Evidence map›Paper›PMID 33991349›Full record

ArticleFEBS letters2021

A weak COPI binding motif in the cytoplasmic tail of SARS-CoV-2 spike glycoprotein is necessary for its cleavage, glycosylation, and localization.

Benjamin C Jennings, Stuart Kornfeld, Balraj Doray

Open access · bronzeAbstract read
In one paragraph

Article in FEBS letters, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.6field-weighted citation impact, top 14% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

20 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
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  13. COVID-19 Biogenesis and Intracellular Transport.International journal of molecular sciences · 2023
    Review
  14. Article
  15. Retro-2 alters Golgi structure.Scientific reports · 2022
    Article
  16. Article
  17. Review
  18. Review
  19. Review
  20. The glycosylation in SARS-CoV-2 and its receptor ACE2.Signal transduction and targeted therapy · 2021
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Benjamin C JenningsDepartment of Internal Medicine, Washington University School of Medicine, St. Louis, Missouri, USA.ORCID 0000-0002-7255-2715
Stuart KornfeldDepartment of Internal Medicine, Washington University School of Medicine, St. Louis, Missouri, USA.ORCID 0000-0002-6417-4478
Balraj DorayDepartment of Internal Medicine, Washington University School of Medicine, St. Louis, Missouri, USA.ORCID 0000-0003-3347-5013
Washington University in St. Louis · US

Funding

Structure, Biosynthesis & Function of GlycoproteinsR01CA008759 · NCI · WASHINGTON UNIVERSITY · PI KORNFELD, STUART A · 1985 to 2023
$3.5M
NCI NIH HHS R01 CA008759
6 · The paper itself

Abstract

The SARS-CoV-2 spike glycoprotein (spike) mediates viral entry by binding ACE2 receptors on host cell surfaces. Spike glycan processing and cleavage, which occur in the Golgi network, are important for fusion at the plasma membrane, promoting both virion infectivity and cell-to-cell viral spreading. We show that a KxHxx motif in the cytosolic tail of spike weakly binds the COPβ' subunit of COPI coatomer, which facilitates some recycling of spike within the Golgi, while releasing the remainder to the cell surface. Although histidine (KxHxx) has been proposed to be equivalent to lysine within di-lysine endoplasmic reticulum (ER) retrieval sequences, we show that histidine-to-lysine substitution (KxKxx) retains spike at the ER and prevents glycan processing, protease cleavage, and transport to the plasma membrane.

Indexed as

Amino Acid SubstitutionAmino Acid MotifsBinding SitesGlycosylationGolgi ApparatusHEK293 CellsHeLa CellsHistidineHumansLysineProtein DomainsProteolysisSARS-CoV-2Spike Glycoprotein, CoronavirusVirus InternalizationHistidineLysineSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2COPI coatomerCOVID-19 SARS-CoV-2di-lysine motifER retrieval signalspike glycoprotein

Identifiers

PMID33991349
PMCPMC8209879
OpenAlexW3161089648

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.