Submitted to: Journal of General Virology
Publication Type: Peer reviewed journal
Publication Acceptance Date: 12/9/2010
Publication Date: 1/27/2010
Citation: Jeffrey, S., Lawrence, S.D., Krell, P.J., Arif, B.M. 2010. A soluble form of P74 can act as a per os infectivity factor to the autographa californica multiple nucleopolyhedrovirus. Journal of General Virology. 91:915-918. Interpretive Summary: Colorado potato beetle (CPB) costs hundreds of millions of dollars for pesticide control and yield loss each year in the United States. To address this problem, we are trying to modify potato plants so they produce compounds toxic to beetles when they feed upon the plant, which will kill the insect with minimal damage to the plant. In this work we characterize a compound that binds to insect gut. We find that this compound can act as a carrier of another compound into the gut and function of both compounds is maintained. This knowledge will benefit researchers in that it allows them to take the next step, testing whether this carrier can be used to take up a compound toxic to beetles and used as an alternative to pesticides for the control of the CPB.
Technical Abstract: The baculovirus occlusion-derived virion (ODV) is required to spread virus infection among insect hosts via the per os route. The Autographa californica Multicapsid Nucleopolyhedrovirus (AcMNPV) P74 protein is an ODV envelope protein that is essential for ODVs to be infectious. P74 is anchored in the ODV envelope by a C-terminal transmembrane anchor domain and is N-terminally exposed on the ODV surface. In the present study, a series of N-terminal and C-terminal truncation mutants of P74 were evaluated for their ability to rescue per os infectivity of the P74-null virus, AcLP4 (Kuzio et al., 1989). It was discovered that a P74 truncation mutant lacking the C-terminal transmembrane anchor domain of P74 was able to rescue per os infection. This result shows that a soluble form of P74 retains per os infectivity factor function and suggests that P74 may be complexed with other proteins in the ODV envelope.