1887

Abstract

Feline calicivirus (FCV) icosahedral viral capsids are composed of dozens of structural subunits that rely on cellular chaperones to self-assemble in an orderly fashion. Here, we report that the heat shock protein 90 (Hsp90) inhibition significantly reduced FCV particle production, suggesting a role in the replicative cycle. We found that Hsp90 inhibition was not related to the synthesis or stability of the early proteins that translate from the gRNA nor to the minor capsid protein VP2 but with a reduction in the major capsid protein VP1 levels, both translated late in infection from the subgenomic RNAs. Reduction in VP1 levels was observed despite an augment of the leader of the capsid (LC)–VP1 precursor levels, from which the LC and VP1 proteins are produced after proteolytic processing by NS6/7. The direct interaction of VP1 with Hsp90 was observed in infected cells. These results suggest that upon release from the polyprotein precursor, VP1 becomes a client of Hsp90 and that this interaction is required for an efficient FCV replicative cycle.

Funding
This study was supported by the:
  • Conahcyt (Award Proyecto 302965, PRONAII 3: Infecciones virales del tracto gastrointestinal.)
    • Principle Award Recipient: AnaLorena Gutiérrez Escolano
  • Conacyt (Award 724626)
    • Principle Award Recipient: NotApplicable
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/content/journal/jgv/10.1099/jgv.0.002030
2024-10-07
2024-11-11
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