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Related Experiment Videos

Viral cell recognition and entry

M G Rossmann1

  • 1Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907-1392.

Protein Science : a Publication of the Protein Society
|October 1, 1994
PubMed
Summary
This summary is machine-generated.

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Rhinovirus binds to cells via intercellular adhesion molecule-1 (ICAM-1) in a viral canyon. A pocket factor binding site overlaps the receptor site, regulating viral RNA entry.

Area of Science:

  • Virology
  • Structural Biology
  • Drug Discovery

Background:

  • Rhinovirus infection begins with cell-surface receptor recognition.
  • Major rhinovirus serotypes utilize intercellular adhesion molecule-1 (ICAM-1) for attachment.
  • Viral attachment triggers conformational changes leading to genomic RNA release.

Purpose of the Study:

  • To structurally characterize the interaction between rhinovirus and its cellular receptor.
  • To identify potential drug-binding sites for inhibiting viral entry.
  • To elucidate the role of the "pocket factor" in viral uncoating and RNA release.

Main Methods:

  • X-ray crystallography and sequence comparisons to predict the receptor binding site.
  • Electron microscopy of human rhinovirus 14 (HRV14) and HRV16 complexed with ICAM-1.

Related Experiment Videos

  • Analysis of hydrophobic drug compound binding within a pocket beneath the viral canyon.

    • Main Results:

    • Electron microscopy confirmed the canyon as the ICAM-1 binding site on HRV14 and HRV16.
    • A hydrophobic pocket adjacent to the canyon binds inhibitory drug compounds.
    • This pocket also binds an unidentified "pocket factor," overlapping the ICAM-1 binding site.

    Conclusions:

    • The viral canyon is the primary binding site for intercellular adhesion molecule-1 (ICAM-1).
    • Drug compounds binding to a hydrophobic pocket can inhibit rhinovirus attachment and uncoating.
    • Competition between the pocket factor and ICAM-1 at the binding site regulates viral RNA entry into the cell.