Peptidbeladung Disulfidbrücken in der MHC-Klasse-I-α-Domäne |
1 6.7 Richtig oder falsch
MHC-Klasse-II-Moleküle präsentieren keine cytosolischen Antigene.
1 6.8 Bitte zuordnen
In welcher Reihenfolge geht die MHC-Klasse-II-Prozessierung in einer antigenpräsentierenden Zelle vor sich?
_____ Abspaltung der Trimerisierungsdomäne CD74
_____ Translokation des MHC-Klasse-II-Moleküls in das endoplasmatische Reticulum
_____ Cathepsin S spaltet LIP22 und das CLIP-Fragment verbleibt auf dem MHC-Molekül
_____ CD74-Trimere binden nichtkovalent an MHC-Klasse-II-α:β-Heterodimere
_____ HLA-DM katalysiert die Freisetzung von CLIP und stimuliert das Peptid-Editing
_____ Calnexin setzt MHC-Klasse-II-Heterodimere für den Transport zu einem endosomalen Kompartiment mit niedrigem pH-Wert frei
1 6.9 Multiple Choice
Bei welchem der folgenden Proteine führt eine Funktionsstörung dazu, dass kein Priming von CD8-T-Zellen mehr möglich ist?
-
A.
HLA-DM
-
B.
Cathepsin S
-
C.
TAP1/2
-
D.
CD74
1 6.10 Multiple Choice
Eine Funktionsstörung in welchem der folgenden Proteine führt dazu, dass die Präsentation cytosolischer Peptide durch MHC-Klasse-II-Moleküle reduziert ist?
-
A.
IRGM3
-
B.
BATF3
-
C.
MARCH-1
-
D.
TAP1/2
1 6.11 Richtig oder falsch
Superantigene induzieren keine adaptive Immunantwort und wirken unabhängig von peptidspezifischen MHC-TCR-Wechselwirkungen?
1 6.12 Multiple Choice
Welche der folgenden Aussagen ist falsch?
-
A.
Polymorphismen an jedem Locus können potenziell die Anzahl der verschiedenen MHC-Moleküle verdoppeln, die ein Individuum exprimieren kann.
-
B.
Pathogene können dem Immunsystem entkommen, indem das immundominante Epitop mutiert, wodurch die Affinität des zugehörigen MHC-Allel-Produkts verlorengeht.
-
C.
Pathogene verursachen keinen Evolutionsdruck zur Selektion von MHC-Allelen, die einen Schutz gegenüber diesen Pathogenen bewirken.
-
D.
Die DRα-Kette und das homologe Protein der Maus Eα sind monomorph.
1 6.13 Richtig oder falsch
Klassische MHC-Klasse-I-Moleküle sind hochgradig polymorph, während MHC-Klasse-Ib-Moleküle oligomorph sind.
1 6.14 Bitte zuordnen
Welche Beschreibung gehört zu welchem MHC-Klasse-Ib-Molekül?
A. | H2-M3 | i. | präsentiert mikrobielle Folsäuremetaboliten |
B. | MIC-A | ii. | bindet α-GalCer |
C. | CD1d | iii. | präsentiert N-formylierte Peptide |
D. | MR1 | iv. | bindet NKG2D |
Literatur
1.1 Allgemeine Literatur
-
■ Germain, R.N.: MHC-dependent antigen processing and peptide presentation: providing ligands for T lymphocyte activation. Cell 1994, 76:287–299.
-
■ Klein, J.: Natural History of the Major Histocompatibility Complex. New York: Wiley, 1986.
-
■ Moller, G. (ed.): Origin of major histocompatibility complex diversity. Immunol. Rev. 1995, 143:5–292.
-
■ Trombetta, E.S. and Mellman, I.: Cell biology of antigen processing in vitro and in vivo. Annu. Rev. Immunol. 2005, 23:975–1028.
1.2 Literatur zu den einzelnen Abschnitten
1.2.1 Abschnitt 6.1.1
-
■ Guermonprez, P., Valladeau, J., Zitvogel, L., Théry, C., and Amigorena, S.: Antigen presentation and T cell stimulation by dendritic cells. Annu. Rev. Immunol. 2002, 20:621–667.
-
■ Lee, H.K., Mattei, L.M., Steinberg, B.E., Alberts, P., Lee, Y.H., Chervonsky, A., Mizushima, N., Grinstein, S., and Iwasaki, A.: In vivo requirement for Atg5 in antigen presentation by dendritic cells. Immunity 2010, 32:227–239.
-
■ Segura, E. and Villadangos, J.A.: Antigen presentation by dendritic cells in vivo. Curr. Opin. Immunol. 2009, 21:105–110.
-
■ Vyas, J.M., Van der Veen, A.G., and Ploegh, H.L.: The known unknowns of anti-gen processing and presentation. Nat. Rev. Immunol. 2008, 8:607–618.
1.2.2 Abschnitt 6.1.2
-
■ Basler, M., Kirk. C.J., and Groettrup, M.: The immunoproteasome in antigen processing and other immunological functions. Curr. Opin. Immunol. 2013, 25:74–80.
-
■ Brocke, P., Garbi, N., Momburg, F., and Hammerling, G.J.: HLA-DM, HLA-DO and tapasin: functional similarities and differences. Curr. Opin. Immunol. 2002, 14:22–29.
-
■ Cascio, P., Call, M., Petre, B.M., Walz, T., and Goldberg, A.L.: Properties of the hybrid form of the 26S proteasome containing both 19S and PA28 complexes. EMBO J. 2002, 21:2636–2645.
-
■ Gromme, M. and Neefjes, J.: Antigen degradation or presentation by MHC class I molecules via classical and non-classical pathways. Mol. Immunol. 2002, 39:181–202.
-
■ Goldberg, A.L., Cascio, P., Saric, T., and Rock, K.L.: The importance of the proteasome and subsequent proteolytic steps in the generation of antigenic peptides. Mol. Immunol. 2002, 39:147–164.
-
■ Hammer, G.E., Gonzalez, F., Champsaur, M., Cado, D., and Shastri, N.: The aminopeptidase ERAAP shapes the peptide repertoire displayed by major histocompatibility complex class I molecules. Nat. Immunol. 2006, 7:103–112.
-
■ Hammer, G.E., Gonzalez, F., James, E., Nolla, H., and Shastri, N.: In the absence of aminopeptidase ERAAP, MHC class I molecules present many unstable and highly immunogenic peptides. Nat. Immunol. 2007, 8:101–108.
-
■ Murata, S., Sasaki, K., Kishimoto, T., Niwa, S., Hayashi, H., Takahama, Y., and Tanaka, K.: Regulation of CD8+ T cell development by thymus-specific proteasomes. Science 2007, 316:1349–1353.
-
■ Schubert, U., Anton, L.C., Gibbs, J., Norbury, C.C., Yewdell, J.W., and Bennink, J.R.: Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature 2000, 404:770–774.
-
■ Serwold, T., Gonzalez, F., Kim, J., Jacob, R., and Shastri, N.: ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum. Nature 2002, 419:480–483.
-
■ Shastri, N., Schwab, S., and Serwold, T.: Producing nature’s gene-chips: the generation of peptides for display by MHC class I molecules. Annu. Rev. Immunol. 2002, 20:463–493.
-
■ Sijts, A., Sun, Y., Janek, K., Kral, S., Paschen, A., Schadendorf, D., and Kloetzel, P.M.: The role of the proteasome activator PA28 in MHC class I antigen processing. Mol. Immunol. 2002, 39:165–169.
-
■ Vigneron, N., Stroobant, V., Chapiro, J., Ooms, A., Degiovanni, G., Morel, S., van der Bruggen, P., Boon, T., and Van den Eynde, B.J.: An antigenic peptide produced by peptide splicing in the proteasome. Science 2004, 304:587–590.
-
■ Villadangos, J.A.: Presentation of antigens by MHC class II molecules: getting the most out of them. Mol. Immunol. 2001, 38:329–346.
-
■ Williams, A., Peh, C.A., and Elliott, T.: The cell biology of MHC class I antigen presentation. Tissue Antigens 2002, 59:3–17.
1.2.3 Abschnitt 6.1.3
-
■ Gorbulev, S., Abele, R., and Tampe, R.: Allosteric crosstalk between peptide-binding, transport, and ATP hydrolysis of the ABC transporter TAP. Proc. Natl Acad. Sci. USA 2001, 98:3732–3737.
-
■ Kelly, A., Powis, S.H., Kerr, L.A., Mockridge, I., Elliott, T., Bastin, J., Uchanska-Ziegler, B., Ziegler, A., Trowsdale, J., and Townsend, A.: Assembly and function of the two ABC transporter proteins encoded in the human major histocompatibility complex. Nature 1992, 355:641–644.
-
■ Lankat-Buttgereit, B. and Tampe, R.: The transporter associated with anti-gen processing: function and implications in human diseases. Physiol. Rev. 2002, 82:187–204.
-
■ Powis, S.J., Townsend, A.R., Deverson, E. V., Bastin, J., Butcher, G.W., and Howard, J.C.: Restoration of antigen presentation to the mutant cell line RMA-S by an MHC-linked transporter. Nature 1991, 354:528–531.
-
■ Townsend, A., Ohlen, C., Foster, L., Bastin, J., Lunggren, H.G., and Karre, K.: A mutant cell in which association of class I heavy and light chains is induced by viral peptides. Cold Spring Harbor Symp. Quant. Biol. 1989, 54:299–308.
1.2.4 Abschnitt 6.1.4
-
■ Bouvier, M.: Accessory proteins and the assembly of human class I MHC molecules: a molecular and structural perspective. Mol. Immunol. 2003, 39:697–706.
-
■ Gao, B., Adhikari, R., Howarth, M., Nakamura, K., Gold, M.C., Hill, A.B., Knee, R., Michalak, M., and Elliott, T.: Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin. Immunity 2002, 16:99–109.
-
■ Grandea III, A.G. and Van Kaer, L.: Tapasin: an ER chaperone that controls MHC class I assembly with peptide. Trends Immunol. 2001, 22:194–199.
-
■ Van Kaer, L.: Accessory proteins that control the assembly of MHC molecules with peptides. Immunol. Res. 2001, 23:205–214.
-
■ Williams, A., Peh, C.A., and Elliott, T.: The cell biology of MHC class I antigen presentation. Tissue Antigens 2002, 59:3–17.
-
■ Williams, A.P., Peh, C.A., Purcell, A.W., McCluskey, J., and Elliott, T.: Optimization of the MHC class I peptide cargo is dependent on tapasin. Immunity 2002, 16:509–520.
-
■ Zhang, W., Wearsch, P.A., Zhu, Y., Leonhardt, R.M., and Cresswell P.: A role for UDP-glucose glycoprotein glucosyltransferase in expression and quality control of MHC class I molecules. Proc. Natl Acad. Sci. USA 2011, 108:4956–4961.
1.2.5 Abschnitt 6.1.5
-
■ Ackerman, A.L. and Cresswell, P.: Cellular mechanisms governing cross-presentation of exogenous antigens. Nat. Immunol. 2004, 5:678–684.
-
■ Bevan, M.J.: Minor H antigens introduced on H-2 different stimulating cells cross-react at the cytotoxic T cell level during in vivo priming. J. Immunol. 1976, 117:2233–2238.
-
■ Bevan, M.J.: Helping the CD8+ T cell response. Nat. Rev. Immunol. 2004, 4:595–602.
-
■ Hildner, K., Edelson, B.T., Purtha, W.E., Diamond, M., Matsushita, H., Kohyama, M., Calderon, B., Schraml, B.U., Unanue, E.R., Diamond, M.S., et al.: Batf3 deficiency reveals a critical role for CD8α+ dendritic cells in cytotoxic T cell immunity. Science 2008, 322:1097–1100.
-
■ Segura, E. and Villadangos, J.A.: A modular and combinatorial view of the antigen cross-presentation pathway in dendritic cells. Traffic 2011, 12:1677–1685.
1.2.6 Abschnitt 6.1.6
-
■ Dengjel, J., Schoor, O., Fischer, R., Reich, M., Kraus, M., Müller, M., Kreymborg, K., Altenberend, F., Brandenburg, J., Kalbacher, H., et al.: Autophagy promotes MHC class II presentation of peptides from intracellular source proteins. Proc. Natl Acad. Sci. USA 2005, 102:7922–7927.
-
■ Deretic, V., Saitoh, T., and Akira, S.: Autophagy in infection, inflammation and immunity. Nat. Rev. Immunol. 2013, 13:722–737.
-
■ Godkin, A.J., Smith, K.J., Willis, A., Tejada-Simon, M.V., Zhang, J., Elliott, T., and Hill, A.V.: Naturally processed HLA class II peptides reveal highly conserved immunogenic flanking region sequence preferences that reflect antigen processing rather than peptide–MHC interactions. J. Immunol. 2001, 166:6720–6727.
-
■ Hiltbold, E.M. and Roche, P.A.: Trafficking of MHC class II molecules in the late secretory pathway. Curr. Opin. Immunol. 2002, 14:30–35.
-
■ Hsieh, C.S., deRoos, P., Honey, K., Beers, C., and Rudensky, A.Y.: A role for cathepsin L and cathepsin S in peptide generation for MHC class II presentation. J. Immunol. 2002, 168:2618–2625.
-
■ Lennon-Duménil, A.M., Bakker, A.H., Wolf-Bryant, P., Ploegh, H.L., and Lagaudrière-Gesbert, C.: A closer look at proteolysis and MHC-class-II-restricted antigen presentation. Curr. Opin. Immunol. 2002, 14:15–21.
-
■ Li, P., Gregg, J.L., Wang, N., Zhou, D., O’Donnell, P., Blum, J.S., and Crotzer, V.L.: Compartmentalization of class II antigen presentation: contribution of cytoplasmic and endosomal processing. Immunol. Rev. 2005, 207:206–217.
-
■ Maric, M., Arunachalam, B., Phan, U.T., Dong, C., Garrett, W.S., Cannon, K.S., Alfonso, C., Karlsson, L., Flavell, R.A., and Cresswell, P.: Defective antigen processing in GILT-free mice. Science 2001, 294:1361–1365.
-
■ Münz, C.: Enhancing immunity through autophagy. Annu. Rev. Immunol. 2009, 27:423–449.
-
■ Pluger, E.B., Boes, M., Alfonso, C., Schroter, C.J., Kalbacher, H., Ploegh, H.L., and Driessen, C.: Specific role for cathepsin S in the generation of antigenic peptides in vivo. Eur. J. Immunol. 2002, 32:467–476.
1.2.7 Abschnitt 6.1.7
-
■ Gregers, T.F., Nordeng, T.W., Birkeland, H.C., Sandlie, I., and Bakke, O.: The cytoplasmic tail of invariant chain modulates antigen processing and presentation. Eur. J. Immunol. 2003, 33:277–286.
-
■ Hiltbold, E.M. and Roche, P.A.: Trafficking of MHC class II molecules in the late secretory pathway. Curr. Opin. Immunol. 2002, 14:30–35.
-
■ Kleijmeer, M., Ramm, G., Schuurhuis, D., Griffith, J., Rescigno, M., Ricciardi-Castagnoli, P., Rudensky, A.Y., Ossendorp, F., Melief, C.J., Stoorvogel, W., et al.: Reorganization of multivesicular bodies regulates MHC class II antigen presentation by dendritic cells. J. Cell Biol. 2001, 155:53–63.
-
■ van Lith, M., van Ham, M., Griekspoor, A., Tjin, E., Verwoerd, D., Calafat, J., Janssen, H., Reits, E., Pastoors, L., and Neefjes, J.: Regulation of MHC class II antigen presentation by sorting of recycling HLA-DM/DO and class II within the multivesicular body. J. Immunol. 2001, 167:884–892.
1.2.8 Abschnitt 6.1.8
-
■ Alfonso, C. and Karlsson, L.: Nonclassical MHC class II molecules. Annu. Rev. Immunol. 2000, 18:113–142.
-
■ Apostolopoulos, V., McKenzie, I.F., and Wilson, I. A.: Getting into the groove: unusual features of peptide binding to MHC class I molecules and implications in vaccine design. Front. Biosci. 2001, 6:D1311–D1320.
-
■ Buslepp, J., Zhao, R., Donnini, D., Loftus, D., Saad, M., Appella, E., and Collins, E.J.: T cell activity correlates with oligomeric peptide-major histocompatibility complex binding on T cell surface. J. Biol. Chem. 2001, 276:47320–47328.
-
■ Gu, Y., Jensen, P.E., and Chen, X.: Immunodeficiency and autoimmunity in H2-O-deficient mice. J. Immunol. 2013, 190:126–137.
-
■ Hill, J.A., Wang, D., Jevnikar, A.M., Cairns, E., and Bell, D.A.: The relationship between predicted peptide-MHC class II affinity and T-cell activation in a HLA-DRβ1*0401 transgenic mouse model. Arthritis Res. Ther. 2003, 5:R40–R48.
-
■ Mellins, E.D. and Stern, L.J.: HLA-DM and HLA-DO, key regulators of MHC-II processing and presentation. Curr. Opin. Immunol. 2014, 26:115–122.
-
■ Nelson, C.A., Vidavsky, I., Viner, N.J., Gross, M.L., and Unanue, E.R.: Amino-terminal trimming of peptides for presentation on major histocompatibility complex class II molecules. Proc. Natl Acad. Sci. USA 1997, 94:628–633.
-
■ Pathak, S.S., Lich, J.D., and Blum, J.S.: Cutting edge: editing of recycling class II:peptide complexes by HLA-DM. J. Immunol. 2001, 167:632–635.
-
■ Pos, W., Sethi, D.K., Call, M.J., Schulze, M.S., Anders, A.K., Pyrdol, J., and Wucherpfennig, K.W.: Crystal structure of the HLA-DM-HLA-DR1 complex defines mechanisms for rapid peptide selection. Cell 2012, 151:1557–1568.
-
■ Qi, L. and Ostrand-Rosenberg, S.: H2-O inhibits presentation of bacterial superantigens, but not endogenous self antigens. J. Immunol. 2001, 167:1371–1378.
-
■ Su, R.C. and Miller, R.G.: Stability of surface H-2Kb, H-2Db, and peptide-receptive H-2Kb on splenocytes. J. Immunol. 2001, 167:4869–4877.
-
■ Zarutskie, J.A., Busch, R., Zavala-Ruiz, Z., Rushe, M., Mellins, E.D., and Stern, L.J.: The kinetic basis of peptide exchange catalysis by HLA-DM. Proc. Natl Acad. Sci. USA 2001, 98:12450–12455.
1.2.9 Abschnitt 6.1.9
-
■ Baravalle, G., Park, H., McSweeney, M., Ohmura-Hoshino, M., Matsuki, Y., Ishido, S., and Shin, J.S.: Ubiquitination of CD86 is a key mechanism in regulating anti-gen presentation by dendritic cells. J. Immunol. 2011, 187:2966–2973.
-
■ De Gassart, A., Camosseto, V., Thibodeau, J., Ceppi, M., Catalan, N., Pierre, P., and Gatti, E.: MHC class II stabilization at the surface of human dendritic cells is the result of maturation-dependent MARCH I down-regulation. Proc. Natl Acad. Sci. USA 2008, 105:3491–3496.
-
■ Jiang, X. and Chen, Z.J.: The role of ubiquitylation in immune defence and pathogen evasion. Nat. Rev. Immunol. 2012, 12:35–48.
-
■ Ma, J.K., Platt, M.Y., Eastham-Anderson, J., Shin, J.S., and Mellman, I.: MHC class II distribution in dendritic cells and B cells is determined by ubiquitin chain length. Proc. Natl Acad. Sci. USA 2012, 109:8820–8827.
-
■ Ohmura-Hoshino, M., Matsuki, Y., Mito-Yoshida, M., Goto, E., Aoki-Kawasumi, M., Nakayama, M., Ohara, O., and Ishido, S.: Cutting edge: requirement of MARCH-I-mediated MHC II ubiquitination for the maintenance of conventional dendritic cells. J. Immunol. 2009, 183:6893–6897.
-
■ Walseng, E., Furuta, K., Bosch, B., Weih, K. A., Matsuki, Y., Bakke, O., Ishido, S., and Roche, P.A.: Ubiquitination regulates MHC class II-peptide complex retention and degradation in dendritic cells. Proc. Natl Acad. Sci. USA 2010, 107:20465–20470.
1.2.10 Abschnitt 6.2.1
-
■ Aguado, B., Bahram, S., Beck, S., Campbell, R.D., Forbes, S.A., Geraghty, D., Guillaudeux, T., Hood, L., Horton, R., Inoko, H., et al. (the MHC Sequencing Consortium): Complete sequence and gene map of a human major histocom-patibility complex. Nature 1999, 401:921–923.
-
■ Chang, C.H., Gourley, T.S., and Sisk, T.J.: Function and regulation of class II transactivator in the immune system. Immunol. Res. 2002, 25:131–142.
-
■ Kumnovics, A., Takada, T., and Lindahl, K.F.: Genomic organization of the mammalian MHC. Annu. Rev. Immunol. 2003, 21:629–657.
-
■ Lefranc, M.P.: IMGT, the international ImMunoGeneTics database. Nucleic Acids Res. 2003, 31:307–310.
1.2.11 Abschnitt 6.2.2
-
■ Gaur, L.K. and Nepom, G.T.: Ancestral major histocompatibility complex DRB genes beget conserved patterns of localized polymorphisms. Proc. Natl Acad. Sci. USA 1996, 93:5380–5383.
-
■ Marsh, S.G.: Nomenclature for factors of the HLA system, update December 2002. Eur. J. Immunogenet. 2003, 30:167–169.
-
■ Robinson, J. and Marsh, S.G.: HLA informatics. Accessing HLA sequences from sequence databases. Methods Mol. Biol. 2003, 210:3–21.
1.2.12 Abschnitt 6.2.3
-
■ Falk, K., Rotzschke, O., Stevanovic, S., Jung, G., and Rammensee, H.G.: Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules. Nature 1991, 351:290–296.
-
■ Garcia, K.C., Degano, M., Speir, J.A., and Wilson, I. A.: Emerging principles for T cell receptor recognition of antigen in cellular immunity. Rev. Immunogenet. 1999, 1:75–90.
-
■ Katz, D.H., Hamaoka, T., Dorf, M. E., Maurer, P.H., and Benacerraf, B.: Cell interactions between histoincompatible T and B lymphocytes. IV. Involvement of immune response (Ir) gene control of lymphocyte interaction controlled by the gene. J. Exp. Med. 1973, 138:734–739.
-
■ Kjer-Nielsen, L., Clements, C.S., Brooks, A.G., Purcell, A.W., Fontes, M.R., McCluskey, J., and Rossjohn, J.: The structure of HLA-B8 complexed to an immunodominant viral determinant: peptide-induced conformational changes and a mode of MHC class I dimerization. J. Immunol. 2002, 169:5153–5160.
-
■ Wang, J.H. and Reinherz, E.L.: Structural basis of T cell recognition of peptides bound to MHC molecules. Mol. Immunol. 2002, 38:1039–1049.
-
■ Zinkernagel, R.M. and Doherty, P.C.: Restriction of in vivo T-cell mediated cytotoxicity in lymphocytic choriomeningitis within a syngeneic or semiallogeneic system. Nature 1974, 248:701–702.
1.2.13 Abschnitt 6.2.4
-
■ Felix, N.J. and Allen, P.M.: Specificity of T-cell alloreactivity. Nat. Rev. Immunol. 2007, 7:942–953.
-
■ Feng, D., Bond, C.J., Ely, L.K., Maynard, J., and Garcia, K.C.: Structural evidence for a germline-encoded T cell receptor–major histocompatibility complex interaction ‘codon.’ Nat. Immunol. 2007, 8:975–993.
-
■ Hennecke, J. and Wiley, D.C.: Structure of a complex of the human α/β T cell receptor (TCR) HA1.7, influenza hemagglutinin peptide, and major histocom-patibility complex class II molecule, HLA-DR4 (DRA*0101 and DRB1*0401): insight into TCR cross-restriction and alloreactivity. J. Exp. Med. 2002, 195:571–581.
-
■ Jankovic, V., Remus, K., Molano, A., and Nikolich-Zugich, J.: T cell recognition of an engineered MHC class I molecule: implications for peptide-independent alloreactivity. J. Immunol. 2002, 169:1887–1892.
-
■ Nesic, D., Maric, M., Santori, F.R., and Vukmanovic, S.: Factors influencing the patterns of T lymphocyte allorecognition. Transplantation 2002, 73:797–803.
-
■ Reiser, J.B., Darnault, C., Guimezanes, A., Gregoire, C., Mosser, T., Schmitt-Verhulst, A.M., Fontecilla-Camps, J.C., Malissen, B., Housset, D., and Mazza, G.: Crystal structure of a T cell receptor bound to an allogeneic MHC molecule. Nat. Immunol. 2000, 1:291–297.
-
■ Rötzschke, O., Falk, K., Faath, S., Rammensee, H.G.: On the nature of peptides involved in T cell alloreactivity. J. Exp. Med. 1991, 174:1059–1071.
-
■ Speir, J.A., Garcia, K.C., Brunmark, A., Degano, M., Peterson, P.A., Teyton, L., and Wilson, I. A.: Structural basis of 2C TCR allorecognition of H-2Ld peptide complexes. Immunity 1998, 8:553–562.
1.2.14 Abschnitt 6.2.5
-
■ Acha-Orbea, H., Finke, D., Attinger, A., Schmid, S., Wehrli, N., Vacheron, S., Xenarios, I., Scarpellino, L., Toellner, K.M., MacLennan, I.C., et al.: Interplays between mouse mammary tumor virus and the cellular and humoral immune response. Immunol. Rev. 1999, 168:287–303.
-
■ Kappler, J.W., Staerz, U., White, J., and Marrack, P.: T cell receptor Vb elements which recognize Mls-modified products of the major histocompatibility complex. Nature 1988, 332:35–40.
-
■ Rammensee, H.G., Kroschewski, R., and Frangoulis, B.: Clonal anergy induced in mature Vβ6+ T lymphocytes on immunizing Mls-1b mice with Mls-1a expressing cells. Nature 1989, 339:541–544.
-
■ Spaulding, A.R., Salgado-Pabón, W., Kohler, P.L., Horswill, A.R., Leung, D.Y., and Schlievert, P.M.: Staphylococcal and streptococcal superantigen exotoxins. Clin. Microbiol. Rev. 2013, 26:422–447.
-
■ Sundberg, E.J., Li, H., Llera, A.S., McCormick, J.K., Tormo, J., Schlievert, P.M., Karjalainen, K., and Mariuzza, R.A.: Structures of two streptococcal superantigens bound to TCR β chains reveal diversity in the architecture of T cell signaling complexes. Structure 2002, 10:687–699.
-
■ Torres, B.A., Perrin, G.Q., Mujtaba, M.G., Subramaniam, P.S., Anderson, A.K., and Johnson, H.M.: Superantigen enhancement of specific immunity: antibody production and signaling pathways. J. Immunol. 2002, 169:2907–2914.
-
■ White, J., Herman, A., Pullen, A.M., Kubo, R., Kappler, J.W., and Marrack, P.: The Vβ-specific super antigen staphylococcal enterotoxin B: stimulation of mature T cells and clonal deletion in neonatal mice. Cell 1989, 56:27–35.
1.2.15 Abschnitt 6.2.6
-
■ Hill, A.V., Elvin, J., Willis, A.C., Aidoo, M., Allsopp, C.E.M., Gotch, F.M., Gao, X.M., Takiguchi, M., Greenwood, B.M., Townsend, A.R.M., et al.: Molecular anal-ysis of the association of B53 and resistance to severe malaria. Nature 1992, 360:435–440.
-
■ Martin, M.P. and Carrington, M.: Immunogenetics of viral infections. Curr. Opin. Immunol. 2005, 17:510–516.
-
■ Messaoudi, I., Guevara Patino, J.A., Dyall, R., LeMaoult, J., and Nikolich-Zugich, J.: Direct link between mhc polymorphism, T cell avidity, and diversity in immune defense. Science 2002, 298:1797–1800.
-
■ Potts, W.K. and Slev, P.R.: Pathogen-based models favouring MHC genetic diversity. Immunol. Rev. 1995, 143:181–197.
1.2.16 Abschnitt 6.3.1
-
■ Alfonso, C. and Karlsson, L.: Nonclassical MHC class II molecules. Annu. Rev. Immunol. 2000, 18:113–142.
-
■ Hofstetter, A.R., Sullivan, L.C., Lukacher, A.E., and Brooks, A.G..: Diverse roles of non-diverse molecules: MHC class Ib molecules in host defense and control of autoimmunity. Curr. Opin. Immunol. 2011, 23:104–110.
-
■ Loconto, J., Papes, F., Chang, E., Stowers, L., Jones, E.P., Takada, T., Kumánovics, A., Fischer Lindahl, K., and Dulac, C.: Functional expression of murine V2R pheromone receptors involves selective association with the M10 and M1 families of MHC class Ib molecules. Cell 2003, 112:607–118.
-
■ Powell, L.W., Subramaniam, V.N., and Yapp, T.R.: Haemochromatosis in the new millennium. J. Hepatol. 2000, 32:48–62.
1.2.17 Abschnitt 6.3.2
-
■ Borrego, F., Kabat, J., Kim, D.K., Lieto, L., Maasho, K., Pena, J., Solana, R., and Coligan, J.E.: Structure and function of major histocompatibility complex (MHC) class I specific receptors expressed on human natural killer (NK) cells. Mol. Immunol. 2002, 38:637–660.
-
■ Boyington, J.C., Riaz, A.N., Patamawenu, A., Coligan, J.E., Brooks, A.G., and Sun, P.D.: Structure of CD94 reveals a novel C-type lectin fold: implications for the NK cell-associated CD94/NKG2 receptors. Immunity 1999, 10:75–82.
-
■ Braud, V.M., Allan, D.S., O’Callaghan, C.A., Söderström, K., D’Andrea, A., Ogg, G.S., Lazetic, S., Young, N.T., Bell, J.I., Phillips, J.H., et al.: HLA-E binds to natural killer cell receptors CD94/NKG2A, B and C. Nature 1998, 391:795–799.
-
■ Braud, V.M. and McMichael, A.J.: Regulation of NK cell functions through interaction of the CD94/NKG2 receptors with the nonclassical class I molecule HLA-E. Curr. Top. Microbiol. Immunol. 1999, 244:85–95.
-
■ Jiang, H., Canfield, S.M., Gallagher, M.P., Jiang, H.H., Jiang, Y., Zheng, Z., and Chess, L.: HLA-E-restricted regulatory CD8(+) T cells are involved in development and control of human autoimmune type 1 diabetes. J. Clin. Invest. 2010, 120:3641–3650.
-
■ Lanier, L.L.: NK cell recognition. Annu. Rev. Immunol. 2005, 23:225–274.
-
■ Lopez-Botet, M., and Bellon, T.: Natural killer cell activation and inhibition by receptors for MHC class I. Curr. Opin. Immunol. 1999, 11:301–307.
-
■ Lopez-Botet, M. Bellon, T., Llano, M., Navarro, F., Garcia, P., and de Miguel, M.: Paired inhibitory and triggering NK cell receptors for HLA class I molecules. Hum. Immunol. 2000, 61:7–17.
-
■ Lopez-Botet, M., Llano, M., Navarro, F., and Bellon, T.: NK cell recognition of non-classical HLA class I molecules. Semin. Immunol. 2000, 12:109–119.
-
■ Lu, L., Ikizawa, K., Hu, D., Werneck, M.B., Wucherpfennig, K.W., and Cantor, H.: Regulation of activated CD4+ T cells by NK cells via the Qa-1-NKG2A inhibitory pathway. Immunity 2007, 26:593–604.
-
■ Pietra, G., Romagnani, C., Moretta, L., and Mingari, M.C.: HLA-E and HLA-E-bound peptides: recognition by subsets of NK and T cells. Curr. Pharm. Des. 2009, 15:3336–3344.
-
■ Rodgers, J.R. and Cook, R.G.: MHC class Ib molecules bridge innate and acquired immunity. Nat. Rev. Immunol. 2005, 5:459–471.
1.2.18 Abschnitt 6.3.3
-
■ Gendzekhadze, K., Norman, P.J., Abi-Rached, L., Graef, T., Moesta, A.K., Layrisse, Z., and Parham, P.: Co-evolution of KIR2DL3 with HLA-C in a human population retaining minimal essential diversity of KIR and HLA class I ligands. Proc. Natl Acad. Sci. USA 2009, 106:18692–18697.
-
■ Godfrey, D.I., Stankovic, S., and Baxter, A.G.: Raising the NKT cell family. Nat. Immunol. 2010, 11:197–206.
-
■ Hava, D.L., Brigl, M., van den Elzen, P., Zajonc, D.M., Wilson, I. A., and Brenner, M.B.: CD1 assembly and the formation of CD1-antigen complexes. Curr. Opin. Immunol. 2005, 17:88–94.
-
■ Moody, D.B. and Besra, G.S.: Glycolipid targets of CD1-mediated T-cell responses. Immunology 2001, 104:243–251.
-
■ Moody, D.B. and Porcelli, S.A.: CD1 trafficking: invariant chain gives a new twist to the tale. Immunity 2001, 15:861–865.
-
■ Moody, D.B. and Porcelli, S.A.: Intracellular pathways of CD1 antigen presentation. Nat. Rev. Immunol. 2003, 3:11–22.
-
■ Scharf, L., Li, N.S., Hawk, A.J., Garzón, D., Zhang, T., Fox, L.M., Kazen, A.R., Shah, S., Haddadian, E.J., Gumperz, J.E., et al.: The 2.5 Å structure of CD1c in complex with a mycobacterial lipid reveals an open groove ideally suited for diverse antigen presentation. Immunity 2010, 33:853–862.
-
■ Schiefner, A., Fujio, M., Wu, D., Wong, C.H., and Wilson, I. A.: Structural evaluation of potent NKT cell agonists: implications for design of novel stimulatory ligands. J. Mol. Biol. 2009, 394:71–82.
1.2.19 Abschnitt 6.3.4
-
■ Birkinshaw, R.W., Kjer-Nielsen, L., Eckle, S.B., McCluskey, J., and Rossjohn, J.: MAITs, MR1 and vitamin B metabolites. Curr. Opin. Immunol. 2014, 26:7–13.
-
■ Kjer-Nielsen, L., Patel, O., Corbett, A.J., Le Nours, J., Meehan, B., Liu, L., Bhati, M., Chen, Z., Kostenko, L., Reantragoon, R., et al.: MR1 presents microbial vitamin B metabolites to MAIT cells. Nature 2012, 491:717–723.
-
■ López-Sagaseta, J., Dulberger, C.L., Crooks, J.E., Parks, C.D., Luoma, A.M., McFedries, A., Van Rhijn, I., Saghatelian, A., and Adams, E.J.: The molecular basis for Mucosal-Associated Invariant T cell recognition of MR1 proteins. Proc. Natl Acad. Sci. USA 2013, 110:E1771–1778.
1.2.20 Abschnitt 6.3.5
-
■ Chien, Y.H., Meyer, C., and Bonneville, M.: γδ T cells: first line of defense and beyond. Annu. Rev. Immunol. 2014, 32:121–155.
-
■ Turchinovich, G. and Hayday, A.C.: Skint-1 identifies a common molecular mechanism for the development of interferon-γ-secreting versus interleukin-17-secreting γδ T cells. Immunity 2011, 35:59–68.
-
■ Uldrich, A.P., Le Nours, J., Pellicci, D.G., Gherardin, N.A., McPherson, K.G., Lim, R.T., Patel, O., Beddoe, T., Gras, S., Rossjohn, J., et al.: CD1d-lipid antigen recognition by the γδ TCR. Nat. Immunol. 2013, 14:1137–1145.
-
■ Willcox, C.R., Pitard, V., Netzer, S., Couzi, L., Salim, M., Silberzahn, T., Moreau, J.F., Hayday, A.C., Willcox, B.E., and Déchanet-Merville, J.: Cytomegalovirus and tumor stress surveillance by binding of a human γδ T cell antigen receptor to endothelial protein C receptor. Nat. Immunol. 2012, 13:872–879.
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Murphy, K., Weaver, C. (2018). Wie Antigene den T-Lymphocyten präsentiert werden. In: Janeway Immunologie. Springer Spektrum, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-56004-4_6
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