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A soluble form of P74 can act as a per os infectivity factor to the Autographa californica multiple
Jeffrey M Slack1, Susan D Lawrence, Peter J Krell
1Great Lakes Forestry Centre, Sault Ste Marie, ON P6A 2E5, Canada.
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 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. 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.
Insights
The Autographa californica multicapsid nucleopolyhedrovirus P74 protein is crucial for insect baculovirus infection. A soluble form of P74, lacking its anchor, retains infectivity, suggesting it may interact with other viral proteins.
Area of Science:
- Virology
- Insect Pathology
- Molecular Biology
Background:
- Baculovirus occlusion-derived virions (ODVs) are essential for per os transmission in insect hosts.
- The Autographa californica multicapsid nucleopolyhedrovirus (AcMNPV) P74 protein is an ODV envelope protein critical for infectivity.
Purpose of the Study:
- To investigate the role of the P74 protein's domains in ODV per os infectivity.
- To determine if a soluble form of P74 can restore infectivity to P74-null baculoviruses.
Main Methods:
- Construction and characterization of N-terminal and C-terminal P74 truncation mutants.
- Evaluation of mutant P74 proteins for their ability to rescue per os infectivity of a P74-null baculovirus (AcLP4).
Main Results:
- A P74 truncation mutant lacking the C-terminal transmembrane anchor domain successfully rescued per os infectivity.
- This indicates that the soluble portion of P74 is sufficient for its infectivity factor function.
Conclusions:
- The C-terminal transmembrane anchor is not essential for P74's role in per os infectivity.
- A soluble form of P74 can function independently, suggesting potential complex formation with other ODV envelope proteins.
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