This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Lung, O. Articles by Blissard, G. W. Search for Related Content PubMed PubMed Citation Articles by Lung, O. Articles by Blissard, G. W.

 Previous Article  |  Next Article 

Journal of Virology, June 2002, p. 5729-5736, Vol. 76, No. 11
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.11.5729-5736.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Pseudotyping Autographa californica Multicapsid Nucleopolyhedrovirus (AcMNPV): F Proteins from Group II NPVs Are Functionally Analogous to AcMNPV GP64

Boyce Thompson Institute, Cornell University, Ithaca, New York 14853,¹ Laboratory of Virology, Wageningen University, Wageningen, The Netherlands²

Received 17 December 2001/ Accepted 27 February 2002

GP64, the major envelope glycoprotein of budded virions of the baculovirus Autographa californica multicapsid nucleopolyhedrovirus (AcMNPV), is involved in viral attachment, mediates membrane fusion during virus entry, and is required for efficient virion budding. Thus, GP64 is essential for viral propagation in cell culture and in animals. Recent genome sequences from a number of baculoviruses show that only a subset of closely related baculoviruses have gp64 genes, while other baculoviruses have a recently discovered unrelated envelope protein named F. F proteins from Lymantria dispar MNPV (LdMNPV) and Spodoptera exigua MNPV (SeMNPV) mediate membrane fusion and are therefore thought to serve roles similar to that of GP64. To determine whether F proteins are functionally analogous to GP64 proteins, we deleted the gp64 gene from an AcMNPV bacmid and inserted F protein genes from three different baculoviruses. In addition, we also inserted envelope protein genes from vesicular stomatitis virus (VSV) and Thogoto virus. Transfection of the gp64-null bacmid DNA into Sf9 cells does not generate infectious particles, but this defect was rescued by introducing either the F protein gene from LdMNPV or SeMNPV or the G protein gene from VSV. These results demonstrate that baculovirus F proteins are functionally analogous to GP64. Because baculovirus F proteins appear to be more widespread within the family and are much more divergent than GP64 proteins, gp64 may represent the acquisition of an envelope protein gene by an ancestral baculovirus. The AcMNPV pseudotyping system provides an efficient and powerful method for examining the functions and compatibilities of analogous or orthologous viral envelope proteins, and it could have important biotechnological applications.

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]  
• Yin, F., Wang, M., Tan, Y., Deng, F., Vlak, J. M., Hu, Z., Wang, H. (2008). A Functional F Analogue of Autographa californica Nucleopolyhedrovirus GP64 from the Agrotis segetum Granulovirus. J. Virol. 82: 8922-8926 [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]  
• Li, Z., Blissard, G. W. (2008). Functional Analysis of the Transmembrane (TM) Domain of the Autographa californica Multicapsid Nucleopolyhedrovirus GP64 Protein: Substitution of Heterologous TM Domains. J. Virol. 82: 3329-3341 [Abstract] [Full Text]  
• Wang, M., Tan, Y., Yin, F., Deng, F., Vlak, J. M., Hu, Z., Wang, H. (2008). The F protein of Helicoverpa armigera single nucleopolyhedrovirus can be substituted functionally with its homologue from Spodoptera exigua multiple nucleopolyhedrovirus. J. Gen. Virol. 89: 791-798 [Abstract] [Full Text]  
• Long, G., Pan, X., Vlak, J. M. (2008). Conserved Leucines in N-Terminal Heptad Repeat HR1 of Envelope Fusion Protein F of Group II Nucleopolyhedroviruses Are Important for Correct Processing and Essential for Fusogenicity. J. Virol. 82: 2437-2447 [Abstract] [Full Text]  
• Westenberg, M., Vlak, J. M. (2008). GP64 of group I nucleopolyhedroviruses cannot readily rescue infectivity of group II f-null nucleopolyhedroviruses. J. Gen. Virol. 89: 424-431 [Abstract] [Full Text]  
• Zhou, J., Blissard, G. W. (2008). Display of Heterologous Proteins on gp64null Baculovirus Virions and Enhanced Budding Mediated by a Vesicular Stomatitis Virus G-Stem Construct. J. Virol. 82: 1368-1377 [Abstract] [Full Text]  
• Westenberg, M., Uijtdewilligen, P., Vlak, J. M. (2007). Baculovirus envelope fusion proteins F and GP64 exploit distinct receptors to gain entry into cultured insect cells. J. Gen. Virol. 88: 3302-3306 [Abstract] [Full Text]  
• Long, G., Pan, X., Vlak, J. M. (2007). Absence of N-linked glycans from the F2 subunit of the major baculovirus envelope fusion protein F enhances fusogenicity. J. Gen. Virol. 88: 441-449 [Abstract] [Full Text]  
• Long, G., Pan, X., Westenberg, M., Vlak, J. M. (2006). Functional Role of the Cytoplasmic Tail Domain of the Major Envelope Fusion Protein of Group II Baculoviruses.. J. Virol. 80: 11226-11234 [Abstract] [Full Text]  
• Long, G., Westenberg, M., Wang, H., Vlak, J. M., Hu, Z. (2006). Function, oligomerization and N-linked glycosylation of the Helicoverpa armigera single nucleopolyhedrovirus envelope fusion protein.. J. Gen. Virol. 87: 839-846 [Abstract] [Full Text]  
• Lung, O., Blissard, G. W. (2005). A Cellular Drosophila melanogaster Protein with Similarity to Baculovirus F Envelope Fusion Proteins. J. Virol. 79: 7979-7989 [Abstract] [Full Text]  
• Liang, C., Song, J., Chen, X. (2005). The GP64 protein of Autographa californica multiple nucleopolyhedrovirus rescues Helicoverpa armigera nucleopolyhedrovirus transduction in mammalian cells. J. Gen. Virol. 86: 1629-1635 [Abstract] [Full Text]  
• Kitagawa, Y., Tani, H., Limn, C. K., Matsunaga, T. M., Moriishi, K., Matsuura, Y. (2005). Ligand-Directed Gene Targeting to Mammalian Cells by Pseudotype Baculoviruses. J. Virol. 79: 3639-3652 [Abstract] [Full Text]  
• Westenberg, M., Veenman, F., Roode, E. C., Goldbach, R. W., Vlak, J. M., Zuidema, D. (2004). Functional Analysis of the Putative Fusion Domain of the Baculovirus Envelope Fusion Protein F. J. Virol. 78: 6946-6954 [Abstract] [Full Text]  
• Garcia-Maruniak, A., Maruniak, J. E., Zanotto, P. M. A., Doumbouya, A. E., Liu, J.-C., Merritt, T. M., Lanoie, J. S. (2004). Sequence Analysis of the Genome of the Neodiprion sertifer Nucleopolyhedrovirus. J. Virol. 78: 7036-7051 [Abstract] [Full Text]  
• Zhang, S. X., Han, Y., Blissard, G. W. (2003). Palmitoylation of the Autographa californica Multicapsid Nucleopolyhedrovirus Envelope Glycoprotein GP64: Mapping, Functional Studies, and Lipid Rafts. J. Virol. 77: 6265-6273 [Abstract] [Full Text]  
• Lung, O. Y., Cruz-Alvarez, M., Blissard, G. W. (2002). Ac23, an Envelope Fusion Protein Homolog in the Baculovirus Autographa californica Multicapsid Nucleopolyhedrovirus, Is a Viral Pathogenicity Factor. J. Virol. 77: 328-339 [Abstract] [Full Text]  
• Lin, G., Blissard, G. W. (2002). Analysis of an Autographa californica Multicapsid Nucleopolyhedrovirus lef-6-Null Virus: LEF-6 Is Not Essential for Viral Replication but Appears To Accelerate Late Gene Transcription. J. Virol. 76: 5503-5514 [Abstract] [Full Text]