Spike trimer moves into the ERGIC membrane

Stable Identifier
R-HSA-9698333
Type
Reaction [uncertain]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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The fully glycosylated Sprike trimer moves into the ERGIC membrane. In infected cells Spike is coexpressed with the viral envelope (E) and the small membrane protein (M). M mediates S retention in the ERGIC through a retrieval motif in S, whereas E induces S retention by modulating the cell secretory pathway (Boson et al, 2020). Despite both mechanisms some Spike may still leak to the cell surface, causing syncytia formation (Cattin-Ortolà et al, 2021).
Literature References
PubMed ID Title Journal Year
33229438 The SARS-CoV-2 envelope and membrane proteins modulate maturation and retention of the spike protein, allowing assembly of virus-like particles

Denolly, S, Lavillette, D, Siret, E, Boson, B, Zhou, B, Mathieu, C, Cosset, FL, Legros, V

J Biol Chem 2021
32366695 Site-specific glycan analysis of the SARS-CoV-2 spike

Watanabe, Y, Crispin, M, Allen, JD, McLellan, JS, Wrapp, D

Science 2020
34504087 Sequences in the cytoplasmic tail of SARS-CoV-2 Spike facilitate expression at the cell surface and syncytia formation

James, LC, Papa, G, Cattin-Ortolá, J, Maslen, SL, Munro, S, Welch, LG

Nat Commun 2021
Participants
Participates
Disease
Name Identifier Synonyms
COVID-19 DOID:0080600 2019 Novel Coronavirus (2019-nCoV), Wuhan seafood market pneumonia virus infection, 2019-nCoV infection, Wuhan coronavirus infection
Authored
Reviewed
Created
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