Home  |  Contact
PROSITE documentation PDOC51960

Coronavirus (CoV) Nsp15 N-terminal oligomerization domain profile





Description

Coronaviruses (CoVs) are enveloped positive-strand RNA viruses that infect many species, including humans, other mammals, and birds. After infection, the host may develop respiratory, bowel, liver, and neurological diseases. Coronaviruses are divided into four genera: αcoronavirus, βcoronavirus, γcoronavirus, and Deltacoronavirus. The ideal hosts of αCoV and βCoV are mammals, and γCoV primarily infects birds, while DeltaCoV has been identified in both mammals and birds. SARS, SARS-CoV-2, BatCoV RaTG13 and Bat-SARS-like coronavirus (BATSL-CoVZXC21 and BAT-SL-CoVZC45) belong to the Sarbecovirus subgenus of βCoV [E1].

The CoV replicase gene encodes two overlapping polyproteins, termed pp1a and pp1ab, which mediate viral replication and transcription. The polypeptides pp1a and pp1ab are processed by the action of a main protease (Nsp5) (see <PDOC51442>) and of one or two papain-like proteases (PLpro) (see <PDOC51124>) found in Nsp3 into non-structural proteins (Nsps) to form the replication/ transcription complex (RTC). Among them, Nsp15 is a nidoviral uridylate-specific endoribonuclease (NendoU) that plays an essential role in the life cycle of the virus. CoV Nsp15 consists of three distinct domains, a small N-terminal, an intermediate-sized middle, and a large C-terminal NendoU domain (see <PDOC51958>). CoV Nsp15 forms double-ring hexamers made of dimers of trimers. The hexameric form is thought to be the fully active form of CoV Nsp15 and the hexamer is stabilized by interactions of the N-terminal oligomerization domain [1,2,3,4,5,6,7].

The CoV Nsp15 NTD oligomerization domain is composed of an antiparallel β-sheet (strands β1, β2, and β3) wrapped around two α-helices (α1 and α2) (see <PDB:6VWW>) [5,6,7].

The profile we developed covers the entire CoV Nsp15 N-terminal oligomerization domain.

Last update:

February 2021 / First entry.

-------------------------------------------------------------------------------

Technical section

PROSITE method (with tools and information) covered by this documentation:

COV_NSP15_NTD, PS51960; Coronavirus (CoV) Nsp15 N-terminal oligomerization domain profile  (MATRIX)


References

1AuthorsSnijder E.J. Decroly E. Ziebuhr J.
TitleThe Nonstructural Proteins Directing Coronavirus RNA Synthesis and Processing.
SourceAdv. Virus. Res. 96:59-126(2016).
PubMed ID27712628
DOI10.1016/bs.aivir.2016.08.008

2AuthorsGorgulla C. Das K.M.P. Leigh K.E. Cespugli M. Fischer P.D. Wang Z.-F. Tesseyre G. Pandita S. Shnapir A. Calderaio A. Hutcheson C. Gechev M. Rose A. Lewis N. Yaffe E. Luxenburg R. Herce H.D. Durmaz V. Halazonetis T.D. Fackeldey K. Patten J.J. Chuprina A. Dziuba I. Plekhova A. Moroz Y. Radchenko D. Tarkhanova O. Yavnyuk I. Gruber C.C. Yust R. Payne D. Naeaer A.M. Namchuk M.N. Davey R.A. Wagner G. Kinney J. Arthanari H.
TitleA Multi-Pronged Approach Targeting SARS-CoV-2 Proteins Using Ultra-Large Virtual Screening.
SourceChemRxiv 0:0-0(2020).
PubMed ID33200116
DOI10.26434/chemrxiv.12682316

3AuthorsXu X. Zhai Y. Sun F. Lou Z. Su D. Xu Y. Zhang R. Joachimiak A. Zhang X.C. Bartlam M. Rao Z.
TitleNew antiviral target revealed by the hexameric structure of mouse hepatitis virus nonstructural protein nsp15.
SourceJ. Virol. 80:7909-7917(2006).
PubMed ID16873248
DOI10.1128/JVI.00525-06

4AuthorsZheng A. Shi Y. Shen Z. Wang G. Shi J. Xiong Q. Fang L. Xiao S. Fu Z.F. Peng G.
TitleInsight into the evolution of nidovirus endoribonuclease based on the finding that nsp15 from porcine Deltacoronavirus functions as a dimer.
SourceJ. Biol. Chem. 293:12054-12067(2018).
PubMed ID29887523
DOI10.1074/jbc.RA118.003756

5AuthorsJoseph J.S. Saikatendu K.S. Subramanian V. Neuman B.W. Buchmeier M.J. Stevens R.C. Kuhn P.
TitleCrystal structure of a monomeric form of severe acute respiratory syndrome coronavirus endonuclease nsp15 suggests a role for hexamerization as an allosteric switch.
SourceJ. Virol. 81:6700-6708(2007).
PubMed ID17409150
DOI10.1128/JVI.02817-06

6AuthorsZhang L. Li L. Yan L. Ming Z. Jia Z. Lou Z. Rao Z.
TitleStructural and Biochemical Characterization of Endoribonuclease Nsp15 Encoded by Middle East Respiratory Syndrome Coronavirus.
SourceJ. Virol. 92:0-0(2018).
PubMed ID30135128
DOI10.1128/JVI.00893-18

7AuthorsKim Y. Jedrzejczak R. Maltseva N.I. Wilamowski M. Endres M. Godzik A. Michalska K. Joachimiak A.
TitleCrystal structure of Nsp15 endoribonuclease NendoU from SARS-CoV-2.
SourceProtein. Sci. 29:1596-1605(2020).
PubMed ID32304108
DOI10.1002/pro.3873

E1Titlehttps://viralzone.expasy.org/30?outline=all_by_species



PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)