A weak COPI binding motif in the cytoplasmic tail of SARS-CoV-2 spike glycoprotein is necessary for its cleavage, glycosylation, and localization.
COPI coatomer
COVID-19 SARS-CoV-2
ER retrieval signal
di-lysine motif
spike glycoprotein
Journal
FEBS letters
ISSN: 1873-3468
Titre abrégé: FEBS Lett
Pays: England
ID NLM: 0155157
Informations de publication
Date de publication:
07 2021
07 2021
Historique:
revised:
26
04
2021
received:
07
04
2021
accepted:
10
05
2021
pubmed:
16
5
2021
medline:
15
7
2021
entrez:
15
5
2021
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 33991349
doi: 10.1002/1873-3468.14109
pmc: PMC8209879
mid: NIHMS1704941
doi:
Substances chimiques
Spike Glycoprotein, Coronavirus
0
spike protein, SARS-CoV-2
0
Histidine
4QD397987E
Lysine
K3Z4F929H6
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
1758-1767Subventions
Organisme : NCI NIH HHS
ID : R01 CA008759
Pays : United States
Informations de copyright
© 2021 Federation of European Biochemical Societies.
Références
PLoS Pathog. 2021 Jan 25;17(1):e1009246
pubmed: 33493182
Science. 1994 Mar 18;263(5153):1629-31
pubmed: 8128252
Proc Natl Acad Sci U S A. 2018 Sep 4;115(36):8984-8989
pubmed: 30126980
J Virol. 2007 Mar;81(5):2418-28
pubmed: 17166901
Viruses. 2021 Jan 14;13(1):
pubmed: 33466921
J Gen Virol. 2016 Aug;97(8):1853-1864
pubmed: 27145752
Life Sci Alliance. 2020 Jul 23;3(9):
pubmed: 32703818
Traffic. 2006 Mar;7(3):337-53
pubmed: 16497227
J Virol. 2007 Apr;81(8):3877-90
pubmed: 17267500
J Biol Chem. 2002 May 24;277(21):18477-82
pubmed: 11886874
Curr Opin Virol. 2021 Apr;47:113-120
pubmed: 33744490
J Virol. 2004 Jun;78(11):5913-22
pubmed: 15140989
Mol Biol Cell. 2001 Jul;12(7):1925-35
pubmed: 11451993
Mol Cell. 2020 May 21;78(4):779-784.e5
pubmed: 32362314
Acta Pharmacol Sin. 2020 Sep;41(9):1141-1149
pubmed: 32747721
Mol Biol Cell. 2007 May;18(5):1887-96
pubmed: 17360967
Nat Commun. 2021 Sep 9;12(1):5333
pubmed: 34504087
Nat Nanotechnol. 2020 Aug;15(8):646-655
pubmed: 32669664
EMBO J. 2013 Apr 3;32(7):926-37
pubmed: 23481256
J Biol Chem. 2021 Jan-Jun;296:100111
pubmed: 33229438
J Biosci. 2017 Jun;42(2):231-244
pubmed: 28569247
J Cell Biol. 2017 Sep 4;216(9):2927-2943
pubmed: 28743825
J Biol Chem. 2001 Apr 20;276(16):13145-52
pubmed: 11139587
Nat Commun. 2020 Mar 27;11(1):1620
pubmed: 32221306
J Biol Chem. 1992 Aug 25;267(24):17110-5
pubmed: 1324923
Science. 2020 Jul 17;369(6501):330-333
pubmed: 32366695
Mol Biol Cell. 2004 Mar;15(3):1011-23
pubmed: 14699056
EMBO J. 1990 Oct;9(10):3153-62
pubmed: 2120038
J Cell Biol. 2003 Dec 22;163(6):1281-90
pubmed: 14691137