ArticleInternational journal of molecular sciences2022
SARS-CoV-2 Spike Protein Mutation at Cysteine-488 Impairs Its Golgi Localization and Intracellular S1/S2 Processing.
Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 10 citations in OpenAlex.
- MicroRNA-122-5p Targets FOXO3 to Mediate Podocyte Senescence and Proteinuria Induced by Angiotensin II Type 1 Receptor Autoantibodies in Preeclampsia.Reproductive sciences (Thousand Oaks, Calif.) · 2026Article
- Identification of Stable Housekeeping Genes for miRNA Expression Studies in a Mouse Unilateral Ureteral Obstruction Model.Biochemical genetics · 2026Article
- Unique Features and Collateral Immune Effects of mRNA-LNP COVID-19 Vaccines: Plausible Mechanisms of Adverse Events and Complications.Pharmaceutics · 2025Review
- Micro-second time-resolved X-ray single-molecule internal motions of SARS-CoV-2 spike variants.Biochemistry and biophysics reports · 2024Article
- The Interactions between Cells and Viruses.International journal of molecular sciences · 2024Article
- Overcoming antibody-resistant SARS-CoV-2 variants with bispecific antibodies constructed using non-neutralizing antibodies.iScience · 2024Article
- FOXO3/Rab7-Mediated Lipophagy and Its Role in Zn-Induced Lipid Metabolism in Yellow Catfish (Genes · 2024Article
- Cardiac macrophages in maintaining heart homeostasis and regulating ventricular remodeling of heart diseases.Frontiers in immunology · 2024Review
- COVID-19 Biogenesis and Intracellular Transport.International journal of molecular sciences · 2023Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein binds to the cellular receptor-angiotensin-converting enzyme-2 (ACE2) as the first step in viral cell entry. SARS-CoV-2 spike protein expression in the ACE2-expressing cell surface induces cell-cell membrane fusion, thus forming syncytia. To exert its fusogenic activity, the spike protein is typically processed at a specific site (the S1/S2 site) by cellular proteases such as furin. The C488 residue, located at the spike-ACE2 interacting surface, is critical for the fusogenic and infectious roles of the SARS-CoV-2 spike protein. We have demonstrated that the C488 residue of the spike protein is involved in subcellular targeting and S1/S2 processing. C488 mutant spike localization to the Golgi apparatus and cell surface were impaired. Consequently, the S1/S2 processing of the spike protein, probed by anti-Ser-686-cleaved spike antibody, markedly decreased in C488 mutant spike proteins. Moreover, brefeldin-A-mediated endoplasmic-reticulum-to-Golgi traffic suppression also suppressed spike protein S1/S2 processing. As brefeldin A treatment and C488 mutation inhibited S1/S2 processing and syncytia formation, the C488 residue of spike protein is required for functional spike protein processing.
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