A weak COPI binding motif in the cytoplasmic tail of SARS-CoV-2 spike glycoprotein is necessary for its cleavage, glycosylation, and localization.
FEBS Lett
; 595(13): 1758-1767, 2021 07.
Article
in English
| MEDLINE | ID: covidwho-1227709
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 COPß' 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.
Keywords
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Amino Acid Substitution
/
Spike Glycoprotein, Coronavirus
/
SARS-CoV-2
Limits:
Humans
Language:
English
Journal:
FEBS Lett
Year:
2021
Document Type:
Article
Affiliation country:
1873-3468.14109
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