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Journal of Virology, February 2008, p. 1368-1377, Vol. 82, No. 3
0022-538X/08/$08.00+0     doi:10.1128/JVI.02007-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Display of Heterologous Proteins on gp64null Baculovirus Virions and Enhanced Budding Mediated by a Vesicular Stomatitis Virus G-Stem Construct

Jian Zhou^1,2 and Gary W. Blissard^1*

Boyce Thompson Institute at Cornell University, Ithaca, New York 14853,¹ Department of Entomology, Cornell University, Ithaca, New York 14853²

Received 11 September 2007/ Accepted 23 October 2007

The Autographa californica multicapsid nucleopolyhedrovirus (AcMNPV) GP64 envelope glycoprotein is essential for virus entry and plays an important role in virion budding. An AcMNPV construct that contains a deletion of the gp64 gene is unable to propagate infection from cell to cell, and this defect results from both a severe reduction in the production of budded virions and the absence of GP64 on virions. In the current study, we examined GP64 proteins containing N- and C-terminal truncations of the ectodomain and identified a minimal construct capable of targeting the truncated GP64 to budded virions. The minimal budding and targeting construct of GP64 contained 38 amino acids from the mature N terminus of the GP64 ectodomain and 52 amino acids from the C terminus of GP64. Because the vesicular stomatitis virus (VSV) G protein was previously found to rescue infectivity of a gp64null AcMNPV, we also examined a small C-terminal construct of the VSV G protein. We found that a construct containing 91 amino acids from the C terminus of VSV G (termed G-stem) was capable of rescuing AcMNPV gp64null virion budding to wild-type (wt) or nearly wt levels. We also examined the display of chimeric proteins on the gp64null AcMNPV virion. By generating viruses that expressed chimeric influenza virus hemagglutinin (HA) proteins containing the GP64 targeting domain and coinfecting those viruses with a virus expressing the G-stem construct, we demonstrated enhanced display of the HA protein on gp64null AcMNPV budded virions. The combined use of gp64null virions, VSV G-stem-enhanced budding, and GP64 domains for targeting heterologous proteins to virions should be valuable for biotechnological applications ranging from targeted transduction of mammalian cells to vaccine production.

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* Corresponding author. Mailing address: Boyce Thompson Institute at Cornell University, Tower Road, Ithaca, NY 14853. Phone: (607) 254-1366. Fax: (413) 480-4762. E-mail: gwb1{at}cornell.edu

Published ahead of print on 7 November 2007.

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Journal of Virology, February 2008, p. 1368-1377, Vol. 82, No. 3
0022-538X/08/$08.00+0     doi:10.1128/JVI.02007-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

This article has been cited by other articles:

• Wang, M., Tan, Y., Yin, F., Deng, F., Vlak, J. M., Hu, Z., Wang, H. (2008). The F-Like Protein Ac23 Enhances the Infectivity of the Budded Virus of gp64-Null Autographa californica Multinucleocapsid Nucleopolyhedrovirus Pseudotyped with Baculovirus Envelope Fusion Protein F. J. Virol. 82: 9800-9804 [Abstract] [Full Text]  
• Zhou, J., Blissard, G. W. (2008). Identification of a GP64 Subdomain Involved in Receptor Binding by Budded Virions of the Baculovirus Autographica californica Multicapsid Nucleopolyhedrovirus. J. Virol. 82: 4449-4460 [Abstract] [Full Text]