A role for molecular chaperone Hsc70 in reovirus outer capsid disassembly

Tijana Ivanovic, Melina A. Agosto, Kartik Chandran, Max L. Nibert

Research output: Contribution to journalArticlepeer-review

54 Scopus citations


After crossing the cellular membrane barrier during cell entry, most animal viruses must undergo further disassembly before initiating viral gene expression. In many cases, these disassembly mechanisms remain poorly defined. For this report, we examined a final step in disassembly of the mammalian reovirus outer capsid: cytoplasmic release of the central, δfragment of membrane penetration protein μ1 to yield the transcriptionally active viral core particle. An in vitro assay with reticulocyte lysate recapitulated the release of intact δ molecules. Requirements for activity in this system were shown to include a protein factor, ATP, and Mg2+ and K + ions, consistent with involvement of a molecular chaperone such as Hsc70. Immunodepletion of Hsc70 and Hsp70 impaired δ release, which was then rescued by addition of purified Hsc70. Hsc70 was associated with released δ molecules not only in the lysate but also during cell entry. We conclude that Hsc70 plays a defined role in reovirus outer capsid disassembly, during or soon after membrane penetration, to prepare the entering particle for gene expression and replication.

Original languageEnglish (US)
Pages (from-to)12210-12219
Number of pages10
JournalJournal of Biological Chemistry
Issue number16
StatePublished - Apr 20 2007

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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