Hsp90 Activity Is Necessary for the Maturation of Rabies Virus Polymerase

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Abstract
Mononegavirales is an order of viruses with a genome in the form of a non-segmented negative-strand RNA that encodes several proteins. The functional polymerase complex of these viruses is composed of two proteins: a large protein (L) and a phosphoprotein (P). The replication of viruses from this order depends on Hsp90 chaperone activity. Previous studies have demonstrated that Hsp90 inhibition results in the degradation of mononegaviruses L protein, with exception of the rabies virus, for which the degradation of P protein was observed. Here, we demonstrated that Hsp90 inhibition does not affect the expression of rabies L and P proteins, but it inhibits binding of the P protein and L protein into functional viral polymerase. Rabies and the vesicular stomatitis virus, but not the measles virus, L proteins can be expressed independently of the presence of a P protein and in the presence of an Hsp90 inhibitor. Our results suggest that the interaction of L proteins with P proteins and Hsp90 in the process of polymerase maturation may be a process specific to particular viruses.
Funding Information
  • Narodowe Centrum Nauki (2016/23/B/NZ6/02536, POWR.03.02.00-00-1028/17-00)
  • European Science Foundation (2016/23/B/NZ6/02536, POWR.03.02.00-00-1028/17-00)
  • Mossakowski Medical Research Institute, Warsaw, Poland (2016/23/B/NZ6/02536, POWR.03.02.00-00-1028/17-00)

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