1887

Abstract

The F protein is the major glycoprotein present in the envelopes of budded virus (BV) of members of the family . The F protein mediates low-pH-activated fusion with insect cell membranes. Baculovirus F proteins are synthesized as a precursor (F) and cleaved post-translationally into two disulfide-bonded subunits, F (C-terminal, large subunit) and F (N-terminal, small subunit). Recently, -linked glycosylation of the F and F subunits of (HearNPV) was demonstrated [ Long, G., Westenberg, M., Wang, H., Vlak, J. M. & Hu, Z. (2006) . , 839–846]. Sequence analysis frequently predicts that one or more -linked glycosylation sites are present in the F subunit of baculovirus F proteins. -glycans on envelope fusion proteins are usually required for proper conformational integrity and biological function, such as infectivity. This study examined the importance of -linked glycosylation of the F subunit of HearNPV by site-directed mutagenesis. The only putative -linked glycosylation site in F was eliminated by mutating asparagine (N) to glutamine (Q), resulting in the mutant HearNPV. When inserted into an -null HearNPV and a -null bacmid of , infectious BV could be retrieved that contained unglycosylated F. The virulence of HearNPV was enhanced, as BV was produced earlier after infection and yielded larger plaques than -null HearNPV repaired with the wild-type gene. HearNPV BV also induced much more efficient low-pH-activated syncytium formation. These results indicate that -linked glycosylation of the HearNPV baculovirus F subunit is not essential for viral infectivity and suggest that it is involved in BV production and fusogenicity.

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2007-02-01
2024-04-19
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