Structures and Functions of Pestivirus Glycoproteins: Not Simply Surface Matters
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 vira...
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| Format: | Article |
| Language: | English |
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MDPI AG
2015-06-01
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| Series: | Viruses |
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| Online Access: | http://www.mdpi.com/1999-4915/7/7/2783 |
| _version_ | 1819161465052987392 |
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| author | Fun-In Wang Ming-Chung Deng Yu-Liang Huang Chia-Yi Chang |
| author_facet | Fun-In Wang Ming-Chung Deng Yu-Liang Huang Chia-Yi Chang |
| author_sort | Fun-In Wang |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-22T17:12:46Z |
| format | Article |
| id | doaj.art-7f3b98e338844f17878ee85eb3a0400e |
| institution | Directory Open Access Journal |
| issn | 1999-4915 |
| language | English |
| last_indexed | 2024-12-22T17:12:46Z |
| publishDate | 2015-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Viruses |
| spelling | doaj.art-7f3b98e338844f17878ee85eb3a0400e2022-12-21T18:19:01ZengMDPI AGViruses1999-49152015-06-01773506352910.3390/v7072783v7072783Structures and Functions of Pestivirus Glycoproteins: Not Simply Surface MattersFun-In Wang0Ming-Chung Deng1Yu-Liang Huang2Chia-Yi Chang3School of Veterinary Medicine, National Taiwan University, No. 1, Section 4, Roosevelt Road, Taipei 10617, TaiwanAnimal Health Research Institute, Council of Agriculture, 376 Chung-Cheng Road, Tansui, New Taipei City 25158, TaiwanAnimal Health Research Institute, Council of Agriculture, 376 Chung-Cheng Road, Tansui, New Taipei City 25158, TaiwanAnimal Health Research Institute, Council of Agriculture, 376 Chung-Cheng Road, Tansui, New Taipei City 25158, TaiwanPestiviruses, 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.http://www.mdpi.com/1999-4915/7/7/2783pestivirusglycoproteinErnsE1E2structurefunction |
| spellingShingle | Fun-In Wang Ming-Chung Deng Yu-Liang Huang Chia-Yi Chang Structures and Functions of Pestivirus Glycoproteins: Not Simply Surface Matters Viruses pestivirus glycoprotein Erns E1 E2 structure function |
| title | Structures and Functions of Pestivirus Glycoproteins: Not Simply Surface Matters |
| title_full | Structures and Functions of Pestivirus Glycoproteins: Not Simply Surface Matters |
| title_fullStr | Structures and Functions of Pestivirus Glycoproteins: Not Simply Surface Matters |
| title_full_unstemmed | Structures and Functions of Pestivirus Glycoproteins: Not Simply Surface Matters |
| title_short | Structures and Functions of Pestivirus Glycoproteins: Not Simply Surface Matters |
| title_sort | structures and functions of pestivirus glycoproteins not simply surface matters |
| topic | pestivirus glycoprotein Erns E1 E2 structure function |
| url | http://www.mdpi.com/1999-4915/7/7/2783 |
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