Rinderpest virus C and V proteins interact with the major (L) component of the viral polymerase.
Virology
; 281(2): 193-204, 2001 Mar 15.
Article
in En
| MEDLINE
| ID: mdl-11277692
ABSTRACT
Rinderpest virus, like other Morbilliviruses, expresses three proteins from the single P gene. In addition to the P protein, which interacts both with the viral polymerase (L) and the nucleocapsid (N) protein, the virus expresses a C and a V protein from the same gene. The functions of these two proteins in the viral life cycle are not clear. Although both C and V proteins are dispensable, in that viable viruses can be made that express neither, each seems to play a role in optimum viral replication. We have used the yeast-two hybrid system, binding to coexpressed fusions of C and V to glutathione-S-transferase, and studies of the native size of these proteins to investigate interactions of the rinderpest virus C and V proteins with other virus-encoded proteins. The V protein was found to interact with both the N and L proteins, while the C protein was found to bind to the L protein, and to self-associate in high-molecular-weight aggregates.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Rinderpest virus
/
Viral Proteins
/
DNA-Directed RNA Polymerases
Limits:
Animals
Language:
En
Journal:
Virology
Year:
2001
Document type:
Article
Affiliation country:
United kingdom