Structures and functions of pestivirus glycoproteins: Not simply surface matters
Journal
Viruses
Journal Volume
7
Journal Issue
7
Pages
3506-3529
Date Issued
2015
Author(s)
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. © 2015 by the authors; licensee MDPI, Basel, Switzerland.
Subjects
E1; E2; Erns; Function; Glycoprotein; Pestivirus; Structure
SDGs
Other Subjects
beta actin; cysteine; epitope; glycoprotein E1; glycoprotein E2; glycoprotein Erns; glycosaminoglycan; interferon; subunit vaccine; unclassified drug; virus glycoprotein; virus envelope protein; antigenicity; crystal structure; dimerization; disulfide bond; enzyme activity; mutation; nonhuman; Pestivirus; protein glycosylation; protein interaction; protein localization; Review; tropism; virus assembly; virus attachment; virus entry; virus infectivity; virus virulence; animal; bovine; cattle disease; chemistry; genetics; metabolism; pathogenicity; Pestivirus; Pestivirus infection; pig; swine disease; veterinary; virology; Animalia; Bovine viral diarrhea virus 1; Classical swine fever virus; Pestivirus; Animals; Cattle; Cattle Diseases; Pestivirus; Pestivirus Infections; Swine; Swine Diseases; Viral Envelope Proteins; Virus Internalization
Type
review