File:(A) CoV genome org & expr strategy (here SARS-CoV) - (B) pp1b pred dom org of 9 nidovir fams.jpg

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(A) Outline of CoV genome organization (Orthocoronavirinae) and expression strategy exemplified by SARS-CoV - (B) Comparison of predicted domain organization of pp1b of all families of order Nidovirales

Summary

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Description
English: (A) Outline of the CoV genome organization and expression strategy (Orthocoronavirinae, ICTV release 2018b). Depicted are the SARS-CoV genome and its 14 open reading frames (ORFs), i.e., the replicase ORFs 1a and 1b, the four common CoV structural protein genes (S, E, M, and N) and the ORFs encoding “accessory proteins.” The bottom half of the scheme summarizes the proteolytic processing and domain organization of the pp1a and pp1ab replicase polyproteins, the latter being produced by –1 ribosomal frameshifting. The nsp3 (PLpro, green) and nsp5 (3CLpro, red) proteases and their cognate cleavage sites are indicated in matching colors. The resulting 16 cleavage products (non-structural proteins, nsps) are indicated, as are the conserved replicase domains that are relevant for the original review this figure was created for. See there for references on nsp functions. Domain abbreviations and corresponding nsp numbers: PLpro, papain-like proteinase (nsp3); 3CLpro, 3C-like or main proteinase (nsp5); TM, transmembrane domain (nsp3, nsp4, and nsp6); NiRAN, nidovirus RdRp-associated nucleotidyl transferase (nsp12); RdRp, RNA-dependent RNA polymerase (nsp12); ZBD, zinc-binding domain (nsp13); HEL1, superfamily 1 helicase (nsp13); ExoN, 3′-to-5′exoribonuclease (nsp14); N7-MTase, N7-guanine methyl transferase (nsp14); endoU, uridylate-specific endoribonuclease (nsp15); 2′-O-MTase, 2′-O-methyl transferase (nsp16); UTR, untranslated region. (B) Comparison of the predicted domain organization in the replicase polyprotein 1b[1] of selected members of the nine families currently classified within the order Nidovirales (ICTV release 2018b). Adapted from Bukhari et al. (2018), with permission. Domains were predicted using HHPred-search (Soding, 2005; Zimmermann et al., 2018); for abbreviations see the legend to panel A. Genbank accession numbers of sequences used: SARS-coronavirus (AY274119.3); Human coronavirus 229E (AF304460.1); Bovine nidovirus 1 (KM589359.1); Sectovirus 1 (KX883637.1); White bream virus (DQ898157.1); Gill-associated virus (AF227196.1); Charybnivirus 1 (KX883628.1); Paguronivirus 1 (KX883627.1); Alphamesonivirus 1 (DQ458789.2); Turrinivirus 1 (KX883629.1); Equine arteritis virus (X53459.3); Aplysia abyssovirus (NC_040711.1); Planidovirus 1 (MH933735).
Deutsch: (A) Darstellung der CoV Genom-Organisation und -Expressionsstrategie (Orthocoronavirinae, ICTV-Ausgabe 2018b). Abgebildet sind das SARS-CoV-Genom und seine 14 „open reading frames“ (ORFs), d.h., die Replikase-ORFs 1a und 1b, die vier gewöhnlichen CoV-Strukturelles-Protein-Gene (S, E, M und N) und die ORFs, die für sog. „accessory proteins“ codieren. Die untere Hälfte des Diagramms gibt einen Überblick über die proteolytische Verarbeitung und Domänen-Organisation der pp1a- und pp1ab-Replikase-Polyproteine, das Letztere produziert durch –1-ribosomales Frameshifting. Die nsp3- (PLpro-, grün) und nsp5- (3CLpro-, rot) Proteasen und ihre zugehörigen Spaltstellen sind in gleicher Farbe gekennzeichnet. Die resultierenden 16 Spaltprodukte („non-structural proteins“, nsps) sind gekennzeichnet, gleichfalls die konservierten Replikase-Domänen, die relevant sind für die Original-Besprechung, für die diese Grafik erstellt ward. Siehe dort für Angaben zu nsp-Funktionen. Domänen-Abkürzungen und zugehörige nsp-Nummern: PLpro, papain-like proteinase (nsp3); 3CLpro, 3C-like oder main proteinase (nsp5); TM, transmembrane domain (nsp3, nsp4, and nsp6); NiRAN, nidovirus RdRp-associated nucleotidyl transferase (nsp12); RdRp, RNA-dependent RNA polymerase (nsp12); ZBD, zinc-binding domain (nsp13); HEL1, superfamily 1 helicase (nsp13); ExoN, 3′-to-5′exoribonuclease (nsp14); N7-MTase, N7-guanine methyl transferase (nsp14); endoU, uridylate-specific endoribonuclease (nsp15); 2′-O-MTase, 2′-O-methyl transferase (nsp16); UTR, untranslated region. (B) Vergleich der vorhergesagten Domänen-Organisation im Replikase-Polyprotein 1b[1] von ausgewählten Mitgliedern der neun Familien, die aktuell innerhalb der Ordnung Nidovirales (ICTV release 2018b) klassifiziert sind. Angepasst von Bukhari et al. (2018), mit Erlaubnis. Domänen warden vorhergesagt unter Nutzung von HHPred-search (Soding, 2005; Zimmermann et al., 2018); für Abkürzungen siehe die Legende zu Panel A. Genbank-Zugriffsschlüssel für genutzte Sequenzen: SARS-coronavirus (AY274119.3); Human coronavirus 229E (AF304460.1); Bovine nidovirus 1 (KM589359.1); Sectovirus 1 (KX883637.1); White bream virus (DQ898157.1); Gill-associated virus (AF227196.1); Charybnivirus 1 (KX883628.1); Paguronivirus 1 (KX883627.1); Alphamesonivirus 1 (DQ458789.2); Turrinivirus 1 (KX883629.1); Equine arteritis virus (X53459.3); Aplysia abyssovirus (NC_040711.1); Planidovirus 1 (MH933735).
Date
Source In: Ogando NS, Ferron F, Decroly E, Canard B, Posthuma CC and Snijder EJ (2019-08-07). “The Curious Case of the Nidovirus Exoribonuclease: Its Role in RNA Synthesis and Replication Fidelity” (PDF). Frontiers in Microbiology 10 (1813): Figure 1. DOI:10.3389/fmicb.2019.01813. PMID 31440227. PMC: 6693484. Retrieved on 2020-06-01.
A: Based on work in: E.J. Snijder, E. Decroly and J. Ziebuhr (2016-09-14). “The Nonstructural Proteins Directing Coronavirus RNA Synthesis and Processing” (PDF). Advances in Virus Research 96 (1st ed.): Figure 2. Burlington: Elsevier Inc./Academic Press. DOI:10.1016/bs.aivir.2016.08.008. PMID 27712628. PMC: 7112286. ISBN 978-0-12-804736-1. ISSN 0065-3527. Retrieved on 2020-06-14.
B: Based on work in: Khulud Bukhari, Geraldine Mulley, Anastasia A. Gulyaeva, Lanying Zhao, Guocheng Shu, Jianping Jiang, Benjamin W. Neuman (2018-09-07). “Description and initial characterization of metatranscriptomic nidovirus-like genomes from the proposed new family Abyssoviridae, and from a sister group to the Coronavirinae, the proposed genus Alphaletovirus” (PDF). Virology 524 (November 2018): Figure 5A. Elsevier. DOI:10.1016/j.virol.2018.08.010. PMID 30199753. PMC: 7112036. Retrieved on 2020-05-18. („Coronavirinae“: now „Orthocoronavirinae“)
Author Current version by: Ogando NS, Ferron F, Decroly E, Canard B, Posthuma CC and Snijder EJ. © 2019 Ogando, Ferron, Decroly, Canard, Posthuma, Snijder. (Adapted with permission by license or former copyright holders.)
A: Base version by: E.J. Snijder, E. Decroly, J. Ziebuhr.
B: Base version by: Khulud Bukhari, Geraldine Mulley, Anastasia A. Gulyaeva, Lanying Zhao, Guocheng Shu, Jianping Jiang, Benjamin W. Neuman (corresponding author).
  1. ↑ a b Khulud Bukhari, Geraldine Mulley, Anastasia A. Gulyaeva, Lanying Zhao, Guocheng Shu, Jianping Jiang, Benjamin W. Neuman (2018-09-07). “Description and initial characterization of metatranscriptomic nidovirus-like genomes from the proposed new family Abyssoviridae, and from a sister group to the Coronavirinae, the proposed genus Alphaletovirus” (PDF). Virology 524 (November 2018): Figure 5A. Elsevier. DOI:10.1016/j.virol.2018.08.010. PMID 30199753. PMC: 7112036. Retrieved on 2020-05-18. („Coronavirinae“: now „Orthocoronavirinae“)

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current05:33, 2 June 2020Thumbnail for version as of 05:33, 2 June 20201,928 × 1,943 (322 KB)Markus Prokott (talk | contribs)Uploaded a work by Ogando NS, Ferron F, Decroly E, Canard B, Posthuma CC and Snijder EJ. © 2019 Ogando, Ferron, Decroly, Canard, Posthuma and Snijder. from Ogando NS, Ferron F, Decroly E, Canard B, Posthuma CC and Snijder EJ (2019) The Curious Case of the Nidovirus Exoribonuclease: Its Role in RNA Synthesis and Replication Fidelity. Front. Microbiol. 10:1813. doi: 10.3389/fmicb.2019.01813. URL: https://www.frontiersin.org/files/Articles/475185/fmicb-10-01813-HTML/image_m/fmicb-10-01813-g001.j...

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