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MARCH8: the tie that binds to viruses

Takuya Tada1,2, Yanzhao Zhang1, Hideaki Fujita3

  • 1Department of Pathology, National Institute of Infectious Diseases, Tokyo, Japan.

The FEBS Journal
|May 16, 2021
PubMed

Insights

Membrane-associated RING-CH (MARCH) 8 protein acts as an antiviral factor by reducing viral glycoproteins on cell surfaces. This novel E3 ubiquitin ligase impacts viral infectivity through multiple mechanisms, regulating cellular homeostasis and enveloped virus infections.

Area of Science:

  • Virology
  • Cell Biology
  • Biochemistry

Background:

  • Membrane-associated RING-CH (MARCH) proteins are E3 ubiquitin ligases.
  • MARCH proteins downregulate cellular transmembrane proteins.
  • MARCH8 is identified as a novel antiviral factor.

Purpose of the Study:

  • To review the molecular mechanisms of MARCH8.
  • To summarize MARCH8's role in regulating cellular homeostasis.
  • To discuss MARCH8's dual role in enveloped virus infection.

Main Methods:

  • Literature review of existing studies on MARCH8.
  • Analysis of MARCH8's function as an E3 ubiquitin ligase.
  • Investigation of MARCH8's impact on viral glycoproteins and infectivity.

Main Results:

  • MARCH8 downregulates HIV-1 envelope glycoprotein and VSV-G from the cell surface.
  • MARCH8 reduces viral infectivity through at least two distinct mechanisms.
  • MARCH8 exhibits both antiviral and virus-supportive functions.

Conclusions:

  • MARCH8 plays a complex role in modulating viral infections.
  • Understanding MARCH8's mechanisms is crucial for antiviral strategies.
  • MARCH8 influences cellular homeostasis and enveloped virus lifecycle.
Keywords:
MARCH8antiviral factordownregulationtransmembrane proteinviral envelope

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