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Viruses 2015, 7(9), 4873-4893; doi:10.3390/v7092848

Structural Conservation and Functional Diversity of the Poxvirus Immune Evasion (PIE) Domain Superfamily

1
Department of Pathology and Immunology, Washington University School of Medicine,  St. Louis, MO 63110, USA
2
Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110, USA
3
Department of Molecular Microbiology,Washington University School of Medicine, St. Louis, MO 63110, USA
*
Authors to whom correspondence should be addressed.
Academic Editors: Elliot J. Lefkowitz and Chris Upton
Received: 21 March 2015 / Revised: 19 August 2015 / Accepted: 20 August 2015 / Published: 28 August 2015
(This article belongs to the Special Issue Poxvirus Evolution)
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Abstract

Poxviruses encode a broad array of proteins that serve to undermine host immune defenses. Structural analysis of four of these seemingly unrelated proteins revealed the recurrent use of a conserved beta-sandwich fold that has not been observed in any eukaryotic or prokaryotic protein. Herein we propose to call this unique structural scaffolding the PIE (Poxvirus Immune Evasion) domain. PIE domain containing proteins are abundant in chordopoxvirinae, with our analysis identifying 20 likely PIE subfamilies among 33 representative genomes spanning 7 genera. For example, cowpox strain Brighton Red appears to encode 10 different PIEs: vCCI, A41, C8, M2, T4 (CPVX203), and the SECRET proteins CrmB, CrmD, SCP-1, SCP-2, and SCP-3. Characterized PIE proteins all appear to be nonessential for virus replication, and all contain signal peptides for targeting to the secretory pathway. The PIE subfamilies differ primarily in the number, size, and location of structural embellishments to the beta-sandwich core that confer unique functional specificities. Reported ligands include chemokines, GM-CSF, IL-2, MHC class I, and glycosaminoglycans. We expect that the list of ligands and receptors engaged by the PIE domain will grow as we come to better understand how this versatile structural architecture can be tailored to manipulate host responses to infection. View Full-Text
Keywords: poxvirus; PIE domain; SECRET domain; viral immune evasion; chemokine and cytokine decoy receptors poxvirus; PIE domain; SECRET domain; viral immune evasion; chemokine and cytokine decoy receptors
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Nelson, C.A.; Epperson, M.L.; Singh, S.; Elliott, J.I.; Fremont, D.H. Structural Conservation and Functional Diversity of the Poxvirus Immune Evasion (PIE) Domain Superfamily. Viruses 2015, 7, 4873-4893.

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