ArticleVirology journal2009
Mutagenesis of the transmembrane domain of the SARS coronavirus spike glycoprotein: refinement of the requirements for SARS coronavirus cell entry.
Article in Virology journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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31 citing papers in PubMed, 59 citations in OpenAlex.
- The impact of clade B lineage 5 MERS coronaviruses spike mutations from 2015 to 2023 on virus entry and replication competence.PLoS pathogens · 2026Article
- 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
- The sequence and structural integrity of the SARS-CoV-2 Spike protein transmembrane domain is crucial for viral entry.Communications biology · 2025Article
- A novel linear B-cell epitope on S2 protein of transmissible gastroenteritis virus identified using a monoclonal antibody.BMC veterinary research · 2025Article
- Entry Inhibitors of SARS-CoV-2 Targeting the Transmembrane Domain of the Spike Protein.Viruses · 2025Article
- SARS-CoV-2 entry and fusion are independent of ACE2 localization to lipid rafts.Journal of virology · 2025Article
- Molecular and phylogenetic analysis of transmissible gastroenteritis virus strain VET-16, isolated from piglets in Vietnam.Archives of virology · 2024Article
- Inconspicuous Yet Indispensable: The Coronavirus Spike Transmembrane Domain.International journal of molecular sciences · 2023Review
- Article
- Cytoplasmic Tail Truncation Stabilizes S1-S2 Association and Enhances S Protein Incorporation into SARS-CoV-2 Pseudovirions.Journal of virology · 2023Article
- Genomic surveillance of genes encoding the SARS-CoV-2 spike protein to monitor for emerging variants on Jeju Island, Republic of Korea.Frontiers in microbiology · 2023Article
- A Uniquely Stable Trimeric Model of SARS-CoV-2 Spike Transmembrane Domain.International journal of molecular sciences · 2022Article
- Mucosal administration of a live attenuated recombinant COVID-19 vaccine protects nonhuman primates from SARS-CoV-2.NPJ vaccines · 2022Article
- Whole genome sequence analysis showing unique SARS-CoV-2 lineages of B.1.524 and AU.2 in Malaysia.PloS one · 2022Article
- Article
- Full-Length Computational Model of the SARS-CoV-2 Spike Protein and Its Implications for a Viral Membrane Fusion Mechanism.Viruses · 2021Article
- Article
- A trimeric hydrophobic zipper mediates the intramembrane assembly of SARS-CoV-2 spike.bioRxiv : the preprint server for biology · 2021Article
- A comparative analysis of SARS-CoV-2 antivirals characterizes 3CLJournal of virology · 2021Article
- A comparative analysis of SARS-CoV-2 antivirals in human airway models characterizes 3CLbioRxiv : the preprint server for biology · 2021Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe spike protein (S) of SARS Coronavirus (SARS-CoV) mediates entry of the virus into target cells, including receptor binding and membrane fusion. Close to or in the viral membrane, the S protein contains three distinct motifs: a juxtamembrane aromatic part, a central highly hydrophobic stretch and a cysteine rich motif. Here, we investigate the role of aromatic and hydrophobic parts of S in the entry of SARS CoV and in cell-cell fusion. This was investigated using the previously described SARS pseudotyped particles system (SARSpp) and by fluorescence-based cell-cell fusion assays.
resultsMutagenesis showed that the aromatic domain was crucial for SARSpp entry into cells, with a likely role in pore enlargement.Introduction of lysine residues in the hydrophobic stretch of S also resulted in a block of entry, suggesting the borders of the actual transmembrane domain. Surprisingly, replacement of a glycine residue, situated close to the aromatic domain, with a lysine residue was tolerated, whereas the introduction of a lysine adjacent to the glycine, was not. In a model, we propose that during fusion, the lateral flexibility of the transmembrane domain plays a critical role, as do the tryptophans and the cysteines.
conclusionsThe aromatic domain plays a crucial role in the entry of SARS CoV into target cells. The positioning of the aromatic domain and the hydrophobic domain relative to each other is another essential characteristic of this membrane fusion process.
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