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The interferon-inducible antiviral GTPase MxB promotes capsid disassembly and genome release of herpesviruses

ABSTRACT: Host proteins sense viral products and induce defense mechanisms, particularly in immune cells. Using cell-free assays and quantitative mass spectrometry, we determined the interactomes of capsidhost protein complexes of herpes simplex virus, and identified the large dynamin-like GTPase myxovirus resistance protein B (MxB) as an interferon-inducible protein interacting with capsids. Electron microscopy analyses showed that cytosols containing MxB had the remarkable capability to disassemble the icosahedral capsids of herpes simplex viruses and varicella zoster virus into flat sheets of connected triangular faces. In contrast, capsids remained intact in cytosols with MxB mutants unable to hydrolyze GTP or to dimerize. Our data suggest that MxB senses herpesviral capsids, mediates their disassembly, and thereby restricts the efficiency of nuclear targeting of incoming capsids and/or the assembly of progeny capsids. The resulting premature release of viral genomes from capsids may enhance the activation of DNA sensors, and thereby amplify the innate immune responses.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human) Human Herpesvirus 1 (strain 17) (hhv-1) (human Herpes Simplex Virus 1)

TISSUE(S): Macrophage

SUBMITTER: Virginie Girault

LAB HEAD: Andreas Pichlmair

PROVIDER: PXD028276 | Pride | 2022-05-06

REPOSITORIES: Pride

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			Action	DRS
	20190416_QEp5_AnPi_SA_01KCl_TrypCaps_A4_13.raw	Raw
	20190416_QEp5_AnPi_SA_01KCl_TrypCaps_B4_14.raw	Raw
	20190416_QEp5_AnPi_SA_01KCl_TrypCaps_C4_15.raw	Raw
	20190416_QEp5_AnPi_SA_01KCl_TrypCaps_D4_16.raw	Raw
	20190416_QEp5_AnPi_SA_01KCl_TrypCaps_MacropCyt_A10_37.raw	Raw

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