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

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

doi:10.1093/procel/pwae009

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

Fumiaki Ito ¹^,²^,³
, Hanjing Yang ¹
, Z. Hong Zhou ²^,³
, Xiaojiang S. Chen ¹^,⁴^,⁵^,⁶^,^†

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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 DOI:10.1093/procel/pwae009

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References

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[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.

[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.

[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.

[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.

[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.

[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.

[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.

[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.

[9]	Hofmann MA, Brian DA. The 5’ end of coronavirus minusstrand RNAs contains a short poly(U) tract. J Virol 1991;65:6331–6333.

[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.

[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.

[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.

[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.

[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.

[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.