How vaccinia virus has evolved to subvert the host immune response

被引:61
作者
Bahar, Mohammad W. [1 ,2 ]
Graham, Stephen C. [1 ,2 ]
Chen, Ron A. -J. [3 ]
Cooray, Samantha [3 ]
Smith, Geoffrey L. [3 ]
Stuart, David I. [1 ,2 ,4 ]
Grimes, Jonathan M. [1 ,2 ,4 ]
机构
[1] Univ Oxford, Div Struct Biol, Oxford OX3 7BN, England
[2] Univ Oxford, Wellcome Trust Ctr Human Genet, Oxford Prot Prod Facil, Oxford OX3 7BN, England
[3] Univ London Imperial Coll Sci Technol & Med, Fac Med, Dept Virol, London W2 1PG, England
[4] Diamond Light Source Ltd, Div Sci, Didcot OX11 0DE, Oxon, England
基金
英国惠康基金; 英国医学研究理事会;
关键词
Structural virology; Innate immunity; Cell signalling; X-ray crystallography; Surface receptors; NF-KAPPA-B; NECROSIS-FACTOR RECEPTOR; TOLL-LIKE-RECEPTORS; PROTEIN-KINASE PKR; RNA HELICASE DDX3; POXVIRUS PROTEIN; STRUCTURAL BASIS; APOPTOTIC PROTEIN; CRYSTAL-STRUCTURE; BINDING-PROTEIN;
D O I
10.1016/j.jsb.2011.03.010
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Viruses are obligate intracellular parasites and are some of the most rapidly evolving and diverse pathogens encountered by the host immune system. Large complicated viruses, such as poxviruses, have evolved a plethora of proteins to disrupt host immune signalling in their battle against immune surveillance. Recent X-ray crystallographic analysis of these viral immunomodulators has helped form an emerging picture of the molecular details of virus-host interactions. In this review we consider some of these immune evasion strategies as they apply to poxviruses, from a structural perspective, with specific examples from the European SPINE2-Complexes initiative. Structures of poxvirus immunomodulators reveal the capacity of viruses to mimic and compete against the host immune system, using a diverse range of structural folds that are unique or acquired from their hosts with both enhanced and unexpectedly divergent functions. (C) 2011 Elsevier Inc. All rights reserved.
引用
收藏
页码:127 / 134
页数:8
相关论文
共 81 条
[1]   Signalling pathways of the TNF superfamily: A double-edged sword [J].
Aggarwal, BB .
NATURE REVIEWS IMMUNOLOGY, 2003, 3 (09) :745-756
[2]   Pathogen recognition and innate immunity [J].
Akira, S ;
Uematsu, S ;
Takeuchi, O .
CELL, 2006, 124 (04) :783-801
[3]   Viral mechanisms of immune evasion [J].
Alcami, A ;
Koszinowski, UH .
IMMUNOLOGY TODAY, 2000, 21 (09) :447-455
[4]   Viral mimicry of cytokines, chemokines and their receptors [J].
Alcami, A .
NATURE REVIEWS IMMUNOLOGY, 2003, 3 (01) :36-50
[5]   Vaccinia virus N1L protein resembles a B cell lymphoma-2 (Bcl-2) family protein [J].
Aoyagi, Mika ;
Zhai, Dayong ;
Jin, Chaofang ;
Aleshin, Alexander E. ;
Stec, Boguslaw ;
Reed, John C. ;
Liddington, Robert C. .
PROTEIN SCIENCE, 2007, 16 (01) :118-124
[6]   Structural determinants of chemokine binding by an ectromelia virus-encoded decoy receptor [J].
Arnold, Phoebe L. ;
Fremont, Daved H. .
JOURNAL OF VIROLOGY, 2006, 80 (15) :7439-7449
[7]   Structure and function of A41, a vaccinia virus chemokine binding protein [J].
Bahar, Mohammad W. ;
Kenyon, Julia C. ;
Putz, Mike M. ;
Abrescia, Nicola G. A. ;
Pease, James E. ;
Wise, Emma L. ;
Stuart, David I. ;
Smith, Geoffrey L. ;
Grimes, Jonathan M. .
PLOS PATHOGENS, 2008, 4 (01) :0055-0068
[8]   What does structure tell us about virus evolution? [J].
Bamford, DH ;
Grimes, JM ;
Stuart, DI .
CURRENT OPINION IN STRUCTURAL BIOLOGY, 2005, 15 (06) :655-663
[9]   The vaccinia virus N1L protein is an intracellular homodimer that promotes virulence [J].
Bartlett, N ;
Symons, JA ;
Tscharke, DC ;
Smith, GL .
JOURNAL OF GENERAL VIROLOGY, 2002, 83 :1965-1976
[10]   VACCINIA VIRUS-ENCODED EIF-2-ALPHA HOMOLOG ABROGATES THE ANTIVIRAL EFFECT OF INTERFERON [J].
BEATTIE, E ;
TARTAGLIA, J ;
PAOLETTIT, E .
VIROLOGY, 1991, 183 (01) :419-422