nsp15 binds nsp8

Stable Identifier
Reaction [binding]
Homo sapiens
Related Species
Human SARS coronavirus
Locations in the PathwayBrowser
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Nonstructural protein 15 (nsp15) of the SARS coronavirus (SARS-CoV-1) binds to the replication-transcription complex (RTC) through interaction with nsp8 (Imbert et al. 2008). This interaction appears to be conserved in other coronaviruses, such as mouse hepatitis virus (MHV) (Athmer et al. 2017). nsp15 is an endonuclease characteristic for the order Nidovirales that includes the family Coronaviridae. nsp15 preferentially cleaves 3' of uridines, generating 2'-3' cyclic phosphates after cleavage. nsp15 requires Mn2+ ions for catalytic activity. Functional nsp15 is needed for production of viable virions and for viral transcription (Guarino et al. 2005, Ricagno et al. 2006, Bhardwaj et al. 2006, Joseph et al. 2007, Bhardwaj et al. 2008, Bhardwaj et al. 2012). The biological role of nsp15 has not been elucidated. It may degrade host mRNAs to shut down host translation, but so far no human or viral RNA targets have been identified.

Literature References
PubMed ID Title Journal Year
18255185 The SARS-Coronavirus PLnc domain of nsp3 as a replication/transcription scaffolding protein

Canard, B, Guillemot, JC, L├ęcine, P, Dimitrova, M, Imbert, I, Snijder, EJ

Virus Res. 2008
Orthologous Events
Name Identifier Synonyms
severe acute respiratory syndrome DOID:2945 SARS-CoV infection, SARS
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