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Hog cholera virus: molecular composition of virions from a pestivirus
H J Thiel1, R Stark, E Weiland
1Federal Research Centre for Virus Diseases of Animals, Tübingen, Federal Republic of Germany.
Abstract:
Virions from hog cholera virus (HCV), a member of the genus Pestivirus, were analyzed by using specific antibodies. The nucleocapsid protein was found to be a 14-kDa molecule (HCV p14). An equivalent protein could also be demonstrated for virions from another pestivirus, bovine viral diarrhea virus. The HCV envelope is composed of three glycoproteins, HCV gp44/48, gp33, and gp55. All three exist in the form of disulfide-linked dimers in virus-infected cells and in virions; HCV gp44/48 and gp55 each form homodimers, whereas gp55 is also found dimerized with gp33. Such complex covalent interactions between structural glycoproteins have not been described so far for any RNA virus.
Insights
Hog cholera virus (HCV) virions contain a 14-kDa nucleocapsid protein (HCV p14) and three envelope glycoproteins (gp44/48, gp33, gp55). These glycoproteins form complex disulfide-linked dimers, a novel finding for RNA viruses.
Area of Science:
- Virology
- Molecular Biology
- Structural Biology
Background:
- Hog cholera virus (HCV) is a significant pathogen within the Pestivirus genus.
- Understanding the structural components of HCV virions is crucial for developing antiviral strategies.
Purpose of the Study:
- To characterize the structural proteins of hog cholera virus (HCV) virions.
- To investigate the covalent interactions among HCV envelope glycoproteins.
Main Methods:
- Analysis of virions using specific antibodies.
- Identification and characterization of viral proteins and their molecular weights.
- Investigation of protein-protein interactions, specifically disulfide-linked dimerization.
Main Results:
- A 14-kDa nucleocapsid protein (HCV p14) was identified in HCV virions, with an equivalent protein found in bovine viral diarrhea virus.
- The HCV envelope comprises three glycoproteins: HCV gp44/48, gp33, and gp55.
- All three glycoproteins exist as disulfide-linked dimers in infected cells and virions, with complex homodimerization (gp44/48, gp55) and heterodimerization (gp55 with gp33) observed.
Conclusions:
- HCV p14 is the nucleocapsid protein of hog cholera virus.
- The complex disulfide-linked dimerization of HCV envelope glycoproteins represents a unique structural feature among RNA viruses.
- These findings provide new insights into the structural organization and potential assembly mechanisms of pestiviruses.
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