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The emerging roles of MARCH8 in viral infections: A double-edged Sword

Changqing Yu1, Qiang Liu2, Zhuo Zhao3

  • 1Engineering Center of Agricultural Biosafety Assessment and Biotechnology, School of Advanced Agricultural Sciences, Yibin Vocational and Technical College, Yibin, People's Republic of China.

Plos Pathogens
|September 14, 2023
PubMed

Insights

The host protein MARCH8 has dual antiviral functions: degrading viral proteins or trapping them in cellular compartments. Some pathogens exploit MARCH8, highlighting its complex role in infection and potential for new antiviral therapies.

Area of Science:

  • Virology
  • Cell Biology
  • Immunology

Background:

  • MARCH8 (membrane-associated RING-CH 8) is an E3 ubiquitin ligase regulating transmembrane protein turnover.
  • MARCH8 exhibits significant antiviral activities against various viruses.
  • MARCH8's functions are crucial in host-pathogen interactions.

Purpose of the Study:

  • To review the antiviral mechanisms of MARCH8.
  • To explore how viruses evade MARCH8 restriction.
  • To discuss MARCH8's duplex role in host-pathogen interactions.

Main Methods:

  • Literature review of MARCH8's antiviral functions.
  • Analysis of MARCH8's interaction with viral components.
  • Examination of MARCH8's role in viral entry and replication.

Main Results:

  • MARCH8 employs two distinct antiviral modes: cytoplasmic tail-dependent (CTD) degradation and cytoplasmic tail-independent (CTI) trapping of viral envelope glycoproteins (VEGs).
  • The CTI mode involves hijacking cellular furin to prevent VEG cleavage, with the MARCH8 C-terminal tyrosine-based motif (TBM) being essential.
  • Viruses and bacteria can hijack MARCH8 to facilitate their invasion, demonstrating its dual role.

Conclusions:

  • MARCH8 is a potent antiviral factor with versatile mechanisms.
  • Understanding viral evasion strategies targeting MARCH8 is key for therapeutic development.
  • MARCH8 represents a promising target for novel antiviral strategies.

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