Rinderpest virus C and V proteins interact with the major (L) component of the viral polymerase.
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.
Institute for Animal Health, Ash Road, Surrey, Pirbright, GU24 0NF, United Kingdom.
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Sweetman
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Miskin
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Baron
D000818:Animals; D002417:Cattle; D002522:Chlorocebus aethiops; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism*; D005057:Eukaryotic Cells / Q000378:metabolism / Q000821:virology; D005455:Fluorescent Antibody Technique; D017353:Gene Deletion; D015870:Gene Expression; D019251:Nucleocapsid / Q000378:metabolism; D011485:Protein Binding; D012302:Rinderpest virus / Q000378:metabolism*; D014709:Vero Cells; D014758:Viral Core Proteins / Q000032:analysis / Q000378:metabolism; D014764:Viral Proteins / Q000378:metabolism*; D014779:Virus Replication
D014758:Viral Core Proteins; D014764:Viral Proteins; D012321:DNA-Directed RNA Polymerases