Key result
Using the yeast two-hybrid system, the Feline calicivirus p32 protein interacted with p39, p30, and p76, while the ProPol p76 formed homo-oligomers and interacted with VPg and ORF2.
Characterization of protein-protein interactions in the feline calicivirus replication complex provides insights into calicivirus replication.
May suggest calicivirus replication targets; leaves open validation in mammalian systems and human relevance.
Caliciviruses are a major cause of gastroenteritis in humans and cause a wide variety of other diseases in animals. Here, the characterization of protein-protein interactions between the individual proteins of Feline calicivirus (FCV), a model system for other members of the family Caliciviridae, is reported. Using the yeast two-hybrid system combined with a number of other approaches, it is demonstrated that the p32 protein (the picornavirus 2B analogue) of FCV interacts with p39 (2C), p30 (3A) and p76 (3CD). The FCV protease/RNA polymerase (ProPol) p76 was found to form homo-oligomers, as well as to interact with VPg and ORF2, the region encoding the major capsid protein VP1. A weak interaction was also observed between p76 and the minor capsid protein encoded by ORF3 (VP2). ORF2 protein was found to interact with VPg, p76 and VP2. The potential roles of the interactions in calicivirus replication are discussed.
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Kaiser et al. (2006) studied Feline calicivirus. Using the yeast two-hybrid system, the Feline calicivirus p32 protein interacted with p39, p30, and p76, while the ProPol p76 formed homo-oligomers and interacted with VPg and ORF2.
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