SARS-CoV-1 nsp1 binds to PPIase

Stable Identifier
R-HSA-9728804
Type
Reaction [binding]
Species
Homo sapiens
Related Species
Human SARS coronavirus
Compartment
cytosol
ReviewStatus
5/5
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SARS-CoV-1 nsp1 binds to PPIase
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Peptidyl-prolyl isomerases (PPIase) function as protein folding chaperones. All five PPIases PPIA, PPIB, PPIG, PPIH, and FKBP1A have been shown to bind to SARS-CoV-1 nonstructural protein 1 (nsp1), significantly activating the Cyclophilin A/NFAT pathway, ultimately enhancing the induction of the IL-2 promoter. The increase of NFAT activation extends to all three major NFAT species, suggesting a potential for induction of broad and systemic cytokine dysregulation by affecting several types of immune cells (Pfefferle et al, 2011; Law et al, 2007).
Literature References
PubMed ID Title Journal Year
17035307 Role for nonstructural protein 1 of severe acute respiratory syndrome coronavirus in chemokine dysregulation

Law, AH, Yim, HC, Cheung, BK, Lee, DC, Lau, AS

J Virol 2007
22046132 The SARS-coronavirus-host interactome: identification of cyclophilins as target for pan-coronavirus inhibitors

Niemeyer, D, Herrler, G, Zimmer, R, Pumpor, K, Friedel, CC, Haas, J, Müller, MA, Weber, F, Kuri, T, Hilgenfeld, R, Ditt, V, Drosten, C, von Dall'Armi, E, von Brunn, A, Thiel, V, Herzog, P, Steffen, I, Kögl, M, Schwegmann-Wessels, C, Züst, R, Thiel, HJ, Schwarz, F, Pöhlmann, S, Kallies, S, Pfefferle, S, Schöpf, J, Carbajo-Lozoya, J, Stellberger, T

PLoS Pathog 2011
Participants
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Output
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as an event of
Disease
Name Identifier Synonyms
severe acute respiratory syndrome DOID:2945 SARS-CoV infection, SARS
Authored
Stephan, R  (2021-04-21)
Reviewed
D'Eustachio, P  (2021-01-26)
Created
Stephan, R  (2021-04-22)
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