{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Mohona S"],"funding":["NIAID NIH HHS","NCI NIH HHS","NIGMS NIH HHS","NIH HHS"],"pubmed_abstract":["Assembly of infectious coronaviruses requires spike (S) protein trafficking by host coatomer, typically via a dibasic signal in the S cytoplasmic tail. However, the human embecoviruses HKU1 and OC43, as well as the model virus MHV, lack this motif. Here we identify a conserved His-x-Asp (HxD) sequence that functions as an unconventional coatomer-binding signal. Structural and biochemical analyses show that the MHV HxD motif engages coatomer subunits through distinct conformations, while cellular imaging demonstrates its role in directing S to assembly sites with the viral M-protein. Disruption of HxD-coatomer interactions impairs S incorporation and provokes compensatory viral adaptations, including emergence of a canonical dibasic motif or mutations in M-protein. Electron microscopy furth"],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2025.10.16.682669"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12633080"],"repository":["biostudies-literature"],"pubmed_title":["An unconventional HxD motif orchestrates coatomer-dependent coronavirus morphogenesis."],"pmcid":["PMC12633080"],"funding_grant_id":["P30 CA134274","R01 GM150187","S10 OD034431","P30 GM133893","R21 AI176252"],"pubmed_authors":["Klose T","Qing E","Doray B","Gallagher T","Hasan SS","Shakya AK","Dey D","Amaro RE","Jennings BC","Erramilli S","Kossiakoff AA","Mohona S","Singh S","Kearns FL","Jemison K"],"additional_accession":[]},"is_claimable":false,"name":"An unconventional HxD motif orchestrates coatomer-dependent coronavirus morphogenesis.","description":"Assembly of infectious coronaviruses requires spike (S) protein trafficking by host coatomer, typically via a dibasic signal in the S cytoplasmic tail. However, the human embecoviruses HKU1 and OC43, as well as the model virus MHV, lack this motif. Here we identify a conserved His-x-Asp (HxD) sequence that functions as an unconventional coatomer-binding signal. Structural and biochemical analyses show that the MHV HxD motif engages coatomer subunits through distinct conformations, while cellular imaging demonstrates its role in directing S to assembly sites with the viral M-protein. Disruption of HxD-coatomer interactions impairs S incorporation and provokes compensatory viral adaptations, including emergence of a canonical dibasic motif or mutations in M-protein. Electron microscopy furth","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Oct","modification":"2026-06-04T03:21:33.982Z","creation":"2026-06-04T03:12:42.747Z"},"accession":"S-EPMC12633080","cross_references":{"pubmed":["41279991"],"doi":["10.1101/2025.10.16.682669"]}}