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Authors propose a model whereby multiple components of the nuclear import machinery and nuclear pore complex help position MX2 at the nuclear envelope to promote MX2-mediated restriction of HIV-1.
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Here, the authors show that HIV-1 capsid can bind multiple nucleoporins that impacts HIV-1 infection in a manner that is strikingly dependent on cell-type, cell-cycle, and cyclophilin A (CypA). They also show that nucleoporins mediate the function of the antiviral protein MX2, and that MX2 can variably inhibit non-viral nuclear localization signal function.
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Study identifies MxB as a potent pan-herpesvirus restriction factor which blocks the uncoating of viral DNA from the incoming viral capsid.
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These data demonstrate that human MXB but not other human or murine MX proteins inhibit murine cytomegalovirus propagation. Evidently, the viral protein expression was delayed and the viral DNA amount in nucleus was diminished in MXB expressing cells indicating an obstruction of nuclear entry.
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Therefore, these results demonstrate the importance of MxB in alpha interferon-mediated inhibition of HIV-1 infection.
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The dynamin-like MxB GTPase serves as a broadly acting intracellular restriction factor that controls retrovirus as well as herpesvirus infections.
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MxB dimers form higher order oligomers that restrict retroviral replication by binding to the viral capsid. [review]
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These experiments suggested that MxB does not contribute to the HIV-1 restriction observed in IFN-alpha-treated human cells.
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Together, the data demonstrate that interferon-beta inhibits foamy virus early in infection and that MxB is not a restriction factor of foamy virus.
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We propose that lower-order oligomerization of MX2 is sufficient for the effective inhibition of human immunodeficiency virus type 1.
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Study analyzed the evolutionary history of MX2 at the inter- and intraspecific level and use this information to identify a haplotype that associates with natural resistance to HIV-1 infection in humans; the ancestral (G) allele of rs2074560 protects from HIV-1 infection with a recessive effect.
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The high prevalence of MxB-resistant mutations in the CypA-binding loop indicates the significant selective pressure of MxB on HIV-1 replication in vivo.
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MxB inhibits HIV-1 by interfering with minimally two steps of infection, nuclear entry and post-nuclear trafficking and/or integration, without destabilizing the inherent catalytic activity of viral preintegration complexes.
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HIV-seronegative women who use Depo-Provera have the highest levels of Mx2 expression, highlighting a possible mechanism for hormonal modulation of HIV resistance.
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The amino-terminal domain of Mx2/MxB-dependent interaction with the HIV-1 capsid has been characterized.
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MxB oligomerization is important for the ability of MxB to bind to the HIV-1 core proteins.
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A triple-arginine motif in the amino-terminal domain and oligomerization are required for HIV-1 inhibition by human MX2.
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structural analysis of assembly of human anti-HIV dynamin-like protein MxB/Mx2
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MxB binding to the HIV-1 capsid.
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To identify protein domains of MX2 that specify HIV-1 inhibition.
