ArticleJournal of biomedical science2014
SARS-CoV envelope protein palmitoylation or nucleocapid association is not required for promoting virus-like particle production.
Article in Journal of biomedical science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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
23 citing papers in PubMed, 40 citations in OpenAlex.
- Palmitoylation of SARS-CoV-2 Envelope protein is central to virus particle formation.Journal of virology · 2024Article
- ER-export and ARFRP1/AP-1-dependent delivery of SARS-CoV-2 Envelope to lysosomes controls late stages of viral replication.Science advances · 2024Article
- Cryo-electron microscopy in the fight against COVID-19-mechanism of virus entry.Frontiers in molecular biosciences · 2023Review
- Nanomedicine approaches to reduce cytokine storms in severe infections.Drug discovery today · 2022Review
- Viroporins: Structure, function, and their role in the life cycle of SARS-CoV-2.The international journal of biochemistry & cell biology · 2022Review
- Phase separation by the SARS-CoV-2 nucleocapsid protein: Consensus and open questions.The Journal of biological chemistry · 2022Review
- Protein Palmitoylation Modification During Viral Infection and Detection Methods of Palmitoylated Proteins.Frontiers in cellular and infection microbiology · 2022Review
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- Article
- S-acylation controls SARS-CoV-2 membrane lipid organization and enhances infectivity.Developmental cell · 2021Article
- Article
- Characterization of the SARS-CoV-2 E Protein: Sequence, Structure, Viroporin, and Inhibitors.Protein science : a publication of the Protein Society · 2021Review
- Effects of SARS-CoV-2 mutations on protein structures and intraviral protein-protein interactions.Journal of medical virology · 2021Article
- Genomic and proteomic mutation landscapes of SARS-CoV-2.Journal of medical virology · 2021Article
- The SARS-Coronavirus Infection Cycle: A Survey of Viral Membrane Proteins, Their Functional Interactions and Pathogenesis.International journal of molecular sciences · 2021Review
- Structure and Function of Major SARS-CoV-2 and SARS-CoV Proteins.Bioinformatics and biology insights · 2021Review
- Palmitoylation of the Bovine Foamy Virus Envelope Glycoprotein Is Required for Viral Replication.Viruses · 2020Article
- Structural Proteins in Severe Acute Respiratory Syndrome Coronavirus-2.Archives of medical research · 2020Review
- Structural Characterization of SARS-CoV-2: Where We Are, and Where We Need to Be.Frontiers in molecular biosciences · 2020Review
- Severe acute respiratory syndrome coronavirus spike protein counteracts BST2-mediated restriction of virus-like particle release.Journal of medical virology · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundCoronavirus membrane (M) proteins are capable of interacting with nucleocapsid (N) and envelope (E) proteins. Severe acute respiratory syndrome coronavirus (SARS-CoV) M co-expression with either N or E is sufficient for producing virus-like particles (VLPs), although at a lower level compared to M, N and E co-expression. Whether E can release from cells or E/N interaction exists so as to contribute to enhanced VLP production is unknown. It also remains to be determined whether E palmitoylation or disulfide bond formation plays a role in SARS-CoV virus assembly.
resultsSARS-CoV N is released from cells through an association with E protein-containing vesicles. Further analysis suggests that domains involved in E/N interaction are largely located in both carboxyl-terminal regions. Changing all three E cysteine residues to alanines did not exert negative effects on E release, E association with N, or E enhancement of VLP production, suggesting that E palmitoylation modification or disulfide bond formation is not required for SARS-CoV virus assembly. We found that removal of the last E carboxyl-terminal residue markedly affected E release, N association, and VLP incorporation, but did not significantly compromise the contribution of E to efficient VLP production.
conclusionsThe independence of the SARS-CoV E enhancement effect on VLP production from its viral packaging capacity suggests a distinct SARS-CoV E role in 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.