ArticleNature communications2021
Sequences in the cytoplasmic tail of SARS-CoV-2 Spike facilitate expression at the cell surface and syncytia formation.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
88 citing papers in PubMed, 124 citations in OpenAlex.
- GPNMB promotes double-membrane vesicle accumulation and facilitates structural protein transport during PEDV infection.Virulence · 2026Article
- Direct lipid interactions control SARS-CoV-2 M protein conformational dynamics and virus assembly.Nature communications · 2026Article
- Disruption of spike protein N-glycosylation induces its endoplasmic reticulum retention and attenuates SARS-CoV-2 infectivity.Journal of virology · 2026Article
- Antigen-specific IgG glycosylation profiles in hamsters and macaques following COVID-19 vaccination.iScience · 2026Article
- VPS26A retromer complex and SNX27 mediate stress-induced Golgi bypass of membrane proteins.Nature communications · 2026Article
- Targeting the host factor HGS-viral membrane protein interaction in coronavirus infection.The Journal of clinical investigation · 2026Article
- Molecular mechanism of cholesterol-dependent membrane fusion in SARS-CoV-2 entry.Signal transduction and targeted therapy · 2026Article
- Identification of immunodominant T cell epitopes in SARS-CoV-2 spike protein in Syrian hamsters.Journal of immunology (Baltimore, Md. : 1950) · 2026Article
- SARS-CoV-2 S assembly into virions facilitated by host ERM proteins.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Article
- A murine coronavirus infection platform identifies proviral and proinflammatory activities of SARS-CoV-2 accessory protein 7a.Journal of virology · 2026Article
- A cluster of acidic residues in the cytoplasmic domain of SARS-CoV-2 Spike is required for virion-incorporation and infectivity.PloS one · 2026Article
- Droplet-based single-cell pairing for high-throughput interaction mapping of antigen-receptor combinations.Science advances · 2025Article
- Mechanisms of Cell-Cell Fusion in SARS-CoV-2: An Evolving Strategy for Transmission and Immune Evasion.Viruses · 2025Review
- An unconventional HxD motif orchestrates coatomer-dependent coronavirus morphogenesis.bioRxiv : the preprint server for biology · 2025Article
- Unique Features and Collateral Immune Effects of mRNA-LNP COVID-19 Vaccines: Plausible Mechanisms of Adverse Events and Complications.Pharmaceutics · 2025Review
- Article
- COP I vesicles facilitate classical swine fever virus proliferation by transporting fatty acid synthase from the Golgi apparatus to the endoplasmic reticulum.Journal of virology · 2025Article
- Production and cryo-electron microscopy structure of an internally tagged SARS-CoV-2 spike ecto-domain construct.Journal of structural biology: X · 2025Article
- Nonlytic Egress and Transmission in the Virus World.Annual review of biochemistry · 2025Review
28 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
6 authors at 1 institution in 1 country.
Funding
Abstract
The Spike (S) protein of SARS-CoV-2 binds ACE2 to direct fusion with host cells. S comprises a large external domain, a transmembrane domain, and a short cytoplasmic tail. Understanding the intracellular trafficking of S is relevant to SARS-CoV-2 infection, and to vaccines expressing full-length S from mRNA or adenovirus vectors. Here we report a proteomic screen for cellular factors that interact with the cytoplasmic tail of S. We confirm interactions with the COPI and COPII vesicle coats, ERM family actin regulators, and the WIPI3 autophagy component. The COPII binding site promotes exit from the endoplasmic reticulum, and although binding to COPI should retain S in the early Golgi where viral budding occurs, there is a suboptimal histidine residue in the recognition motif. As a result, S leaks to the surface where it accumulates and can direct the formation of multinucleate syncytia. Thus, the trafficking signals in the tail of S indicate that syncytia play a role in the SARS-CoV-2 lifecycle.
Indexed as
Identifiers
What OpenQuestion holds
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.