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Related Experiment Videos

Trypsin-induced structural transformation in aquareovirus.

E L Nason1, S K Samal, B V Venkataram Prasad

  • 1Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas 77030, USA.

Journal of Virology
|June 23, 2000
PubMed
Summary

Aquareovirus infectivity is altered by trypsin. Short treatment removes outer spikes, enhancing cell entry, while prolonged treatment inactivates the virus by altering core structures.

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Area of Science:

  • Virology
  • Structural Biology
  • Molecular Biology

Background:

  • Aquareovirus (family Reoviridae) is a double-stranded RNA virus with a multi-layered capsid.
  • Proteolytic treatment with trypsin significantly affects Aquareovirus infectivity.
  • Optimal infectivity is achieved after 5 minutes of trypsin treatment, with prolonged exposure reducing it.

Purpose of the Study:

  • To investigate the structural basis of trypsin-induced alterations in Aquareovirus infectivity.
  • To elucidate the structural changes in the virion at various trypsin treatment intervals using cryo-electron microscopy.

Main Methods:

  • Three-dimensional electron cryo-microscopy (3D cryo-EM).
  • Proteolytic treatment of Aquareovirus with trypsin for varying durations.

Related Experiment Videos

  • Structural analysis of virions at different stages of trypsinization.

    • Main Results:

    • 5-minute trypsinization completely removes outer VP7 spikes, inducing conformational changes in underlying VP5 subunits, potentially aiding cell entry.
    • Prolonged trypsinization removes the outer capsid, creating a core particle, and alters the turret protein structure, shortening it and narrowing its channel.
    • Structural changes in the turret protein suggest implications for viral transcription activity.

    Conclusions:

    • Trypsin treatment induces significant structural modifications in Aquareovirus, correlating with changes in infectivity.
    • Outer spike removal and VP5 conformational changes are linked to enhanced cell entry.
    • Alterations in the turret protein structure likely regulate viral transcriptional activity.