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Viruses 2015, 7(7), 3506-3529; doi:10.3390/v7072783

Structures and Functions of Pestivirus Glycoproteins: Not Simply Surface Matters

1
School of Veterinary Medicine, National Taiwan University, No. 1, Section 4, Roosevelt Road, Taipei 10617, Taiwan
2
Animal Health Research Institute, Council of Agriculture, 376 Chung-Cheng Road, Tansui, New Taipei City 25158, Taiwan
*
Author to whom correspondence should be addressed.
Academic Editor: Andrew Ward
Received: 3 March 2015 / Revised: 11 June 2015 / Accepted: 18 June 2015 / Published: 29 June 2015
(This article belongs to the Special Issue Viral Glycoprotein Structure)
View Full-Text   |   Download PDF [367 KB, uploaded 29 June 2015]   |  

Abstract

Pestiviruses, which include economically important animal pathogens such as bovine viral diarrhea virus and classical swine fever virus, possess three envelope glycoproteins, namely Erns, E1, and E2. This article discusses the structures and functions of these glycoproteins and their effects on viral pathogenicity in cells in culture and in animal hosts. E2 is the most important structural protein as it interacts with cell surface receptors that determine cell tropism and induces neutralizing antibody and cytotoxic T-lymphocyte responses. All three glycoproteins are involved in virus attachment and entry into target cells. E1-E2 heterodimers are essential for viral entry and infectivity. Erns is unique because it possesses intrinsic ribonuclease (RNase) activity that can inhibit the production of type I interferons and assist in the development of persistent infections. These glycoproteins are localized to the virion surface; however, variations in amino acids and antigenic structures, disulfide bond formation, glycosylation, and RNase activity can ultimately affect the virulence of pestiviruses in animals. Along with mutations that are driven by selection pressure, antigenic differences in glycoproteins influence the efficacy of vaccines and determine the appropriateness of the vaccines that are currently being used in the field. View Full-Text
Keywords: pestivirus; glycoprotein; Erns; E1; E2; structure; function pestivirus; glycoprotein; Erns; E1; E2; structure; function
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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Wang, F.-I.; Deng, M.-C.; Huang, Y.-L.; Chang, C.-Y. Structures and Functions of Pestivirus Glycoproteins: Not Simply Surface Matters. Viruses 2015, 7, 3506-3529.

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