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Journal of Virology, January 2002, p. 178-184, Vol. 76, No. 1
0022-538X/01/$04.00+0     DOI: 10.1128/JVI.76.1.178-184.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Furin Is Involved in Baculovirus Envelope Fusion Protein Activation

Marcel Westenberg,1 Hualin Wang,1,2 Wilfred F. J. IJkel,1 Rob W. Goldbach,1 Just M. Vlak,1 and Douwe Zuidema1*

Laboratory of Virology, Wageningen University and Research Center, 6709 PD Wageningen, The Netherlands,1 Joint Laboratory of Invertebrate Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, People’s Republic of China2

Received 19 July 2001/ Accepted 26 September 2001

The Spodoptera exigua multicapsid nucleopolyhedrovirus (SeMNPV) Se8 gene was recently shown to encode the viral envelope fusion (F) protein. A 60-kDa C-terminal subunit (F1) of the 76-kDa primary translation product of this gene was found to be the major envelope protein of SeMNPV budded virus (BV) (W. F. J. IJkel, M. Westenberg, R. W. Goldbach, G. W. Blissard, J. M. Vlak, and D. Zuidema, Virology 275:30–41, 2000). A specific inhibitor was used to show that furin is involved in cleavage of the precursor envelope fusion (F0) protein. BV produced in the presence of the inhibitor possesses the uncleaved F0 protein, while an F protein with a mutation in the furin cleavage site was translocated to the plasma membrane but lost its fusogenic activity. These results indicate that cleavage of F0 is required to activate the SeMNPV F protein and is necessary for BV infectivity. Specific antibodies against F1 and against the putative N terminus (F2) of the primary translation product were used to show that the F protein is BV specific and that BVs contain both the 60- (F1) and 21-kDa (F2) cleavage products. In nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis both subunits migrate as a single 80-kDa protein, indicating that the subunits remain associated by a disulfide linkage. In addition, the presence of the F protein predominately as a monomer suggests that disulfide links are not involved in oligomerization. Thus, the envelope fusion protein from group II nucleopolyhedroviruses of baculoviruses has properties similar to those of proteins from a number of vertebrate viruses.

* Corresponding author. Mailing address: Laboratory of Virology, Wageningen University and Research Center, Binnenhaven 11, 6709 PD Wageningen, The Netherlands. Phone: 31-317-483089. Fax: 31-317-484820. E-mail: just.vlak{at}viro.dpw.wau.nl.

Journal of Virology, January 2002, p. 178-184, Vol. 76, No. 1
0022-538X/01/$04.00+0     DOI: 10.1128/JVI.76.1.178-184.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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