1887

Abstract

The baculovirus occlusion-derived virion (ODV) is required to spread virus infection among insect hosts via the route. The multicapsid nucleopolyhedrovirus 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 infectivity of the P74-null virus, AcLP4. It was discovered that a P74 truncation mutant lacking the C-terminal transmembrane anchor domain of P74 was able to rescue infection. This result shows that a soluble form of P74 retains infectivity factor function and suggests that P74 may be complexed with other proteins in the ODV envelope.

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2010-04-01
2019-11-19
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