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SARS-related coronavirus

December 04, 2023

This article is about a species of coronavirus comprising multiple strains. For the strain that causes SARS, see SARS-CoV-1. For the strain that causes COVID-19, see SARS-CoV-2.

Severe acute respiratory syndrome–related coronavirus (SARSr-CoV or SARS-CoV)[note 1] is a species of virus consisting of many known strains phylogenetically related to severe acute respiratory syndrome coronavirus 1 (SARS-CoV-1) that have been shown to possess the capability to infect humans, bats, and certain other mammals.[2][3] These enveloped, positive-sense single-stranded RNA viruses enter host cells by binding to the angiotensin-converting enzyme 2 (ACE2) receptor.[4] The SARSr-CoV species is a member of the genus Betacoronavirus and of the subgenus Sarbecovirus (SARS Betacoronavirus).[5][6]

Sarbecovirus
Transmission electron micrograph of SARS-related coronaviruses emerging from host cells cultured in the lab
Virus classification
(unranked): Virus
Realm: Riboviria
Kingdom: Orthornavirae
Phylum: Pisuviricota
Class: Pisoniviricetes
Order: Nidovirales
Family: Coronaviridae
Genus: Betacoronavirus
Subgenus: Sarbecovirus
Strains
Synonyms
  • SARS coronavirus
  • SARS-related coronavirus
  • Severe acute respiratory syndrome coronavirus[1]

Two strains of the virus have caused outbreaks of severe respiratory diseases in humans: severe acute respiratory syndrome coronavirus 1 (SARS-CoV or SARS-CoV-1), which caused the 2002–2004 outbreak of severe acute respiratory syndrome (SARS), and severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), which is causing the ongoing pandemic of COVID-19.[7][8] There are hundreds of other strains of SARSr-CoV, which are only known to infect non-human species: bats are a major reservoir of many strains of SARSr-CoV; several strains have been identified in Himalayan palm civets, which were likely ancestors of SARS-CoV-1.[7][9]

The SARS-related coronavirus was one of several viruses identified by the World Health Organization (WHO) in 2016 as a likely cause of a future epidemic in a new plan developed after the Ebola epidemic for urgent research and development before and during an epidemic towards diagnostic tests, vaccines and medicines. This prediction came to pass with the COVID-19 pandemic.[10][11]

Classification edit

SARS-related coronavirus is a member of the genus Betacoronavirus (group 2) and monotypic of the subgenus Sarbecovirus (subgroup B).[12] Sarbecoviruses, unlike embecoviruses or alphacoronaviruses, have only one papain-like proteinase (PLpro) instead of two in the open reading frame ORF1ab.[13] SARSr-CoV was determined to be an early split-off from the betacoronaviruses based on a set of conserved domains that it shares with the group.[14][15]

Bats serve as the main host reservoir species for the SARS-related coronaviruses like SARS-CoV-1 and SARS-CoV-2. The virus has coevolved in the bat host reservoir over a long period of time.[16] Only recently have strains of SARS-related coronavirus been observed to have evolved into having been able to make the cross-species jump from bats to humans, as in the case of the strains SARS-CoV-1 and SARS-CoV-2.[17][4] Both of these strains descended from a single ancestor but made the cross-species jump into humans separately. SARS-CoV-2 is not a direct descendant of SARS-CoV-1.[7]

Genome edit

 
Genome organization and viral proteins of SARS-CoV

The SARS-related coronavirus is an enveloped, positive-sense, single-stranded RNA virus. Its genome is about 30 kb, which is one of the largest among RNA viruses. The virus has 14 open reading frames which overlap in some cases.[18] The genome has the usual 5′ methylated cap and a 3′ polyadenylated tail.[19] There are 265 nucleotides in the 5'UTR and 342 nucleotides in the 3'UTR.[18]

The 5' methylated cap and 3' polyadenylated tail allows the positive-sense RNA genome to be directly translated by the host cell's ribosome on viral entry.[20] SARSr-CoV is similar to other coronaviruses in that its genome expression starts with translation by the host cell's ribosomes of its initial two large overlapping open reading frames (ORFs), 1a and 1b, both of which produce polyproteins.[18]

Function of SARSr-CoV
genome proteins
Protein Function[21][22][23][24]
ORF1ab
P0C6X7 		Replicase/transcriptase polyprotein (pp1ab)
(nonstructural proteins)
ORF2
P59594 		Spike (S) protein, virus binding and entry
(structural protein)
ORF3a
P59632		 Interacts with S, E, M structural proteins;
Ion channel activity;
Upregulates cytokines and chemokines such as IL-8 and RANTES;
Upregulates NF-κB and JNK;
Induces apoptosis and cell cycle arrest, via Caspase 8 and -9,
and by Bax, p53, and p38 MAP kinase
ORF3b
P59633		 Upregulates cytokines and chemokines by RUNX1b;
Inhibits Type I IFN production and signaling;
Induces apoptosis and cell cycle arrest;
ORF3c
P0DTG1		 Unknown; first identified in SARS-CoV-2 but also present in SARS-CoV
ORF3d
P0DTG0		 Novel gene in SARS-CoV-2, of unknown function
ORF4
P59637 		Envelope (E) protein, virus assembly and budding
(structural protein)
ORF5
P59596 		Membrane (M) protein, virus assembly and budding
(structural protein)
ORF6
P59634		 Enhances cellular DNA synthesis;
Inhibits Type I IFN production and signaling
ORF7a
P59635		 Inhibits cellular protein synthesis;
Induces inflammatory response by NF-kappaB and IL-8 promotor;
Upregulate chemokines such as IL-8 and RANTES;
Upregulates JNK, p38 MAP kinase;
Induces apoptosis and cell cycle arrest
ORF7b
Q7TFA1		 Unknown
ORF8a
Q7TFA0		 Induces apoptosis through mitochondria pathway
ORF8b
Q80H93		 Enhances cellular DNA synthesis, also known as X5.
ORF9a
P59595 		Nucleocapsid (N) protein, viral RNA packaging
(structural protein)
ORF9b
P59636		 Induces apoptosis
ORF9c
Q7TLC7		 Also known as ORF14; function unknown and may not be protein-coding
ORF10
A0A663DJA2		 Novel gene in SARS-CoV-2, of unknown function; may not be protein-coding
UniProt identifiers shown for SARS-CoV proteins unless they are specific to SARS-CoV-2

The functions of several of the viral proteins are known.[25] ORFs 1a and 1b encode the replicase/transcriptase polyprotein, and later ORFs 2, 4, 5, and 9a encode, respectively, the four major structural proteins: spike (S), envelope (E), membrane (M), and nucleocapsid (N).[26] The later ORFs also encode for eight unique proteins (orf3a to orf9b), known as the accessory proteins, many with no known homologues. The different functions of the accessory proteins are not well understood.[25]

SARS coronaviruses have been genetically engineered in several laboratories.[27]

Phylogenetics edit

 
Phylogenetic tree of SARS-CoV-2 and closely related betacoronaviruses (left) and their geographic context (right)

Phylogenetic analysis showed that the evolutionary branch composed of Bat coronavirus BtKY72 and BM48-31 was the base group of SARS–related CoVs evolutionary tree, which separated from other SARS–related CoVs earlier than SARS-CoV-1 and SARS-CoV-2.[28][29]

SARSr‑CoV

Bat CoV BtKY72

Bat CoV BM48-31

SARS-CoV-1 related coronavirus

SARS-CoV-2 related coronavirus

SARS-CoV-1 related edit

A phylogenetic tree based on whole-genome sequences of SARS-CoV-1 and related coronaviruses is:

SARS‑CoV‑1 related coronavirus

Bat SARS CoV Rf1, 87.8% to SARS-CoV-1, Rhinolophus ferrumequinum, Yichang, Hubei[32]

BtCoV HKU3, 87.9% to SARS-CoV-1, Rhinolophus sinicus, Hong Kong and Guangdong[33]

LYRa11, 90.9% to SARS-CoV-1, Rhinolophus affinis, Baoshan, Yunnan[34]

Bat SARS-CoV/Rp3, 92.6% to SARS-CoV-1, Rhinolophus pearsoni, Nanning, Guangxi[32]

Bat SL-CoV YNLF_31C, 93.5% to SARS-CoV-1, Rhinolophus ferrumequinum, Lufeng, Yunnan[35]

Bat SL-CoV YNLF_34C, 93.5% to SARS-CoV-1, Rhinolophus ferrumequinum, Lufeng, Yunnan[35]

WIV16, 96.0% to SARS-CoV-1, Rhinolophus sinicus Kunming, Yunnan[37]

Civet SARS-CoV, 99.8% to SARS-CoV-1, Paguma larvata, market in Guangdong, China[33]

SARS-CoV-1

SARS-CoV-2, 79% to SARS-CoV-1[38]


SARS-CoV-2 related edit

A phylogenetic tree based on whole-genome sequences of SARS-CoV-2 and related coronaviruses is:[39][40]

SARS‑CoV‑2 related coronavirus

(Bat) Rc-o319, 81% to SARS-CoV-2, Rhinolophus cornutus, Iwate, Japan[41]

Bat SL-ZXC21, 88% to SARS-CoV-2, Rhinolophus pusillus, Zhoushan, Zhejiang[42]

Bat SL-ZC45, 88% to SARS-CoV-2, Rhinolophus pusillus, Zhoushan, Zhejiang[42]

Pangolin SARSr-CoV-GX, 85.3% to SARS-CoV-2, Manis javanica, smuggled from Southeast Asia[43]

Pangolin SARSr-CoV-GD, 90.1% to SARS-CoV-2, Manis javanica, smuggled from Southeast Asia[44]

Bat RshSTT182, 92.6% to SARS-CoV-2, Rhinolophus shameli, Steung Treng, Cambodia[45]

Bat RshSTT200, 92.6% to SARS-CoV-2, Rhinolophus shameli, Steung Treng, Cambodia[45]

(Bat) RacCS203, 91.5% to SARS-CoV-2, Rhinolophus acuminatus, Chachoengsao, Thailand[40]

(Bat) RmYN02, 93.3% to SARS-CoV-2, Rhinolophus malayanus, Mengla, Yunnan[46]

(Bat) RpYN06, 94.4% to SARS-CoV-2, Rhinolophus pusillus, Xishuangbanna, Yunnan[39]

(Bat) RaTG13, 96.1% to SARS-CoV-2, Rhinolophus affinis, Mojiang, Yunnan[47]

(Bat) BANAL-52, 96.8% to SARS-CoV-2, Rhinolophus malayanus, Vientiane, Laos[48]

SARS-CoV-2

SARS-CoV-1, 79% to SARS-CoV-2


Morphology edit

 
Illustration created at the Centers for Disease Control and Prevention (CDC), reveals ultrastructural morphology exhibited by coronaviruses; note the spikes that adorn the outer surface, which impart the look of a corona surrounding the virion.[49]
 
Illustration of SARSr-CoV virion

The morphology of the SARS-related coronavirus is characteristic of the coronavirus family as a whole. The viruses are large pleomorphic spherical particles with bulbous surface projections that form a corona around the particles in electron micrographs.[50] The size of the virus particles is in the 80–90 nm range. The envelope of the virus in electron micrographs appears as a distinct pair of electron dense shells.[51]

The viral envelope consists of a lipid bilayer where the membrane (M), envelope (E) and spike (S) proteins are anchored.[52] The spike proteins provide the virus with its bulbous surface projections, known as peplomers. The spike protein's interaction with its complement host cell receptor is central in determining the tissue tropism, infectivity, and species range of the virus.[53][54]

Inside the envelope, there is the nucleocapsid, which is formed from multiple copies of the nucleocapsid (N) protein, which are bound to the positive-sense single-stranded (~30 kb) RNA genome in a continuous beads-on-a-string type conformation.[55][56] The lipid bilayer envelope, membrane proteins, and nucleocapsid protect the virus when it is outside the host.[57]

Life cycle edit

SARS-related coronavirus follows the replication strategy typical of all coronaviruses.[19][58]

Attachment and entry edit

 
Coronavirus replication cycle

The attachment of the SARS-related coronavirus to the host cell is mediated by the spike protein and its receptor.[59] The spike protein receptor binding domain (RBD) recognizes and attaches to the angiotensin-converting enzyme 2 (ACE2) receptor.[4] Following attachment, the virus can enter the host cell by two different paths. The path the virus takes depends on the host protease available to cleave and activate the receptor-attached spike protein.[60]

The attachment of sarbecoviruses to ACE2 has been shown to be an evolutionarily conserved feature, present in many species of the taxon.[61]

The first path the SARS coronavirus can take to enter the host cell is by endocytosis and uptake of the virus in an endosome. The receptor-attached spike protein is then activated by the host's pH-dependent cysteine protease cathepsin L. Activation of the receptor-attached spike protein causes a conformational change, and the subsequent fusion of the viral envelope with the endosomal wall.[60]

Alternatively, the virus can enter the host cell directly by proteolytic cleavage of the receptor-attached spike protein by the host's TMPRSS2 or TMPRSS11D serine proteases at the cell surface.[62][63] In the SARS coronavirus, the activation of the C-terminal part of the spike protein triggers the fusion of the viral envelope with the host cell membrane by inducing conformational changes which are not fully understood.[64]

Genome translation edit

Function of coronavirus
nonstructural proteins (nsps)[65]
Protein Function
nsp1 Promotes host mRNA degradation, blocks host translation;[66]
blocks innate immune response
nsp2 Binds to prohibitin proteins;
unknown function
nsp3 Multidoman transmembrane protein; interacts with N protein; promotes cytokine expression; PLPro domain cleaves polyprotein pp1ab and blocks host's innate immune response; other domains unknown functions
nsp4 Transmembrane scaffold protein;
allows proper structure for double membrane vesicles (DMVs)
nsp5 3CLPro cleaves polyprotein pp1ab
nsp6 Transmembrane scaffold protein;
unknown function
nsp7 Forms hexadecameric complex with nsp8; processivity clamp for RdRp (nsp12)
nsp8 Forms hexadecameric complex with nsp7; processivity clamp for RdRp (nsp12); acts as a primase
nsp9 RNA-binding protein (RBP)
nsp10 nsp16 and nsp14 cofactor; forms heterodimer with both; stimulates 2-O-MT (nsp16) and ExoN (nsp14) activity
nsp11 Unknown function
nsp12 RNA-dependent RNA polymerase (RdRp)
nsp13 RNA helicase, 5′ triphosphatase
nsp14 N7 Methyltransferase, 3′-5′ exoribonuclease (ExoN); N7 MTase adds 5′ cap, ExoN proofreads genome
nsp15 Endoribonuclease (NendoU)
nsp16 2′-O-Methyltransferase (2-O-MT); protects viral RNA from MDA5

After fusion the nucleocapsid passes into the cytoplasm, where the viral genome is released.[59] The genome acts as a messenger RNA, and the cell's ribosome translates two-thirds of the genome, which corresponds to the open reading frame ORF1a and ORF1b, into two large overlapping polyproteins, pp1a and pp1ab.

The larger polyprotein pp1ab is a result of a -1 ribosomal frameshift caused by a slippery sequence (UUUAAAC) and a downstream RNA pseudoknot at the end of open reading frame ORF1a.[67] The ribosomal frameshift allows for the continuous translation of ORF1a followed by ORF1b.[68]

The polyproteins contain their own proteases, PLpro and 3CLpro, which cleave the polyproteins at different specific sites. The cleavage of polyprotein pp1ab yields 16 nonstructural proteins (nsp1 to nsp16). Product proteins include various replication proteins such as RNA-dependent RNA polymerase (RdRp), RNA helicase, and exoribonuclease (ExoN).[68]

The two SARS-CoV-2 proteases (PLpro and 3CLpro) also interfere with the immune system response to the viral infection by cleaving three immune system proteins. PLpro cleaves IRF3 and 3CLpro cleaves both NLRP12 and TAB1. "Direct cleavage of IRF3 by NSP3 could explain the blunted Type-I IFN response seen during SARS-CoV-2 infections while NSP5 mediated cleavage of NLRP12 and TAB1 point to a molecular mechanism for enhanced production of IL-6 and inflammatory response observed in COVID-19 patients."[69]

Replication and transcription edit

 
Model of the replicase-transcriptase complex of a coronavirus. RdRp for replication (red), ExoN for proofreading (dark blue), ExoN cofactor (yellow), RBPs to avoid secondary structure (light blue), RNA sliding clamp for processivity and primase domain for priming (green/orange), and a helicase to unwind RNA (downstream).

A number of the nonstructural replication proteins coalesce to form a multi-protein replicase-transcriptase complex (RTC).[68] The main replicase-transcriptase protein is the RNA-dependent RNA polymerase (RdRp). It is directly involved in the replication and transcription of RNA from an RNA strand. The other nonstructural proteins in the complex assist in the replication and transcription process.[65]

The protein nsp14 is a 3'-5' exoribonuclease which provides extra fidelity to the replication process. The exoribonuclease provides a proofreading function to the complex which the RNA-dependent RNA polymerase lacks. Similarly, proteins nsp7 and nsp8 form a hexadecameric sliding clamp as part of the complex which greatly increases the processivity of the RNA-dependent RNA polymerase.[65] The coronaviruses require the increased fidelity and processivity during RNA synthesis because of the relatively large genome size in comparison to other RNA viruses.[70]

One of the main functions of the replicase-transcriptase complex is to transcribe the viral genome. RdRp directly mediates the synthesis of negative-sense subgenomic RNA molecules from the positive-sense genomic RNA. This is followed by the transcription of these negative-sense subgenomic RNA molecules to their corresponding positive-sense mRNAs.[71]

The other important function of the replicase-transcriptase complex is to replicate the viral genome. RdRp directly mediates the synthesis of negative-sense genomic RNA from the positive-sense genomic RNA. This is followed by the replication of positive-sense genomic RNA from the negative-sense genomic RNA.[71]

The replicated positive-sense genomic RNA becomes the genome of the progeny viruses. The various smaller mRNAs are transcripts from the last third of the virus genome which follows the reading frames ORF1a and ORF1b. These mRNAs are translated into the four structural proteins (S, E, M, and N) that will become part of the progeny virus particles and also eight other accessory proteins (orf3 to orf9b) which assist the virus.[72]

Recombination edit

When two SARS-CoV genomes are present in a host cell, they may interact with each other to form recombinant genomes that can be transmitted to progeny viruses. Recombination likely occurs during genome replication when the RNA polymerase switches from one template to another (copy choice recombination).[73] Human SARS-CoV appears to have had a complex history of recombination between ancestral coronaviruses that were hosted in several different animal groups.[73][74]

Assembly and release edit

RNA translation occurs inside the endoplasmic reticulum. The viral structural proteins S, E and M move along the secretory pathway into the Golgi intermediate compartment. There, the M proteins direct most protein-protein interactions required for assembly of viruses following its binding to the nucleocapsid.[75]

Progeny viruses are released from the host cell by exocytosis through secretory vesicles.[75]

See also edit

Notes edit

  1. ^ The terms SARSr-CoV and SARS-CoV are sometimes used interchangeably, especially prior to the discovery of SARS-CoV-2. This may cause confusion when some publications refer to SARS-CoV-1 as SARS-CoV.

References edit

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Further reading edit

  • Peiris JS, Lai ST, Poon LL, Guan Y, Yam LY, Lim W, et al. (April 2003). "Coronavirus as a possible cause of severe acute respiratory syndrome". Lancet. 361 (9366): 1319–25. doi:10.1016/s0140-6736(03)13077-2. PMC 7112372. PMID 12711465.
  • Rota PA, Oberste MS, Monroe SS, Nix WA, Campagnoli R, Icenogle JP, et al. (May 2003). "Characterization of a novel coronavirus associated with severe acute respiratory syndrome". Science. 300 (5624): 1394–9. Bibcode:2003Sci...300.1394R. doi:10.1126/science.1085952. PMID 12730500.
  • Marra MA, Jones SJ, Astell CR, Holt RA, Brooks-Wilson A, Butterfield YS, et al. (May 2003). "The Genome sequence of the SARS-associated coronavirus". Science. 300 (5624): 1399–404. Bibcode:2003Sci...300.1399M. doi:10.1126/science.1085953. PMID 12730501.
  • Snijder EJ, Bredenbeek PJ, Dobbe JC, Thiel V, Ziebuhr J, Poon LL, et al. (August 2003). "Unique and conserved features of genome and proteome of SARS-coronavirus, an early split-off from the coronavirus group 2 lineage". Journal of Molecular Biology. 331 (5): 991–1004. CiteSeerX 10.1.1.319.7007. doi:10.1016/S0022-2836(03)00865-9. PMC 7159028. PMID 12927536. S2CID 14974326.
  • Yount B, Roberts RS, Lindesmith L, Baric RS (August 2006). "Rewiring the severe acute respiratory syndrome coronavirus (SARS-CoV) transcription circuit: engineering a recombination-resistant genome". Proceedings of the National Academy of Sciences of the United States of America. 103 (33): 12546–51. Bibcode:2006PNAS..10312546Y. doi:10.1073/pnas.0605438103. PMC 1531645. PMID 16891412.
  • Thiel V, ed. (2007). Coronaviruses: Molecular and Cellular Biology (1st ed.). Caister Academic Press. ISBN 978-1-904455-16-5.
  • Enjuanes L, Sola I, Zúñiga S, Almazán F (2008). "Coronavirus Replication and Interaction with Host". In Mettenleiter TC, Sobrino F (eds.). Animal Viruses: Molecular Biology. Caister Academic Press. ISBN 978-1-904455-22-6.

External links edit

  •   Media related to Severe acute respiratory syndrome-related coronavirus at Wikimedia Commons
  •   Data related to SARS-related coronavirus at Wikispecies
  • (archived 23 April 2003)
  • The SARS virus genetic map 18 August 2006 at the Wayback Machine
  • Science special on the SARS virus (free content: no registration required)
  • at the Wayback Machine (archived 1 March 2005)
  • (archived 12 April 2016)
  • World Health Organization on alert

December 04, 2023
sars, related, coronavirus, this, article, about, species, coronavirus, comprising, multiple, strains, strain, that, causes, sars, sars, strain, that, causes, covid, sars, severe, acute, respiratory, syndrome, related, coronavirus, sarsr, sars, note, species, . This article is about a species of coronavirus comprising multiple strains For the strain that causes SARS see SARS CoV 1 For the strain that causes COVID 19 see SARS CoV 2 Severe acute respiratory syndrome related coronavirus SARSr CoV or SARS CoV note 1 is a species of virus consisting of many known strains phylogenetically related to severe acute respiratory syndrome coronavirus 1 SARS CoV 1 that have been shown to possess the capability to infect humans bats and certain other mammals 2 3 These enveloped positive sense single stranded RNA viruses enter host cells by binding to the angiotensin converting enzyme 2 ACE2 receptor 4 The SARSr CoV species is a member of the genus Betacoronavirus and of the subgenus Sarbecovirus SARS Betacoronavirus 5 6 SarbecovirusTransmission electron micrograph of SARS related coronaviruses emerging from host cells cultured in the labVirus classification unranked VirusRealm RiboviriaKingdom OrthornaviraePhylum PisuviricotaClass PisoniviricetesOrder NidoviralesFamily CoronaviridaeGenus BetacoronavirusSubgenus SarbecovirusStrainsSARS CoV 1 SARS CoV 2 Bat SARS like coronavirus WIV1 Bat coronavirus RaTG13 Numerous other bat hosted strainsSynonymsSARS coronavirus SARS related coronavirus Severe acute respiratory syndrome coronavirus 1 Two strains of the virus have caused outbreaks of severe respiratory diseases in humans severe acute respiratory syndrome coronavirus 1 SARS CoV or SARS CoV 1 which caused the 2002 2004 outbreak of severe acute respiratory syndrome SARS and severe acute respiratory syndrome coronavirus 2 SARS CoV 2 which is causing the ongoing pandemic of COVID 19 7 8 There are hundreds of other strains of SARSr CoV which are only known to infect non human species bats are a major reservoir of many strains of SARSr CoV several strains have been identified in Himalayan palm civets which were likely ancestors of SARS CoV 1 7 9 The SARS related coronavirus was one of several viruses identified by the World Health Organization WHO in 2016 as a likely cause of a future epidemic in a new plan developed after the Ebola epidemic for urgent research and development before and during an epidemic towards diagnostic tests vaccines and medicines This prediction came to pass with the COVID 19 pandemic 10 11 Contents 1 Classification 2 Genome 3 Phylogenetics 3 1 SARS CoV 1 related 3 2 SARS CoV 2 related 4 Morphology 5 Life cycle 5 1 Attachment and entry 5 2 Genome translation 5 3 Replication and transcription 5 4 Recombination 5 5 Assembly and release 6 See also 7 Notes 8 References 9 Further reading 10 External linksClassification editSARS related coronavirus is a member of the genus Betacoronavirus group 2 and monotypic of the subgenus Sarbecovirus subgroup B 12 Sarbecoviruses unlike embecoviruses or alphacoronaviruses have only one papain like proteinase PLpro instead of two in the open reading frame ORF1ab 13 SARSr CoV was determined to be an early split off from the betacoronaviruses based on a set of conserved domains that it shares with the group 14 15 Bats serve as the main host reservoir species for the SARS related coronaviruses like SARS CoV 1 and SARS CoV 2 The virus has coevolved in the bat host reservoir over a long period of time 16 Only recently have strains of SARS related coronavirus been observed to have evolved into having been able to make the cross species jump from bats to humans as in the case of the strains SARS CoV 1 and SARS CoV 2 17 4 Both of these strains descended from a single ancestor but made the cross species jump into humans separately SARS CoV 2 is not a direct descendant of SARS CoV 1 7 Genome edit nbsp Genome organization and viral proteins of SARS CoVThe SARS related coronavirus is an enveloped positive sense single stranded RNA virus Its genome is about 30 kb which is one of the largest among RNA viruses The virus has 14 open reading frames which overlap in some cases 18 The genome has the usual 5 methylated cap and a 3 polyadenylated tail 19 There are 265 nucleotides in the 5 UTR and 342 nucleotides in the 3 UTR 18 The 5 methylated cap and 3 polyadenylated tail allows the positive sense RNA genome to be directly translated by the host cell s ribosome on viral entry 20 SARSr CoV is similar to other coronaviruses in that its genome expression starts with translation by the host cell s ribosomes of its initial two large overlapping open reading frames ORFs 1a and 1b both of which produce polyproteins 18 Function of SARSr CoV genome proteinsProtein Function 21 22 23 24 ORF1abP0C6X7 Replicase transcriptase polyprotein pp1ab nonstructural proteins ORF2P59594 Spike S protein virus binding and entry structural protein ORF3aP59632 Interacts with S E M structural proteins Ion channel activity Upregulates cytokines and chemokines such as IL 8 and RANTES Upregulates NF kB and JNK Induces apoptosis and cell cycle arrest via Caspase 8 and 9 and by Bax p53 and p38 MAP kinaseORF3bP59633 Upregulates cytokines and chemokines by RUNX1b Inhibits Type I IFN production and signaling Induces apoptosis and cell cycle arrest ORF3cP0DTG1 Unknown first identified in SARS CoV 2 but also present in SARS CoVORF3dP0DTG0 Novel gene in SARS CoV 2 of unknown functionORF4P59637 Envelope E protein virus assembly and budding structural protein ORF5P59596 Membrane M protein virus assembly and budding structural protein ORF6P59634 Enhances cellular DNA synthesis Inhibits Type I IFN production and signalingORF7aP59635 Inhibits cellular protein synthesis Induces inflammatory response by NF kappaB and IL 8 promotor Upregulate chemokines such as IL 8 and RANTES Upregulates JNK p38 MAP kinase Induces apoptosis and cell cycle arrestORF7bQ7TFA1 UnknownORF8aQ7TFA0 Induces apoptosis through mitochondria pathwayORF8bQ80H93 Enhances cellular DNA synthesis also known as X5 ORF9aP59595 Nucleocapsid N protein viral RNA packaging structural protein ORF9bP59636 Induces apoptosisORF9cQ7TLC7 Also known as ORF14 function unknown and may not be protein codingORF10A0A663DJA2 Novel gene in SARS CoV 2 of unknown function may not be protein codingUniProt identifiers shown for SARS CoV proteins unless they are specific to SARS CoV 2The functions of several of the viral proteins are known 25 ORFs 1a and 1b encode the replicase transcriptase polyprotein and later ORFs 2 4 5 and 9a encode respectively the four major structural proteins spike S envelope E membrane M and nucleocapsid N 26 The later ORFs also encode for eight unique proteins orf3a to orf9b known as the accessory proteins many with no known homologues The different functions of the accessory proteins are not well understood 25 SARS coronaviruses have been genetically engineered in several laboratories 27 Phylogenetics edit nbsp Phylogenetic tree of SARS CoV 2 and closely related betacoronaviruses left and their geographic context right Phylogenetic analysis showed that the evolutionary branch composed of Bat coronavirus BtKY72 and BM48 31 was the base group of SARS related CoVs evolutionary tree which separated from other SARS related CoVs earlier than SARS CoV 1 and SARS CoV 2 28 29 SARSr CoV Bat CoV BtKY72Bat CoV BM48 31SARS CoV 1 related coronavirusSARS CoV 2 related coronavirusSARS CoV 1 related edit A phylogenetic tree based on whole genome sequences of SARS CoV 1 and related coronaviruses is SARS CoV 1 related coronavirus 16BO133 86 3 to SARS CoV 1 Rhinolophus ferrumequinum North Jeolla South Korea 30 JTMC15 86 4 to SARS CoV 1 Rhinolophus ferrumequinum Tonghua Jilin 31 Bat SARS CoV Rf1 87 8 to SARS CoV 1 Rhinolophus ferrumequinum Yichang Hubei 32 BtCoV HKU3 87 9 to SARS CoV 1 Rhinolophus sinicus Hong Kong and Guangdong 33 LYRa11 90 9 to SARS CoV 1 Rhinolophus affinis Baoshan Yunnan 34 Bat SARS CoV Rp3 92 6 to SARS CoV 1 Rhinolophus pearsoni Nanning Guangxi 32 Bat SL CoV YNLF 31C 93 5 to SARS CoV 1 Rhinolophus ferrumequinum Lufeng Yunnan 35 Bat SL CoV YNLF 34C 93 5 to SARS CoV 1 Rhinolophus ferrumequinum Lufeng Yunnan 35 SHC014 CoV 95 4 to SARS CoV 1 Rhinolophus sinicus Kunming Yunnan 36 WIV1 95 6 to SARS CoV 1 Rhinolophus sinicus Kunming Yunnan 36 WIV16 96 0 to SARS CoV 1 Rhinolophus sinicus Kunming Yunnan 37 Civet SARS CoV 99 8 to SARS CoV 1 Paguma larvata market in Guangdong China 33 SARS CoV 1SARS CoV 2 79 to SARS CoV 1 38 SARS CoV 2 related edit A phylogenetic tree based on whole genome sequences of SARS CoV 2 and related coronaviruses is 39 40 SARS CoV 2 related coronavirus Bat Rc o319 81 to SARS CoV 2 Rhinolophus cornutus Iwate Japan 41 Bat SL ZXC21 88 to SARS CoV 2 Rhinolophus pusillus Zhoushan Zhejiang 42 Bat SL ZC45 88 to SARS CoV 2 Rhinolophus pusillus Zhoushan Zhejiang 42 Pangolin SARSr CoV GX 85 3 to SARS CoV 2 Manis javanica smuggled from Southeast Asia 43 Pangolin SARSr CoV GD 90 1 to SARS CoV 2 Manis javanica smuggled from Southeast Asia 44 Bat RshSTT182 92 6 to SARS CoV 2 Rhinolophus shameli Steung Treng Cambodia 45 Bat RshSTT200 92 6 to SARS CoV 2 Rhinolophus shameli Steung Treng Cambodia 45 Bat RacCS203 91 5 to SARS CoV 2 Rhinolophus acuminatus Chachoengsao Thailand 40 Bat RmYN02 93 3 to SARS CoV 2 Rhinolophus malayanus Mengla Yunnan 46 Bat RpYN06 94 4 to SARS CoV 2 Rhinolophus pusillus Xishuangbanna Yunnan 39 Bat RaTG13 96 1 to SARS CoV 2 Rhinolophus affinis Mojiang Yunnan 47 Bat BANAL 52 96 8 to SARS CoV 2 Rhinolophus malayanus Vientiane Laos 48 SARS CoV 2SARS CoV 1 79 to SARS CoV 2Morphology edit nbsp Illustration created at the Centers for Disease Control and Prevention CDC reveals ultrastructural morphology exhibited by coronaviruses note the spikes that adorn the outer surface which impart the look of a corona surrounding the virion 49 nbsp Illustration of SARSr CoV virionThe morphology of the SARS related coronavirus is characteristic of the coronavirus family as a whole The viruses are large pleomorphic spherical particles with bulbous surface projections that form a corona around the particles in electron micrographs 50 The size of the virus particles is in the 80 90 nm range The envelope of the virus in electron micrographs appears as a distinct pair of electron dense shells 51 The viral envelope consists of a lipid bilayer where the membrane M envelope E and spike S proteins are anchored 52 The spike proteins provide the virus with its bulbous surface projections known as peplomers The spike protein s interaction with its complement host cell receptor is central in determining the tissue tropism infectivity and species range of the virus 53 54 Inside the envelope there is the nucleocapsid which is formed from multiple copies of the nucleocapsid N protein which are bound to the positive sense single stranded 30 kb RNA genome in a continuous beads on a string type conformation 55 56 The lipid bilayer envelope membrane proteins and nucleocapsid protect the virus when it is outside the host 57 Life cycle editSARS related coronavirus follows the replication strategy typical of all coronaviruses 19 58 Attachment and entry edit nbsp Coronavirus replication cycleThe attachment of the SARS related coronavirus to the host cell is mediated by the spike protein and its receptor 59 The spike protein receptor binding domain RBD recognizes and attaches to the angiotensin converting enzyme 2 ACE2 receptor 4 Following attachment the virus can enter the host cell by two different paths The path the virus takes depends on the host protease available to cleave and activate the receptor attached spike protein 60 The attachment of sarbecoviruses to ACE2 has been shown to be an evolutionarily conserved feature present in many species of the taxon 61 The first path the SARS coronavirus can take to enter the host cell is by endocytosis and uptake of the virus in an endosome The receptor attached spike protein is then activated by the host s pH dependent cysteine protease cathepsin L Activation of the receptor attached spike protein causes a conformational change and the subsequent fusion of the viral envelope with the endosomal wall 60 Alternatively the virus can enter the host cell directly by proteolytic cleavage of the receptor attached spike protein by the host s TMPRSS2 or TMPRSS11D serine proteases at the cell surface 62 63 In the SARS coronavirus the activation of the C terminal part of the spike protein triggers the fusion of the viral envelope with the host cell membrane by inducing conformational changes which are not fully understood 64 Genome translation edit Function of coronavirus nonstructural proteins nsps 65 Protein Functionnsp1 Promotes host mRNA degradation blocks host translation 66 blocks innate immune responsensp2 Binds to prohibitin proteins unknown functionnsp3 Multidoman transmembrane protein interacts with N protein promotes cytokine expression PLPro domain cleaves polyprotein pp1ab and blocks host s innate immune response other domains unknown functionsnsp4 Transmembrane scaffold protein allows proper structure for double membrane vesicles DMVs nsp5 3CLPro cleaves polyprotein pp1abnsp6 Transmembrane scaffold protein unknown functionnsp7 Forms hexadecameric complex with nsp8 processivity clamp for RdRp nsp12 nsp8 Forms hexadecameric complex with nsp7 processivity clamp for RdRp nsp12 acts as a primasensp9 RNA binding protein RBP nsp10 nsp16 and nsp14 cofactor forms heterodimer with both stimulates 2 O MT nsp16 and ExoN nsp14 activitynsp11 Unknown functionnsp12 RNA dependent RNA polymerase RdRp nsp13 RNA helicase 5 triphosphatasensp14 N7 Methyltransferase 3 5 exoribonuclease ExoN N7 MTase adds 5 cap ExoN proofreads genomensp15 Endoribonuclease NendoU nsp16 2 O Methyltransferase 2 O MT protects viral RNA from MDA5After fusion the nucleocapsid passes into the cytoplasm where the viral genome is released 59 The genome acts as a messenger RNA and the cell s ribosome translates two thirds of the genome which corresponds to the open reading frame ORF1a and ORF1b into two large overlapping polyproteins pp1a and pp1ab The larger polyprotein pp1ab is a result of a 1 ribosomal frameshift caused by a slippery sequence UUUAAAC and a downstream RNA pseudoknot at the end of open reading frame ORF1a 67 The ribosomal frameshift allows for the continuous translation of ORF1a followed by ORF1b 68 The polyproteins contain their own proteases PLpro and 3CLpro which cleave the polyproteins at different specific sites The cleavage of polyprotein pp1ab yields 16 nonstructural proteins nsp1 to nsp16 Product proteins include various replication proteins such as RNA dependent RNA polymerase RdRp RNA helicase and exoribonuclease ExoN 68 The two SARS CoV 2 proteases PLpro and 3CLpro also interfere with the immune system response to the viral infection by cleaving three immune system proteins PLpro cleaves IRF3 and 3CLpro cleaves both NLRP12 and TAB1 Direct cleavage of IRF3 by NSP3 could explain the blunted Type I IFN response seen during SARS CoV 2 infections while NSP5 mediated cleavage of NLRP12 and TAB1 point to a molecular mechanism for enhanced production of IL 6 and inflammatory response observed in COVID 19 patients 69 Replication and transcription edit nbsp Model of the replicase transcriptase complex of a coronavirus RdRp for replication red ExoN for proofreading dark blue ExoN cofactor yellow RBPs to avoid secondary structure light blue RNA sliding clamp for processivity and primase domain for priming green orange and a helicase to unwind RNA downstream A number of the nonstructural replication proteins coalesce to form a multi protein replicase transcriptase complex RTC 68 The main replicase transcriptase protein is the RNA dependent RNA polymerase RdRp It is directly involved in the replication and transcription of RNA from an RNA strand The other nonstructural proteins in the complex assist in the replication and transcription process 65 The protein nsp14 is a 3 5 exoribonuclease which provides extra fidelity to the replication process The exoribonuclease provides a proofreading function to the complex which the RNA dependent RNA polymerase lacks Similarly proteins nsp7 and nsp8 form a hexadecameric sliding clamp as part of the complex which greatly increases the processivity of the RNA dependent RNA polymerase 65 The coronaviruses require the increased fidelity and processivity during RNA synthesis because of the relatively large genome size in comparison to other RNA viruses 70 One of the main functions of the replicase transcriptase complex is to transcribe the viral genome RdRp directly mediates the synthesis of negative sense subgenomic RNA molecules from the positive sense genomic RNA This is followed by the transcription of these negative sense subgenomic RNA molecules to their corresponding positive sense mRNAs 71 The other important function of the replicase transcriptase complex is to replicate the viral genome RdRp directly mediates the synthesis of negative sense genomic RNA from the positive sense genomic RNA This is followed by the replication of positive sense genomic RNA from the negative sense genomic RNA 71 The replicated positive sense genomic RNA becomes the genome of the progeny viruses The various smaller mRNAs are transcripts from the last third of the virus genome which follows the reading frames ORF1a and ORF1b These mRNAs are translated into the four structural proteins S E M and N that will become part of the progeny virus particles and also eight other accessory proteins orf3 to orf9b which assist the virus 72 Recombination edit When two SARS CoV genomes are present in a host cell they may interact with each other to form recombinant genomes that can be transmitted to progeny viruses Recombination likely occurs during genome replication when the RNA polymerase switches from one template to another copy choice recombination 73 Human SARS CoV appears to have had a complex history of recombination between ancestral coronaviruses that were hosted in several different animal groups 73 74 Assembly and release edit RNA translation occurs inside the endoplasmic reticulum The viral structural proteins S E and M move along the secretory pathway into the Golgi intermediate compartment There the M proteins direct most protein protein interactions required for assembly of viruses following its binding to the nucleocapsid 75 Progeny viruses are released from the host cell by exocytosis through secretory vesicles 75 See also edit nbsp COVID 19 portal nbsp Viruses portalBat SARS like coronavirus WIV1 SL CoV WIV1 Bat SARS like coronavirus RsSHC014 Bat coronavirus RaTG13 Civet SARS CoVNotes edit The terms SARSr CoV and SARS CoV are sometimes used interchangeably especially prior to the discovery of SARS CoV 2 This may cause confusion when some publications refer to SARS CoV 1 as SARS CoV References edit ICTV Taxonomy history Severe acute respiratory syndrome related coronavirus International Committee on Taxonomy of Viruses ICTV Retrieved 27 January 2019 Branswell H 9 November 2015 SARS like virus in bats shows potential to infect humans study finds Stat News Retrieved 20 February 2020 Wong AC Li X Lau SK Woo PC February 2019 Global Epidemiology of Bat Coronaviruses Viruses 11 2 174 doi 10 3390 v11020174 PMC 6409556 PMID 30791586 Most notably horseshoe bats were found to be the reservoir of SARS like CoVs while palm civet cats are considered to be the intermediate host for SARS CoVs 43 44 45 a b c Ge XY Li JL Yang XL Chmura AA Zhu G Epstein JH et al November 2013 Isolation and characterization of a bat SARS like coronavirus that uses the ACE2 receptor Nature 503 7477 535 8 Bibcode 2013Natur 503 535G doi 10 1038 nature12711 PMC 5389864 PMID 24172901 Virus Taxonomy 2018 Release International Committee on Taxonomy of Viruses ICTV October 2018 Retrieved 13 January 2019 Woo PC Huang Y Lau SK Yuen KY August 2010 Coronavirus genomics and bioinformatics analysis Viruses 2 8 1804 20 doi 10 3390 v2081803 PMC 3185738 PMID 21994708 Figure 2 Phylogenetic analysis of RNA dependent RNA polymerases Pol of coronaviruses with complete genome sequences available The tree was constructed by the neighbor joining method and rooted using Breda virus polyprotein a b c Coronaviridae Study Group of the International Committee on Taxonomy of Viruses March 2020 The species Severe acute respiratory syndrome related coronavirus classifying 2019 nCoV and naming it SARS CoV 2 Nature Microbiology 5 4 536 544 doi 10 1038 s41564 020 0695 z PMC 7095448 PMID 32123347 Kohen Jon Kupferschmidth Kai 28 February 2020 Strategies shift as coronavirus pandemic looms Science 367 6481 962 963 Bibcode 2020Sci 367 962C doi 10 1126 science 367 6481 962 PMID 32108093 S2CID 211556915 Lau SK Li KS Huang Y Shek CT Tse H Wang M et al March 2010 Ecoepidemiology and complete genome comparison of different strains of severe acute respiratory syndrome related Rhinolophus bat coronavirus in China reveal bats as a reservoir for acute self limiting infection that allows recombination events Journal of Virology 84 6 2808 19 doi 10 1128 JVI 02219 09 PMC 2826035 PMID 20071579 Kieny M After Ebola a Blueprint Emerges to Jump Start R amp D Scientific American Blog Network Archived from the original on 20 December 2016 Retrieved 13 December 2016 LIST OF PATHOGENS World Health Organization Archived from the original on 20 December 2016 Retrieved 13 December 2016 Wong AC Li X Lau SK Woo PC February 2019 Global Epidemiology of Bat Coronaviruses Viruses 11 2 174 doi 10 3390 v11020174 PMC 6409556 PMID 30791586 See Figure 1 Woo PC Huang Y Lau SK Yuen KY August 2010 Coronavirus genomics and bioinformatics analysis Viruses 2 8 1804 20 doi 10 3390 v2081803 PMC 3185738 PMID 21994708 See Figure 1 Woo PC Huang Y Lau SK Yuen KY August 2010 Coronavirus genomics and bioinformatics analysis Viruses 2 8 1804 20 doi 10 3390 v2081803 PMC 3185738 PMID 21994708 Furthermore subsequent phylogenetic analysis using both complete genome sequence and proteomic approaches it was concluded that SARSr CoV is probably an early split off from the Betacoronavirus lineage 1 See Figure 2 Coronaviridae Figures Positive Sense RNA Viruses Positive 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pleomorphic particles that averaged 78 nm in diameter Figure 1A Neuman BW Adair BD Yoshioka C Quispe JD Orca G Kuhn P et al August 2006 Supramolecular architecture of severe acute respiratory syndrome coronavirus revealed by electron cryomicroscopy Journal of Virology 80 16 7918 28 doi 10 1128 JVI 00645 06 PMC 1563832 PMID 16873249 Particle diameters ranged from 50 to 150 nm excluding the spikes with mean particle diameters of 82 to 94 nm Also See Figure 1 for double shell Lai MM Cavanagh D 1997 The molecular biology of coronaviruses Advances in Virus Research 48 1 100 doi 10 1016 S0065 3527 08 60286 9 ISBN 9780120398485 PMC 7130985 PMID 9233431 Masters PS 1 January 2006 The molecular biology of coronaviruses Advances in Virus Research Vol 66 Academic Press pp 193 292 doi 10 1016 S0065 3527 06 66005 3 ISBN 9780120398690 PMC 7112330 PMID 16877062 Nevertheless the interaction between S protein and receptor remains the principal if not sole determinant of coronavirus host species range 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March 2022 ACE2 binding is an ancestral and evolvable trait of sarbecoviruses Nature 603 7903 913 918 Bibcode 2022Natur 603 913S doi 10 1038 s41586 022 04464 z ISSN 1476 4687 PMC 8967715 PMID 35114688 Heurich A Hofmann Winkler H Gierer S Liepold T Jahn O Pohlmann S January 2014 TMPRSS2 and ADAM17 cleave ACE2 differentially and only proteolysis by TMPRSS2 augments entry driven by the severe acute respiratory syndrome coronavirus spike protein Journal of Virology 88 2 1293 307 doi 10 1128 JVI 02202 13 PMC 3911672 PMID 24227843 The SARS CoV can hijack two cellular proteolytic systems to ensure the adequate processing of its S protein Cleavage of SARS S can be facilitated by cathepsin L a pH dependent endo lysosomal host cell protease upon uptake of virions into target cell endosomes 25 Alternatively the type II transmembrane serine proteases TTSPs TMPRSS2 and HAT can activate SARS S presumably by cleavage of SARS S at or close to the cell surface and activation of SARS S by TMPRSS2 allows for cathepsin L independent cellular entry 26 28 Zumla A Chan JF Azhar EI Hui DS Yuen KY May 2016 Coronaviruses drug discovery and therapeutic options Nature Reviews Drug Discovery 15 5 327 47 doi 10 1038 nrd 2015 37 PMC 7097181 PMID 26868298 S is activated and cleaved into the S1 and S2 subunits by other host proteases such as transmembrane protease serine 2 TMPRSS2 and TMPRSS11D which enables cell surface non endosomal virus entry at the plasma membrane Li Z Tomlinson AC Wong AH Zhou D Desforges M Talbot PJ et al October 2019 The human coronavirus HCoV 229E S protein structure and receptor binding eLife 8 doi 10 7554 eLife 51230 PMC 6970540 PMID 31650956 a b c Fehr AR Perlman S 2015 Coronaviruses An Overview of Their Replication and Pathogenesis In Maier HJ Bickerton E Britton P eds Coronaviruses Methods in Molecular Biology Vol 1282 Springer pp 1 23 doi 10 1007 978 1 4939 2438 7 1 ISBN 978 1 4939 2438 7 PMC 4369385 PMID 25720466 See Table 2 Rao S Hoskins I Tonn T Garcia PD Ozadam H Sarinay Cenik E Cenik C September 2021 Genes with 5 terminal oligopyrimidine tracts preferentially escape global suppression of translation by the SARS CoV 2 Nsp1 protein RNA 27 9 1025 1045 doi 10 1261 rna 078661 120 PMC 8370740 PMID 34127534 Masters PS 1 January 2006 The molecular biology of coronaviruses Advances in Virus Research Academic Press 66 193 292 doi 10 1016 S0065 3527 06 66005 3 ISBN 9780120398690 PMC 7112330 PMID 16877062 See Figure 8 a b c Fehr AR Perlman S 2015 Coronaviruses An Overview of Their Replication and Pathogenesis In Maier HJ Bickerton E Britton P eds Coronaviruses Methods in Molecular Biology Vol 1282 Springer pp 1 23 doi 10 1007 978 1 4939 2438 7 1 ISBN 978 1 4939 2438 7 PMC 4369385 PMID 25720466 See section Replicase Protein Expression Mehdi Moustaqil 5 June 2020 SARS CoV 2 proteases cleave IRF3 and critical modulators of inflammatory pathways NLRP12 and TAB1 implications for disease presentation across species and the search for reservoir hosts bioRxiv 2020 06 05 135699 doi 10 1101 2020 06 05 135699 S2CID 219604020 Sexton NR Smith EC Blanc H Vignuzzi M Peersen OB Denison MR August 2016 Homology Based Identification of a Mutation in the Coronavirus RNA Dependent RNA Polymerase That Confers Resistance to Multiple Mutagens Journal of Virology 90 16 7415 28 doi 10 1128 JVI 00080 16 PMC 4984655 PMID 27279608 Finally these results combined with those from previous work 33 44 suggest that CoVs encode at least three proteins involved in fidelity nsp12 RdRp nsp14 ExoN and nsp10 supporting the assembly of a multiprotein replicase fidelity complex as described previously 38 a b Fehr AR Perlman S 2015 Coronaviruses An Overview of Their Replication and Pathogenesis In Maier HJ Bickerton E Britton P eds Coronaviruses Methods in Molecular Biology Vol 1282 Springer pp 1 23 doi 10 1007 978 1 4939 2438 7 1 ISBN 978 1 4939 2438 7 PMC 4369385 PMID 25720466 See section Corona Life Cycle Replication and Transcription Fehr AR Perlman S 2015 Coronaviruses An Overview of Their Replication and Pathogenesis In Maier HJ Bickerton E Britton P eds Coronaviruses Methods in Molecular Biology Vol 1282 Springer pp 1 23 doi 10 1007 978 1 4939 2438 7 1 ISBN 978 1 4939 2438 7 PMC 4369385 PMID 25720466 See Figure 1 a b Zhang XW Yap YL Danchin A Testing the hypothesis of a recombinant origin of the SARS associated coronavirus Arch Virol 2005 Jan 150 1 1 20 Epub 2004 Oct 11 PMID 15480857 Stanhope MJ Brown JR Amrine Madsen H Evidence from the evolutionary analysis of nucleotide sequences for a recombinant history of SARS CoV Infect Genet Evol 2004 Mar 4 1 15 9 PMID 15019585 a b Fehr AR Perlman S 2015 Coronaviruses An Overview of Their Replication and Pathogenesis In Maier HJ Bickerton E Britton P eds Coronaviruses Methods in Molecular Biology Vol 1282 Springer pp 1 23 doi 10 1007 978 1 4939 2438 7 1 ISBN 978 1 4939 2438 7 PMC 4369385 PMID 25720466 See section Coronavirus Life Cycle Assembly and ReleaseFurther reading editPeiris JS Lai ST Poon LL Guan Y Yam LY Lim W et al April 2003 Coronavirus as a possible cause of severe acute respiratory syndrome Lancet 361 9366 1319 25 doi 10 1016 s0140 6736 03 13077 2 PMC 7112372 PMID 12711465 Rota PA Oberste MS Monroe SS Nix WA Campagnoli R Icenogle JP et al May 2003 Characterization of a novel coronavirus associated with severe acute respiratory syndrome Science 300 5624 1394 9 Bibcode 2003Sci 300 1394R doi 10 1126 science 1085952 PMID 12730500 Marra MA Jones SJ Astell CR Holt RA Brooks Wilson A Butterfield YS et al May 2003 The Genome sequence of the SARS associated coronavirus Science 300 5624 1399 404 Bibcode 2003Sci 300 1399M doi 10 1126 science 1085953 PMID 12730501 Snijder EJ Bredenbeek PJ Dobbe JC Thiel V Ziebuhr J Poon LL et al August 2003 Unique and conserved features of genome and proteome of SARS coronavirus an early split off from the coronavirus group 2 lineage Journal of Molecular Biology 331 5 991 1004 CiteSeerX 10 1 1 319 7007 doi 10 1016 S0022 2836 03 00865 9 PMC 7159028 PMID 12927536 S2CID 14974326 Yount B Roberts RS Lindesmith L Baric RS August 2006 Rewiring the severe acute respiratory syndrome coronavirus SARS CoV transcription circuit engineering a recombination resistant genome Proceedings of the National Academy of Sciences of the United States of America 103 33 12546 51 Bibcode 2006PNAS 10312546Y doi 10 1073 pnas 0605438103 PMC 1531645 PMID 16891412 Thiel V ed 2007 Coronaviruses Molecular and Cellular Biology 1st ed Caister Academic Press ISBN 978 1 904455 16 5 Enjuanes L Sola I Zuniga S Almazan F 2008 Coronavirus Replication and Interaction with Host In Mettenleiter TC Sobrino F eds Animal Viruses Molecular Biology Caister Academic Press ISBN 978 1 904455 22 6 External links edit nbsp Media related to Severe acute respiratory syndrome related coronavirus at Wikimedia Commons nbsp Data related to SARS related coronavirus at Wikispecies WHO press release identifying and naming the SARS virus archived 23 April 2003 The SARS virus genetic map Archived 18 August 2006 at the Wayback Machine Science special on the SARS virus free content no registration required McGill University SARS Resources at the Wayback Machine archived 1 March 2005 U S Centers for Disease Control and Prevention CDC SARS home archived 12 April 2016 World Health Organization on alert Retrieved from https en wikipedia org w index php title SARS related coronavirus amp oldid 1186624745, wikipedia, wiki, book, books, library,

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