Journal
FEBS JOURNAL
Volume 289, Issue 13, Pages 3642-3654Publisher
WILEY
DOI: 10.1111/febs.16017
Keywords
antiviral factor; downregulation; MARCH8; transmembrane protein; viral envelope
Categories
Funding
- Japan Society for the Promotion of Science (KAKENHI) [18K07156, 21K07060]
- Grants-in-Aid for Scientific Research [18K07156, 21K07060] Funding Source: KAKEN
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MARCH8 is a novel antiviral factor that reduces viral infectivity by downregulating envelope glycoproteins from the cell surface, and it has multiple mechanisms for inhibiting virus infection.
Membrane-associated RING-CH (MARCH) family member proteins are RING-finger E3 ubiquitin ligases that are known to downregulate cellular transmembrane proteins. MARCH8 is a novel antiviral factor that inhibits HIV-1 envelope glycoprotein and vesicular stomatitis virus G by downregulating these envelope glycoproteins from the cell surface, resulting in their reduced incorporation into virions. More recently, we have found that MARCH8 reduces viral infectivity via two different mechanisms. Additionally, several groups have reported further antiviral or virus-supportive functions of the MARCH8 protein and its other cellular mechanisms. In this review, we summarize the current knowledge about the molecular mechanisms by which MARCH8 can regulate cellular homeostasis and inhibit and occasionally support enveloped virus infection.
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