Recruitment of Spike trimer to assembling virion

Stable Identifier
R-HSA-9694553
Type
Reaction [binding]
Species
Homo sapiens
Related Species
Severe acute respiratory syndrome coronavirus 2
Compartment
endoplasmic reticulum-Golgi intermediate compartment membrane
ReviewStatus
5/5
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Recruitment of Spike trimer to assembling virion
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This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Based on studies in other coronaviruses, SARS-COV-2 S trimers are presumed to be recruited to the assembling virion through interaction with M protein (reviewed in Ujike and Taguchi, 2015). Multiple regions of M contribute to the recruitment of S, with a single tyrosine residue in the C-terminal domain of M playing a critical role (McBride et al, 2010a; Hsieh et al, 2008). Interaction with M is aided by a dibasic motif in the C-terminus of S, which promotes retrieval of the spike protein from the cell surface by binding the COPI coat (McBride et al, 2007; Ujike et al, 2016). Palmitoylation of the C-terminus of S appears dispensible for the interaction with M in SARS-COV-1, unlike the case in other coronaviruses; whether this is also true for SARS-COV-2 remains to be determined (Ujike et al, 2012; McBride 2010b; reviewed in Ujike and Taguchi, 2015). Size estimates and modelling suggest the mature virion has approximately 300 S trimers (Neuman et al, 2006; reviewed in Chang et al, 2014).
Literature References
PubMed ID Title Journal Year
17166901 The cytoplasmic tail of the severe acute respiratory syndrome coronavirus spike protein contains a novel endoplasmic reticulum retrieval signal that binds COPI and promotes interaction with membrane protein

Li, J, Machamer, CE, McBride, CE

J. Virol. 2007
20007283 A single tyrosine in the severe acute respiratory syndrome coronavirus membrane protein cytoplasmic tail is important for efficient interaction with spike protein

Machamer, CE, McBride, CE

J. Virol. 2010
22238235 Two palmitylated cysteine residues of the severe acute respiratory syndrome coronavirus spike (S) protein are critical for S incorporation into virus-like particles, but not for M-S co-localization

Ujike, M, Huang, C, Makino, S, Matsuyama, S, Shirato, K, Taguchi, F

J. Gen. Virol. 2012
25855243 Incorporation of spike and membrane glycoproteins into coronavirus virions

Ujike, M, Taguchi, F

Viruses 2015
27145752 The contribution of the cytoplasmic retrieval signal of severe acute respiratory syndrome coronavirus to intracellular accumulation of S proteins and incorporation of S protein into virus-like particles

Ujike, M, Huang, C, Makino, S, Shirato, K, Taguchi, F

J. Gen. Virol. 2016
18792806 Interactions between M protein and other structural proteins of severe, acute respiratory syndrome-associated coronavirus

Chen, SC, Li, HC, Lo, SY, Hsieh, YC

J. Biomed. Sci. 2008
16873249 Supramolecular architecture of severe acute respiratory syndrome coronavirus revealed by electron cryomicroscopy

Neuman, BW, Buchmeier, MJ, Milligan, RA, Yeager, M, Adair, BD, Orca, G, Kuhn, P, Yoshioka, C, Quispe, JD

J. Virol. 2006
24418573 The SARS coronavirus nucleocapsid protein--forms and functions

Chang, CK, Hsiao, CD, Hou, MH, Chang, CF, Huang, TH

Antiviral Res. 2014
20580052 Palmitoylation of SARS-CoV S protein is necessary for partitioning into detergent-resistant membranes and cell-cell fusion but not interaction with M protein

Machamer, CE, McBride, CE

Virology 2010
Participants
Input
Output
Participates
as an event of
Inferred From
Recruitment of Spike trimer to assembling virion (Homo sapiens)
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
Rothfels, K  (2020-07-30)
Reviewed
Acencio, ML  (2020-09-09)
Created
Cook, J  (2020-07-07)
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