<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>11(38)</volume><submitter>Wang J</submitter><pubmed_abstract>Several enveloped viruses, including paramyxoviruses, assemble and bud from the host plasma membrane (PM). Nipah virus (NiV), a deadly zoonotic paramyxovirus, uses its matrix protein (M) to drive virus assembly and budding through dimerization and PM interaction. We show that NiV-M-mediated virus-like particle (VLP) production depends on its interaction with host F-actin via its carboxyl-terminal domain. We demonstrate that F-actin retains NiV-M assembly sites at the PM by analyzing NiV-M assembly kinetics. Disrupting actin dynamics or NiV-M-actin interaction alters M nanoscale organization and reduces membrane retention, without affecting initial recruitment. We also show that the Arp2/3 complex, an actin-branching factor, promotes VLP production. Inhibiting Arp2/3 reduces NiV-M retention</pubmed_abstract><journal>Science advances</journal><pagination>eadw4609</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12448087</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Nipah virus matrix protein uses cortical actin to stabilize the virus assembly sites and promote budding.</pubmed_title><pmcid>PMC12448087</pmcid><pubmed_authors>Matta GL</pubmed_authors><pubmed_authors>Liu J</pubmed_authors><pubmed_authors>Wang Q</pubmed_authors><pubmed_authors>Kliemke V</pubmed_authors><pubmed_authors>Liu Q</pubmed_authors><pubmed_authors>Zhang M</pubmed_authors><pubmed_authors>Luo Y</pubmed_authors><pubmed_authors>Wang J</pubmed_authors><pubmed_authors>Liu G</pubmed_authors></additional><is_claimable>false</is_claimable><name>Nipah virus matrix protein uses cortical actin to stabilize the virus assembly sites and promote budding.</name><description>Several enveloped viruses, including paramyxoviruses, assemble and bud from the host plasma membrane (PM). Nipah virus (NiV), a deadly zoonotic paramyxovirus, uses its matrix protein (M) to drive virus assembly and budding through dimerization and PM interaction. We show that NiV-M-mediated virus-like particle (VLP) production depends on its interaction with host F-actin via its carboxyl-terminal domain. We demonstrate that F-actin retains NiV-M assembly sites at the PM by analyzing NiV-M assembly kinetics. Disrupting actin dynamics or NiV-M-actin interaction alters M nanoscale organization and reduces membrane retention, without affecting initial recruitment. We also show that the Arp2/3 complex, an actin-branching factor, promotes VLP production. Inhibiting Arp2/3 reduces NiV-M retention</description><dates><release>2025-01-01T00:00:00Z</release><publication>2025 Sep</publication><modification>2026-07-15T05:50:11.489Z</modification><creation>2026-06-29T03:19:42.819Z</creation></dates><accession>S-EPMC12448087</accession><cross_references><pubmed>40971433</pubmed><doi>10.1126/sciadv.adw4609</doi></cross_references></HashMap>