SARS-CoV-2 nsp16 binds to U1 snRNA

Stable Identifier
R-HSA-9730483
Type
Reaction [binding]
Species
Homo sapiens
Related Species
Severe acute respiratory syndrome coronavirus 2
Compartment
ReviewStatus
5/5
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Upon SARS-CoV-2 infection a strong global decrease in steady-state mRNA levels (relative to ncRNA levels) is observed. Many of the key genes stimulated by IFN are spliced, and an increase in intron retention in multiple IFN-responsive genes (such as ISG15 and RIG-I) is seen in infected human lung epithelial cells (Calu3). SARS-CoV-2 nonstructural protein 16 (nsp16), besides its role in viral RNA cap modification, binds to the 5′ splice site recognition sequence of U1 snRNA and the branchpoint recognition site of U2 snRNA, both parts of the spliceosome, disrupting global mRNA splicing (Banerjee et al, 2020).
Literature References
PubMed ID Title Journal Year
33080218 SARS-CoV-2 Disrupts Splicing, Translation, and Protein Trafficking to Suppress Host Defenses

Thai, J, Bruce, EA, Honson, DD, Ollikainen, N, Botten, JW, Miller, ZD, Voorhees, RM, Goldfarb, D, Guttman, M, Schmidt, MM, Chow, A, Blanco, MR, Quinodoz, SA, Majumdar, D, Bhat, P, Lin, AE, Stewart, DG, Banerjee, AK, Loney, C, Rihn, SJ, De Lorenzo, G, Chen, LM

Cell 2020
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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