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MARCH2 is upregulated in HIV-1 infection and inhibits HIV-1 production through envelope protein translocation or degradation.

MARCH2 is upregulated in HIV-1 infection and inhibits HIV-1 production through envelope protein translocation or degradation.
Author Information (click to view)

Zhang Y, Lu J, Liu X,


Zhang Y, Lu J, Liu X, (click to view)

Zhang Y, Lu J, Liu X,

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Virology 2018 03 21518() 293-300 pii 10.1016/j.virol.2018.02.003

Abstract

MARCH2 is one of the MARCH family E3 ligases, which contains eleven members that play pivotal roles in controlling the turn-over of membrane proteins, such as MHC class I, MHC class II, and cell surface receptors. In this study, we found the expression of MARCH2 to be upregulated upon HIV-1 infection. MARCH2 inhibits the production and infection of HIV-1 through ligase activity-dependent envelope protein degradation and/or intracellular retention, a mechanism shared by MARCH8 that also leads to the inhibition of HIV-1 infection. Nevertheless, unlike MARCH8 and other MARCH proteins whose transcription levels are unrelated to viral infection, the expression level of MARCH2 is markedly upregulated upon HIV-1 infection, conferring MARCH2 a unique role in monitoring and regulating the HIV-1 infection-associated process.

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