<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Mo Q</submitter><funding>European Union’s Horizon 2020 project</funding><funding>National Natural Science Foundation of China</funding><funding>National Key Research and Development Program of China</funding><funding>Youth Innovation Promotion Association of the Chinese Academy of Sciences</funding><pagination>e1009129</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC7746268</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>16(12)</volume><pubmed_abstract>Bunyavirus ribonucleoprotein (RNP) that is assembled by polymerized nucleoproteins (N) coating a viral RNA and associating with a viral polymerase can be both the RNA synthesis machinery and the structural core of virions. Bunyaviral N and RNP thus could be assailable targets for host antiviral defense; however, it remains unclear which and how host factors target N/RNP to restrict bunyaviral infection. By mass spectrometry and protein-interaction analyses, we here show that host protein MOV10 targets the N proteins encoded by a group of emerging high-pathogenic representatives of bunyaviruses including severe fever with thrombocytopenia syndrome virus (SFTSV), one of the most dangerous pathogens listed by World Health Organization, in RNA-independent manner. MOV10 that was further shown t</pubmed_abstract><journal>PLoS pathogens</journal><pubmed_title>Host restriction of emerging high-pathogenic bunyaviruses via MOV10 by targeting viral nucleoprotein and blocking ribonucleoprotein assembly.</pubmed_title><pmcid>PMC7746268</pmcid><funding_grant_id>31870162</funding_grant_id><funding_grant_id>2018YFA0507202</funding_grant_id><funding_grant_id>653316</funding_grant_id><pubmed_authors>Mo Q</pubmed_authors><pubmed_authors>Wang H</pubmed_authors><pubmed_authors>Deng F</pubmed_authors><pubmed_authors>Ning YJ</pubmed_authors><pubmed_authors>Xu Z</pubmed_authors></additional><is_claimable>false</is_claimable><name>Host restriction of emerging high-pathogenic bunyaviruses via MOV10 by targeting viral nucleoprotein and blocking ribonucleoprotein assembly.</name><description>Bunyavirus ribonucleoprotein (RNP) that is assembled by polymerized nucleoproteins (N) coating a viral RNA and associating with a viral polymerase can be both the RNA synthesis machinery and the structural core of virions. Bunyaviral N and RNP thus could be assailable targets for host antiviral defense; however, it remains unclear which and how host factors target N/RNP to restrict bunyaviral infection. By mass spectrometry and protein-interaction analyses, we here show that host protein MOV10 targets the N proteins encoded by a group of emerging high-pathogenic representatives of bunyaviruses including severe fever with thrombocytopenia syndrome virus (SFTSV), one of the most dangerous pathogens listed by World Health Organization, in RNA-independent manner. MOV10 that was further shown t</description><dates><release>2020-01-01T00:00:00Z</release><publication>2020 Dec</publication><modification>2026-04-29T21:30:36.444Z</modification><creation>2021-02-20T17:33:55Z</creation></dates><accession>S-EPMC7746268</accession><cross_references><pubmed>33284835</pubmed><doi>10.1371/journal.ppat.1009129</doi></cross_references></HashMap>