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Host cell proteases controlling virus pathogenicity

H D Klenk1, W Garten

  • 1Institut für Virologie, Philipps-Universität Marburg, Germany.

Trends in Microbiology
|February 1, 1994
PubMed
Summary

Viral glycoproteins are mostly cleaved by intracellular proteases, but some use secreted proteases. This interaction influences viral infection spread, host range, and pathogenicity.

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Area of Science:

  • Virology
  • Molecular Biology
  • Protease Function

Background:

  • Many viral glycoproteins require post-translational proteolysis for maturation and function.
  • Proteolytic cleavage is a critical step in the viral life cycle, affecting infectivity.

Purpose of the Study:

  • To investigate the distinct roles of intracellular versus secreted proteases in viral glycoprotein processing.
  • To understand how protease availability in different host systems impacts viral characteristics.

Main Methods:

  • Comparative analysis of viral glycoprotein cleavage sites.
  • Examination of protease activity in various host cell environments.
  • Correlation of cleavage mechanisms with viral spread and pathogenicity data.

Main Results:

  • Most viral glycoproteins are processed by common intracellular proteases.
  • A subset of viral glycoproteins are cleaved by specialized secreted proteases found in limited hosts.
  • Differential protease access impacts viral infection dynamics.

Conclusions:

  • The type of protease (intracellular vs. secreted) involved in viral glycoprotein processing is a key determinant of viral behavior.
  • Host-specific protease availability can shape viral tropism and virulence.
  • Targeting these protease-host interactions could offer novel antiviral strategies.

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