ArticleJournal of virology2010
A conserved domain in the coronavirus membrane protein tail is important for virus assembly.
Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers, 3 of them syntheses that pooled it.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
101 citing papers in PubMed, 3 syntheses or guidelines pooled it, 187 citations in OpenAlex.
- Review: A systematic review of virus-like particles of coronavirus: Assembly, generation, chimerism and their application in basic research and in the clinic.International journal of biological macromolecules · 2022Pooled it
- Promising Antiviral Activities of Natural Flavonoids against SARS-CoV-2 Targets: Systematic Review.International journal of molecular sciences · 2021Pooled it
- Drug targets for corona virus: A systematic review.Indian journal of pharmacologyPooled it
- Coronavirus membrane protein with a fluorescent protein tag enables particle tracking for the study of virus assembly and egress in live cells.Journal of virology · 2026Article
- Beyond assembly: functions of the coronavirus M protein.Virology journal · 2026Review
- Structural mimics of SARS-CoV-2.Infection · 2026Review
- Clustering of SARS-CoV-2 membrane proteins in lipid bilayer membranes.PLoS computational biology · 2026Article
- Coronavirus genome packaging and nucleocapsid assembly.Journal of virology · 2026Review
- The structure and function of membrane protein in coronavirus infection and its applications in the development of vaccines and therapeutic drugs.Frontiers in microbiology · 2026Review
- Coronavirus membrane protein with a fluorescent protein tag enables tracking of virus particles in live cells.bioRxiv : the preprint server for biology · 2025Article
- Definition of the components required for selective packaging of coronavirus genomic RNA.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Midnolin inhibits coronavirus proliferation by degrading viral proteins.Journal of virology · 2025Article
- SIRT5-mediated desuccinylation of the porcine deltacoronavirus M protein drives pexophagy to enhance viral proliferation.PLoS pathogens · 2025Article
- Siglec-15 is a putative receptor for porcine epidemic diarrhea virus infection.Cellular and molecular life sciences : CMLS · 2025Article
- Article
- Effect of Exportin 1/XPO1 Nuclear Export Pathway Inhibition on Coronavirus Replication.Viruses · 2025Article
- Effect of exportin 1/XPO1 nuclear export pathway inhibition on coronavirus replication.bioRxiv : the preprint server for biology · 2024Article
- SARS-CoV-2 Assembly: Gaining Infectivity and Beyond.Viruses · 2024Review
- Review
- Coronavirus M Protein Trafficking in Epithelial Cells Utilizes a Myosin Vb Splice Variant and Rab10.Cells · 2024Article
41 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Coronavirus membrane (M) proteins play key roles in virus assembly, through M-M, M-spike (S), and M-nucleocapsid (N) protein interactions. The M carboxy-terminal endodomain contains a conserved domain (CD) following the third transmembrane (TM) domain. The importance of the CD (SWWSFNPETNNL) in mouse hepatitis virus was investigated with a panel of mutant proteins, using genetic analysis and transient-expression assays. A charge reversal for negatively charged E(121) was not tolerated. Lysine (K) and arginine (R) substitutions were replaced in recovered viruses by neutrally charged glutamine (Q) and leucine (L), respectively, after only one passage. E121Q and E121L M proteins were capable of forming virus-like particles (VLPs) when coexpressed with E, whereas E121R and E121K proteins were not. Alanine substitutions for the first four or the last four residues resulted in viruses with significantly crippled phenotypes and proteins that failed to assemble VLPs or to be rescued into the envelope. All recovered viruses with alanine substitutions in place of SWWS residues had second-site, partially compensating, changes in the first TM of M. Alanine substitution for proline had little impact on the virus. N protein coexpression with some M mutants increased VLP production. The results overall suggest that the CD is important for formation of the viral envelope by helping mediate fundamental M-M interactions and that the presence of the N protein may help stabilize M complexes during virus assembly.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.