Pathogen evasion strategies for the major histocompatibility complex class I assembly pathway

被引:44
作者
Antoniou, Antony N. [2 ]
Powis, Simon J. [1 ]
机构
[1] Univ St Andrews, Bute Med Sch, St Andrews, Fife, Scotland
[2] UCL, Windeyer Inst Med Sci, Dept Immunol & Mol Pathol, Div Infect & Immun & Rheumatol, London W1T 4JF, England
关键词
biosynthesis; cross-presentation; ER associated degradation (ERAD); major histocompatibility complex class I (MHC class I); viral evasion;
D O I
10.1111/j.1365-2567.2008.02804.x
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
Major histocompatibility complex (MHC) class I molecules bind and present short antigenic peptides from endogenously or exogenously derived sources to CD8(+) cytotoxic T lymphocytes (CTL), with recognition of a foreign peptide normally targeting the cell for lysis. It is generally thought that the high level of MHC polymorphism, which is concentrated mostly within the peptide-binding groove, is driven by the 'evolutionary arms race' against pathogens. Many pathogens have developed novel and intriguing mechanisms for evading the continuous sampling of the intracellular and intercellular environments by MHC molecules, none more so than viruses. The characterization of immunoevasion mechanisms has improved our understanding of MHC biology. This review will highlight our current understanding of the MHC class I biosynthetic pathway and how it has been exploited by pathogens, especially viruses, to potentially evade CTL recognition.
引用
收藏
页码:1 / 12
页数:12
相关论文
共 128 条
[1]   The specificity of association of the IgD molecule with the accessory proteins BAP31/BAP29 lies in the IgD transmembrane sequence [J].
Adachi, T ;
Schamel, WWA ;
Kim, KM ;
Watanabe, T ;
Becker, B ;
Nielsen, PJ ;
Reth, M .
EMBO JOURNAL, 1996, 15 (07) :1534-1541
[2]   Molecular mechanism and species specificity of TAP inhibition by herpes simplex virus protein ICP47 [J].
Ahn, K ;
Meyer, TH ;
Uebel, S ;
Sempe, P ;
Djaballah, H ;
Yang, Y ;
Peterson, PA ;
Fruh, K ;
Tampe, R .
EMBO JOURNAL, 1996, 15 (13) :3247-3255
[3]   Human cytomegalovirus inhibits antigen presentation by a sequential multistep process [J].
Ahn, KS ;
Angulo, A ;
Ghazal, P ;
Peterson, PA ;
Yang, Y ;
Fruh, K .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (20) :10990-10995
[4]   IMPAIRED INTRACELLULAR-TRANSPORT OF CLASS-I MHC ANTIGENS AS A POSSIBLE MEANS FOR ADENOVIRUSES TO EVADE IMMUNE SURVEILLANCE [J].
ANDERSSON, M ;
PAABO, S ;
NILSSON, T ;
PETERSON, PA .
CELL, 1985, 43 (01) :215-222
[5]   Formation of HLA-B27 homodimers and their relationship to assembly kinetics [J].
Antoniou, AN ;
Ford, S ;
Taurog, JD ;
Butcher, GW ;
Powis, SJ .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (10) :8895-8902
[6]   Characterization of the ERp-57-tapasin complex by rapid cellular acidification and thiol modification [J].
Antoniou, AN ;
Powis, SJ .
ANTIOXIDANTS & REDOX SIGNALING, 2003, 5 (04) :375-379
[7]   Assembly and export of MHC class I peptide ligands [J].
Antoniou, AN ;
Powis, SJ ;
Elliott, T .
CURRENT OPINION IN IMMUNOLOGY, 2003, 15 (01) :75-81
[8]   The oxidoreductase ERp57 efficiently reduces partially folded in preference to fully folded MHC class I molecules [J].
Antoniou, AN ;
Ford, S ;
Alphey, M ;
Osborne, A ;
Elliott, T ;
Powis, SJ .
EMBO JOURNAL, 2002, 21 (11) :2655-2663
[9]   Interactions formed by individually expressed TAP1 and TAP2 polypeptide subunits [J].
Antoniou, AN ;
Ford, S ;
Pilley, ES ;
Blake, N ;
Powis, SJ .
IMMUNOLOGY, 2002, 106 (02) :182-189
[10]   ERp57 interacts with conserved cysteine residues in the MHC class I peptide-binding groove [J].
Antoniou, Antony N. ;
Santos, Susana G. ;
Campbell, Elaine C. ;
Lynch, Sarah ;
Arosa, Fernando A. ;
Powis, Simon J. .
FEBS LETTERS, 2007, 581 (10) :1988-1992