ArticleThe Journal of biological chemistry2009
Role of spike protein endodomains in regulating coronavirus entry.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 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
50 citing papers in PubMed, 73 citations in OpenAlex.
- Role of the transmembrane domain in severe acute respiratory syndrome (SARS) coronavirus 2 spike for palmitoylation and membrane fusion.Protein science : a publication of the Protein Society · 2026Article
- SARS-CoV-2 Omicron variations reveal mechanisms controlling cell entry dynamics and antibody neutralization.PLoS pathogens · 2024Article
- Inconspicuous Yet Indispensable: The Coronavirus Spike Transmembrane Domain.International journal of molecular sciences · 2023Review
- Metabolic alterations upon SARS-CoV-2 infection and potential therapeutic targets against coronavirus infection.Signal transduction and targeted therapy · 2023Review
- Ongoing Positive Selection Drives the Evolution of SARS-CoV-2 Genomes.Genomics, proteomics & bioinformatics · 2022Article
- Article
- SARS-CoV-2 diverges from other betacoronaviruses in only partially activating the IRE1α/XBP1 ER stress pathway in human lung-derived cells.bioRxiv : the preprint server for biology · 2022Article
- Review
- Article
- Article
- Protein Palmitoylation Modification During Viral Infection and Detection Methods of Palmitoylated Proteins.Frontiers in cellular and infection microbiology · 2022Review
- COVID-19: the CaMKII-like system of S protein drives membrane fusion and induces syncytial multinucleated giant cells.Immunologic research · 2021Article
- Biochemical composition, transmission and diagnosis of SARS-CoV-2.Bioscience reports · 2021Review
- S-Acylation of Proteins of Coronavirus and Influenza Virus: Conservation of Acylation Sites in Animal Viruses and DHHC Acyltransferases in Their Animal Reservoirs.Pathogens (Basel, Switzerland) · 2021Article
- SARS-CoV-2 Disease through Viral Genomic and Receptor Implications: An Overview of Diagnostic and Immunology Breakthroughs.Microorganisms · 2021Review
- Common low complexity regions for SARS-CoV-2 and human proteomes as potential multidirectional risk factor in vaccine development.BMC bioinformatics · 2021Article
- Palmitoylation of the envelope membrane proteins GP5 and M of porcine reproductive and respiratory syndrome virus is essential for virus growth.PLoS pathogens · 2021Article
- SARS-CoV-2 Disease Adjuvant Therapies and Supplements Breakthrough for the Infection Prevention.Microorganisms · 2021Review
- Article
- The biogenesis of SARS-CoV-2 spike glycoprotein: multiple targets for host-directed antiviral therapy.Biochemical and biophysical research communications · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Enveloped viruses enter cells by viral glycoprotein-mediated binding to host cells and subsequent fusion of virus and host cell membranes. For the coronaviruses, viral spike (S) proteins execute these cell entry functions. The S proteins are set apart from other viral and cellular membrane fusion proteins by their extensively palmitoylated membrane-associated tails. Palmitate adducts are generally required for protein-mediated fusions, but their precise roles in the process are unclear. To obtain additional insights into the S-mediated membrane fusion process, we focused on these acylated carboxyl-terminal intravirion tails. Substituting alanines for the cysteines that are subject to palmitoylation had effects on both S incorporation into virions and S-mediated membrane fusions. In specifically dissecting the effects of endodomain mutations on the fusion process, we used antiviral heptad repeat peptides that bind only to folding intermediates in the S-mediated fusion process and found that mutants lacking three palmitoylated cysteines remained in transitional folding states nearly 10 times longer than native S proteins. This slower refolding was also reflected in the paucity of postfusion six-helix bundle configurations among the mutant S proteins. Viruses with fewer palmitoylated S protein cysteines entered cells slowly and had reduced specific infectivities. These findings indicate that lipid adducts anchoring S proteins into virus membranes are necessary for the rapid, productive S protein refolding events that culminate in membrane fusions. These studies reveal a previously unappreciated role for covalently attached lipids on the endodomains of viral proteins eliciting membrane fusion reactions.
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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.