The F-like protein of group I NPVs enhances the production and infectivity of the budded virus of gp64-null AcMNPV pseudotyped with the envelope fusion protein F of Group II NPVs

M. Wang, Y. Tan, F. Deng, Z.H. Hu, J.M. Vlak, H. Wang

Research output: Chapter in Book/Report/Conference proceedingAbstract

Abstract

GP64 and F proteins were previously identified as the principle functional envelope fusion proteins in the Baculoviridae. The F-like proteins in group I NPVs, which use GP64 as a functional envelope fusion protein, are thought to be remnants of F in group I NPVs and lack a furin cleavage site. The F-like proteins were demonstrated to be a pathogenicity factor in vivo, but to be irrelevant for budded virus production in cell culture. However, in the current study we analyzed the function of the F-like protein Ac23 of Autographa californica MNPV in the absence of Ac-GP64 and found that the presence of Ac23 significantly enhanced infectious BV production of gp64 null-AcMNPV pseudotyped with Spodoptera exigua MNPV F protein. Quantitative PCR further revealed the absence of Ac23 leads to a lower production of infectious progeny virions as compared to control viruses. These findings provide evidence that the F-like protein not only enhances viral infectivity in vivo, but also in vitro. The role of the F-like protein as an auxiliary factor in BV maturation in group I NPVs will be further discussed.
Original languageEnglish
Title of host publicationAbstract Book of the 41st Annual Meeting of the Society for Invertebrate Pathology and 9th International Conference on Bacillus thuringiensis, Warwick, United Kingdom, 3-7 August 2008
Place of PublicationWarwick
Pages49-49
Publication statusPublished - 2008
Event41st Annual Meeting of the Society for Invertebrate Pathology and the 9th International Conference on Bacillus thuringiensis -
Duration: 3 Aug 20087 Aug 2008

Conference

Conference41st Annual Meeting of the Society for Invertebrate Pathology and the 9th International Conference on Bacillus thuringiensis
Period3/08/087/08/08

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