Structural basis for polyuridine tract recognition by SARS-CoV-2 Nsp15

Fumiaki Ito, Hanjing Yang, Z. Hong Zhou, Xiaojiang S. Chen

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Protein Cell ›› 2024, Vol. 15 ›› Issue (7) : 547-552. DOI: 10.1093/procel/pwae009
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Structural basis for polyuridine tract recognition by SARS-CoV-2 Nsp15

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Fumiaki Ito, Hanjing Yang, Z. Hong Zhou, Xiaojiang S. Chen. Structural basis for polyuridine tract recognition by SARS-CoV-2 Nsp15. Protein Cell, 2024, 15(7): 547‒552 https://doi.org/10.1093/procel/pwae009

References

[1]
Athmer J, Fehr AR, Grunewald M et al. In situ tagged Nsp15 reveals interactions with coronavirus replication/transcription complex-associated proteins. Mbio 2017;8:e02320–e02316.
CrossRef Google scholar
[2]
Bhardwaj K, Guarino L, Kao CC. The severe acute respiratory syndrome coronavirus Nsp15 protein is an endoribonuclease that prefers manganese as a cofactor. J Virol 2004;78:12218–12224.
CrossRef Google scholar
[3]
Deng X, Baker SC. An “Old”protein with a new story: coronavirus endoribonuclease is important for evading host antiviral defenses. Virology 2018;517:157–163.
CrossRef Google scholar
[4]
Deng X, Hackbart M, Mettelman RC et al. Coronavirus nonstructural protein 15 mediates evasion of dsRNA sensors and limits apoptosis in macrophages. Proc Natl Acad Sci U S A 2017;114:e4251–e4260.
CrossRef Google scholar
[5]
Deng X, Van Geelen A, Buckley AC et al. Coronavirus endoribonuclease activity in porcine epidemic diarrhea virus suppresses Type I And Type III interferon responses. J Virol 2019;93.
CrossRef Google scholar
[6]
Frazier MN, Dillard LB, Krahn JM et al. Characterization Of SARS2 Nsp15 nuclease activity reveals it’s mad about U. Nucleic Acids Res 2021;49:10136–10149.
CrossRef Google scholar
[7]
Frazier MN, Wilson IM, Krahn JM et al. Flipped over U: structural basis for dsRNA cleavage by the SARS-Cov-2 endoribonuclease. Nucleic Acids Res 2022;50:8290–8301.
CrossRef Google scholar
[8]
Hackbart M, Deng X, Baker SC. Coronavirus endoribonuclease targets viral polyuridine sequences to evade activating host sensors. Proc Natl Acad Sci U S A 2020;117:8094–8103.
CrossRef Google scholar
[9]
Hofmann MA, Brian DA. The 5’ end of coronavirus minusstrand RNAs contains a short poly(U) tract. J Virol 1991;65:6331–6333.
CrossRef Google scholar
[10]
Ivanov KA, Hertzig T, Rozanov M et al. Major genetic marker of nidoviruses encodes a replicative endoribonuclease. Proc Natl Acad Sci U S A 2004;101:12694–12699.
CrossRef Google scholar
[11]
Kang DC, Gopalkrishnan RV, Wu Q et al. mda-5: an interferon-inducible putative RNA helicase with double-stranded RNA-dependent ATPase activity and melanoma growth-suppressive properties. Proc Natl Acad Sci U S A 2002;99:637–642.
CrossRef Google scholar
[12]
Kato H, Takeuchi O, Sato S et al. Differential roles of MDa5 and RIG-I helicases in the recognition of RNA viruses. Nature 2006;441:101–105.
CrossRef Google scholar
[13]
Kim Y, Jedrzejczak R, Maltseva NI et al. Crystal structure Of Nsp15 Endoribonuclease NendoU from SARS-CoV-2. Protein Sci 2020;29:1596–1605.
CrossRef Google scholar
[14]
Kim Y, Wower J, Maltseva N et al. Tipiracil binds to uridine site and inhibits Nsp15 Endoribonuclease NendoU from SARS-Cov-2. Commun Biol 2021;4:193.
CrossRef Google scholar
[15]
Zhang L, Li L, Yan L et al. Structural And biochemical characterization of endoribonuclease Nsp15 Encoded By Middle East respiratory syndrome coronavirus. J Virol 2018;92.
CrossRef Google scholar

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2024 The Author(s) 2024. Published by Oxford University Press on behalf of Higher Education Press.
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