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Published online ahead of print on 4 March 2009 as doi:10.1099/vir.0.009035-0
Journal of General Virology 2009;90:1499.

A more recent version of this article appeared on June 1, 2009 J Gen Virol (2009), DOI 10.1099/vir.0.009035-0
© 2009 Society for General Microbiology
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Autographa californica multiple nucleopolyhedrovirus (AcMNPV) ORF 23 null mutant produces occlusion-derived virions with fewer nucleocapsids

Ian-Ling Yu1, Doug Bray1, Ying-chu Lin2 and Oliver Lung3,4

1 University of Lethbridge;
2 Kaohsiung Medical University;
3 Canadian Food Inspection Agency

4 E-mail: lungo{at}inspection.gc.ca

Two envelope fusion protein gene homologs have been identified in the baculovirus Autographa californica multiple nucleopolyhedrovirus (AcMNPV). AcMNPV GP64 protein is fusogenic and essential for propagation and pathogenicity. The F homologue (Ac23) is not essential, is fusion-incompetent in standard assays, but contributes to faster host death. Here, we show occlusion bodies (OB) from Ac23null mutants and control viruses do not differ significantly in size and the number of occlusion-derived virions (ODV) contained, however, Ac23null OBs had a much higher percentage of ODVs with a single nucleocapsid (44.5%) than the near-isogenic control (11.3%). Infection of Sf9 cells with Ac23gfp expressing recombinant viruses showed Ac23-gfp fluorescence overlapping peri-nuclear DAPI staining at later times, a pattern not observed with GP64. These results suggest that F proteins have evolved functions beyond envelope fusion and play a different role from that of GP64 in viruses that contain both proteins.

Received 24 November 2008; accepted 12 February 2009.




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