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Autographa californica multiple nucleopolyhedrovirus ORF 23 null mutant produces occlusion-derived virions with fewer

Ian-Ling Yu1, Doug Bray1, Ying-Chu Lin2

  • 1Department of Biological Sciences, University of Lethbridge, Lethbridge, AB T1K 3M4, Canada.

The Journal of General Virology
|March 7, 2009
PubMed

Insights

Autographa californica multiple nucleopolyhedrovirus (AcMNPV) F protein (Ac23) is not essential for fusion but influences virion structure and host death. Ac23 plays a distinct role from GP64 in AcMNPV infection.

Area of Science:

  • Virology
  • Molecular Biology
  • Insect Pathology

Background:

  • Baculoviruses, such as AcMNPV, utilize envelope fusion proteins for infection.
  • GP64 is a known fusogenic protein essential for AcMNPV propagation.
  • The F homologue (Ac23) in AcMNPV is non-essential and fusion-incompetent in standard assays, yet impacts host mortality.

Purpose of the Study:

  • To investigate the role of the AcMNPV F homologue (Ac23) in viral structure and infection dynamics.
  • To compare the functions of Ac23 with the essential fusion protein GP64.

Main Methods:

  • Analysis of occlusion bodies (OBs) and occlusion-derived virions (ODVs) from Ac23-null mutants and control viruses.
  • Characterization of ODV nucleocapsid content.
  • Infection assays using recombinant AcMNPV expressing Ac23-green fluorescent protein (gfp) in Sf9 cells.
  • Confocal microscopy to visualize Ac23-gfp localization.

Main Results:

  • Ac23-null OBs showed a significantly higher percentage of ODVs with single nucleocapsids (44.6%) compared to controls (11.3%).
  • OB size and ODV content did not differ significantly between Ac23-null and control viruses.
  • Ac23-gfp fluorescence localized to the perinuclear region in infected Sf9 cells, a pattern distinct from GP64.

Conclusions:

  • AcMNPV F protein (Ac23) influences the structural integrity of ODVs, specifically nucleocapsid formation.
  • Ac23 plays a role beyond envelope fusion, potentially in viral assembly or egress.
  • Ac23 and GP64 have distinct and non-redundant functions during AcMNPV infection.

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