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Journal of Virology, July 2004, p. 6946-6954, Vol. 78, No. 13
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.13.6946-6954.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Functional Analysis of the Putative Fusion Domain of the Baculovirus Envelope Fusion Protein F

Marcel Westenberg, Frank Veenman, Els C. Roode, Rob W. Goldbach, Just M. Vlak,* and Douwe Zuidema

Laboratory of Virology, Wageningen University, 6709 PD Wageningen, The Netherlands

Received 7 November 2003/ Accepted 25 February 2004

Group II nucleopolyhedroviruses (NPVs), e.g., Spodoptera exigua MNPV, lack a GP64-like protein that is present in group I NPVs but have an unrelated envelope fusion protein named F. In contrast to GP64, the F protein has to be activated by a posttranslational cleavage mechanism to become fusogenic. In several vertebrate viral fusion proteins, the cleavage activation generates a new N terminus which forms the so-called fusion peptide. This fusion peptide inserts in the cellular membrane, thereby facilitating apposition of the viral and cellular membrane upon sequential conformational changes of the fusion protein. A similar peptide has been identified in NPV F proteins at the N terminus of the large membrane-anchored subunit F1. The role of individual amino acids in this putative fusion peptide on viral infectivity and propagation was studied by mutagenesis. Mutant F proteins with single amino acid changes as well as an F protein with a deleted putative fusion peptide were introduced in gp64-null Autographa californica MNPV budded viruses (BVs). None of the mutations analyzed had an major effect on the processing and incorporation of F proteins in the envelope of BVs. Only two mutants, one with a substitution for a hydrophobic residue (F152R) and one with a deleted putative fusion peptide, were completely unable to rescue the gp64-null mutant. Several nonconservative substitutions for other hydrophobic residues and the conserved lysine residue had only an effect on viral infectivity. In contrast to what was expected from vertebrate virus fusion peptides, alanine substitutions for glycines did not show any effect.

* Corresponding author. Mailing address: Wageningen University, Laboratory of Virology, Binnenhaven 11, 6709 PD Wageningen, The Netherlands. Phone: 31-317-483090. Fax: 31-317-484820. E-mail: just.vlak{at}wur.nl.

Journal of Virology, July 2004, p. 6946-6954, Vol. 78, No. 13
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.13.6946-6954.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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