Spike protein gets N-glycosylated

Stable Identifier
R-HSA-9694793
Type
Reaction [uncertain]
Species
Homo sapiens
Related Species
Severe acute respiratory syndrome coronavirus 2
Compartment
ReviewStatus
5/5
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General
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Glycosyltransferases in the endoplasmatic reticulum are responsible for the attachment of numerous high-mannose N-glycans on the SARS-CoV-2 spike protein. After virion assembly and release these glycosidations are required for fusion with host cells (Watanabe et al, 2020, Breuer et al, 2001).

O-glycosylations do occur on the Spike protein with an average overall frequency per site of less than 50 percent (Sanda et al, 2020).
Literature References
PubMed ID Title Journal Year
32518941 Identification of 22 N-glycosites on spike glycoprotein of SARS-CoV-2 and accessible surface glycopeptide motifs: implications for vaccination and antibody therapeutics

Tian, X, Zhang, W, Zhou, D, Qi, R, Peng, C

Glycobiology 2020
32366695 Site-specific glycan analysis of the SARS-CoV-2 spike

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

Science 2020
32363391 Deducing the N- and O-glycosylation profile of the spike protein of novel coronavirus SARS-CoV-2

Shajahan, A, Azadi, P, Supekar, NT, Gleinich, AS

Glycobiology 2020
32676595 N and O glycosylation of the SARS-CoV-2 spike protein

Goldman, R, Morrison, L, Sanda, M

bioRxiv 2020
Participants
Participates
Catalyst Activity

dolichyl-diphosphooligosaccharide-protein glycotransferase activity of OST complex [endoplasmic reticulum membrane]

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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