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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.

Original publication

DOI

10.1016/j.jsb.2011.03.010

Type

Journal article

Journal

J Struct Biol

Publication Date

08/2011

Volume

175

Pages

127 - 134

Keywords

Amino Acid Sequence, Animals, Biological Evolution, Chemokines, Host-Pathogen Interactions, Humans, Immune Evasion, Immunologic Factors, Molecular Sequence Data, Phylogeny, Poxviridae, Protein Conformation, Signal Transduction, Tumor Necrosis Factor-alpha, Vaccinia virus, Viral Proteins