Viral Bcl2s' transmembrane domain interact with host Bcl2 proteins to control cellular apoptosis

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Maria Jesús García-Murria1, Gerard Duart1, Brayan Grau1

  • 1Department of Biochemistry and Molecular Biology, Institut de Biotecnologia i Biomedicina, Universitat de València, 46100, Burjassot, Spain.

Nature Communications
|November 28, 2020
PubMed

Insights

Viral Bcl2 proteins use transmembrane domains to interact with host cell proteins, controlling programmed cell death. Inhibiting these interactions offers a novel therapeutic strategy against viral infections.

Area of Science:

  • Molecular Biology
  • Virology
  • Cell Biology

Background:

  • Viruses manipulate programmed cell death using viral Bcl2 analogs (vBcl2s).
  • vBcl2s interact with host Bcl2 family proteins to regulate apoptosis.

Purpose of the Study:

  • To investigate the role of the carboxyl-terminal hydrophobic region of viral Bcl2s.
  • To determine if viral transmembrane domains mediate interactions with cellular Bcl2 proteins.

Main Methods:

  • Analysis of carboxyl-terminal hydrophobic regions of herpesviral and poxviral vBcl2s.
  • Investigating protein-protein interactions within the cell membrane.

Main Results:

  • Viral Bcl2s possess transmembrane domains (TMDs) capable of homo-oligomerization.
  • Viral TMDs mediate interactions with cellular Bcl2 TMDs within the membrane.
  • These intra-membrane interactions are crucial for regulating apoptosis.

Conclusions:

  • Viral TMDs are key mediators of vBcl2 function in controlling apoptosis.
  • Targeting these viral-cellular membrane interactions presents a potential therapeutic avenue for viral infections.

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