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Related Experiment Videos

Cooperativity in viral fusion.

R Blumenthal1

  • 1Section on Membrane Structure and Function, NCI, Bethesda, MD 20892.

Cell Biophysics
|January 1, 1988
PubMed
Summary
This summary is machine-generated.

This study presents a model for viral membrane fusion, showing how H+ binding to spike glycoproteins triggers conformational changes that drive membrane fusion. The model accurately predicts fusion rates for Vesicular Stomatitis virus.

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Area of Science:

  • Biophysics
  • Virology
  • Molecular Biology

Background:

  • Membrane fusion is critical for viral entry and requires viral glycoproteins.
  • Viral spike glycoproteins are proposed to act as allosteric proteins undergoing conformational changes.
  • Proton (H+) concentration is a key environmental factor influencing viral fusion.

Purpose of the Study:

  • To develop a simple biophysical model for membrane fusion mediated by viral spike glycoproteins.
  • To investigate the role of allosteric conformational transitions in viral fusion.
  • To establish a quantitative relationship between ligand (H+) concentration and fusion rates.

Main Methods:

  • Development of a mathematical model for allosteric protein conformational transitions.
  • Derivation of an equation describing fusion rates based on ligand concentration, dissociation constant (Kd), equilibrium constant (L), and subunit number (n).

Related Experiment Videos

  • Fitting the derived equation to experimental data for Vesicular Stomatitis virus (VSV) fusion.
  • Main Results:

    • The model successfully describes membrane fusion as a process driven by H+-induced allosteric changes in viral spike proteins.
    • An equation was derived relating fusion rates to H+ concentration, Kd, L, and n.
    • The model parameters (pKd=6.3, L=1000, n=6) provided a good fit to VSV fusion data.

    Conclusions:

    • Viral spike glycoproteins can act as allosteric effectors, with H+ binding inducing conformational changes that mediate membrane fusion.
    • The developed model provides a quantitative framework for understanding pH-dependent viral fusion.
    • This work offers insights into the molecular mechanisms underlying viral entry and infection.