{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["11(38)"],"submitter":["Wang J"],"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"],"journal":["Science advances"],"pagination":["eadw4609"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12448087"],"repository":["biostudies-literature"],"pubmed_title":["Nipah virus matrix protein uses cortical actin to stabilize the virus assembly sites and promote budding."],"pmcid":["PMC12448087"],"pubmed_authors":["Matta GL","Liu J","Wang Q","Kliemke V","Liu Q","Zhang M","Luo Y","Wang J","Liu G"],"additional_accession":[]},"is_claimable":false,"name":"Nipah virus matrix protein uses cortical actin to stabilize the virus assembly sites and promote budding.","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","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Sep","modification":"2026-07-15T05:50:11.489Z","creation":"2026-06-29T03:19:42.819Z"},"accession":"S-EPMC12448087","cross_references":{"pubmed":["40971433"],"doi":["10.1126/sciadv.adw4609"]}}