SARS-related coronavirus

Species of coronavirus causing SARS and COVID-19

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.

Betacoronavirus pandemicum

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
Species:  |

Betacoronavirus pandemicum

Strains

* SARS-CoV-1
* SARS-CoV-2
* Bat SARS-like coronavirus WIV1
* Bat coronavirus RaTG13
* Numerous other bat-hosted strains

Synonyms

* SARS coronavirus
* SARS-related coronavirus
* Severe acute respiratory syndrome coronavirus[1]

Betacoronavirus pandemicum[2] (commonly known as Severe acute respiratory syndrome–related coronavirus, abbreviated as SARSr-CoV or SARS-CoV)[note 1] is a species of virus consisting of many known strains. 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), the cause of the 2002–2004 outbreak of severe acute respiratory syndrome (SARS), and severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the cause of the pandemic of COVID-19.[3][4] There are hundreds of other strains of SARSr-CoV, which are only known to infect non-human mammal 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.[3][5][6][7]

These enveloped, positive-sense single-stranded RNA viruses enter host cells by binding to the angiotensin-converting enzyme 2 (ACE2) receptor.[8] The SARSr-CoV species is a member of the genus Betacoronavirus and the only species of the subgenus Sarbecovirus (SARS Betacoronavirus).[9][10]

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.[11][12]

## Classification

[edit]

SARS-related coronavirus is a member of the genus Betacoronavirus (group 2) and monotypic of the subgenus Sarbecovirus (subgroup B).[13] Sarbecoviruses, unlike embecoviruses or alphacoronaviruses, have only one papain-like proteinase (PLpro) instead of two in the open reading frame ORF1ab.[14] 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.[15][16]

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.[17] 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.[18][8] 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.[3]

## 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.[19] The genome has the usual 5′ methylated cap and a 3′ polyadenylated tail.[20] There are 265 nucleotides in the 5'UTR and 342 nucleotides in the 3'UTR.[19]

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.[21] 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.[19]

Function of SARSr-CoV
genome proteins

Protein | Function[22][23][24][25]
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.[26] 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).[27] 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.[26]

SARS coronaviruses have been genetically engineered in several laboratories.[28]

## 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.[29][3]

SARSr‑CoV |

|  |

|  |

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Bat CoV BtKY72

|

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Bat CoV BM48-31

|

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|  |

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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 |

|  |

|  |

|  |

|  |

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-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.[20][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.[8] 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]

* COVID-19 portal
* Viruses portal

* Bat SARS-like coronavirus WIV1 (SL-CoV-WIV1)
* Bat SARS-like coronavirus RsSHC014
* Bat coronavirus RaTG13
* Civet SARS-CoV

## 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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65. ^ 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."1-23&rft.pub=Springer&rft.date=2015&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4369385#id-name=PMC&rft_id=info:pmid/25720466&rft_id=info:doi/10.1007/978-1-4939-2438-7_1&rft.isbn=978-1-4939-2438-7&rft.aulast=Fehr&rft.aufirst=AR&rft.au=Perlman,+S&rfr_id=info:sid/en.wikipedia.org:SARS-related+coronavirus" class="Z3988">
66. ^ 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 34127534.1025-1045&rft.date=2021-09&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8370740#id-name=PMC&rft_id=info:pmid/34127534&rft_id=info:doi/10.1261/rna.078661.120&rft.aulast=Rao&rft.aufirst=S&rft.au=Hoskins,+I&rft.au=Tonn,+T&rft.au=Garcia,+PD&rft.au=Ozadam,+H&rft.au=Sarinay+Cenik,+E&rft.au=Cenik,+C&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8370740&rfr_id=info:sid/en.wikipedia.org:SARS-related+coronavirus" class="Z3988">
67. ^ Masters PS (1 January 2006). "The molecular biology of coronaviruses". Advances in Virus Research. 66. Academic Press: 193–292\. doi:10.1016/S0065-3527(06)66005-3. ISBN 9780120398690. PMC 7112330. PMID 16877062. "See Figure 8."193-292&rft.date=2006-01-01&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7112330#id-name=PMC&rft_id=info:pmid/16877062&rft_id=info:doi/10.1016/S0065-3527(06)66005-3&rft.isbn=9780120398690&rft.aulast=Masters&rft.aufirst=PS&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7112330&rfr_id=info:sid/en.wikipedia.org:SARS-related+coronavirus" class="Z3988">
68. ^ 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"1-23&rft.pub=Springer&rft.date=2015&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4369385#id-name=PMC&rft_id=info:pmid/25720466&rft_id=info:doi/10.1007/978-1-4939-2438-7_1&rft.isbn=978-1-4939-2438-7&rft.aulast=Fehr&rft.aufirst=AR&rft.au=Perlman,+S&rfr_id=info:sid/en.wikipedia.org:SARS-related+coronavirus" class="Z3988">
69. ^ 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.
70. ^ 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)."7415-28&rft.date=2016-08&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4984655#id-name=PMC&rft_id=info:pmid/27279608&rft_id=info:doi/10.1128/JVI.00080-16&rft.aulast=Sexton&rft.aufirst=NR&rft.au=Smith,+EC&rft.au=Blanc,+H&rft.au=Vignuzzi,+M&rft.au=Peersen,+OB&rft.au=Denison,+MR&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4984655&rfr_id=info:sid/en.wikipedia.org:SARS-related+coronavirus" class="Z3988">
71. ^ 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"1-23&rft.pub=Springer&rft.date=2015&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4369385#id-name=PMC&rft_id=info:pmid/25720466&rft_id=info:doi/10.1007/978-1-4939-2438-7_1&rft.isbn=978-1-4939-2438-7&rft.aulast=Fehr&rft.aufirst=AR&rft.au=Perlman,+S&rfr_id=info:sid/en.wikipedia.org:SARS-related+coronavirus" class="Z3988">
72. ^ 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."1-23&rft.pub=Springer&rft.date=2015&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4369385#id-name=PMC&rft_id=info:pmid/25720466&rft_id=info:doi/10.1007/978-1-4939-2438-7_1&rft.isbn=978-1-4939-2438-7&rft.aulast=Fehr&rft.aufirst=AR&rft.au=Perlman,+S&rfr_id=info:sid/en.wikipedia.org:SARS-related+coronavirus" class="Z3988">
73. ^ 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
74. ^ 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
75. ^ 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 Release"1-23&rft.pub=Springer&rft.date=2015&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4369385#id-name=PMC&rft_id=info:pmid/25720466&rft_id=info:doi/10.1007/978-1-4939-2438-7_1&rft.isbn=978-1-4939-2438-7&rft.aulast=Fehr&rft.aufirst=AR&rft.au=Perlman,+S&rfr_id=info:sid/en.wikipedia.org:SARS-related+coronavirus" class="Z3988">

## 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 12711465.1319-25&rft.date=2003-04&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7112372#id-name=PMC&rft_id=info:pmid/12711465&rft_id=info:doi/10.1016/s0140-6736(03)13077-2&rft.aulast=Peiris&rft.aufirst=JS&rft.au=Lai,+ST&rft.au=Poon,+LL&rft.au=Guan,+Y&rft.au=Yam,+LY&rft.au=Lim,+W&rft.au=Nicholls,+J&rft.au=Yee,+WK&rft.au=Yan,+WW&rft.au=Cheung,+MT&rft.au=Cheng,+VC&rft.au=Chan,+KH&rft.au=Tsang,+DN&rft.au=Yung,+RW&rft.au=Ng,+TK&rft.au=Yuen,+KY&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7112372&rfr_id=info:sid/en.wikipedia.org:SARS-related+coronavirus" class="Z3988">
* 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 12730500.1394-9&rft.date=2003-05&rft_id=info:pmid/12730500&rft_id=info:doi/10.1126/science.1085952&rft_id=info:bibcode/2003Sci...300.1394R&rft.aulast=Rota&rft.aufirst=PA&rft.au=Oberste,+MS&rft.au=Monroe,+SS&rft.au=Nix,+WA&rft.au=Campagnoli,+R&rft.au=Icenogle,+JP&rft.au=Peñaranda,+S&rft.au=Bankamp,+B&rft.au=Maher,+K&rft.au=Chen,+MH&rft.au=Tong,+S&rft.au=Tamin,+A&rft.au=Lowe,+L&rft.au=Frace,+M&rft.au=DeRisi,+JL&rft.au=Chen,+Q&rft.au=Wang,+D&rft.au=Erdman,+DD&rft.au=Peret,+TC&rft.au=Burns,+C&rft.au=Ksiazek,+TG&rft.au=Rollin,+PE&rft.au=Sanchez,+A&rft.au=Liffick,+S&rft.au=Holloway,+B&rft.au=Limor,+J&rft.au=McCaustland,+K&rft.au=Olsen-Rasmussen,+M&rft.au=Fouchier,+R&rft.au=Günther,+S&rft.au=Osterhaus,+AD&rft.au=Drosten,+C&rft.au=Pallansch,+MA&rft.au=Anderson,+LJ&rft.au=Bellini,+WJ&rft_id=https://doi.org/10.1126%2Fscience.1085952&rfr_id=info:sid/en.wikipedia.org:SARS-related+coronavirus" class="Z3988">
* 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 12730501.1399-404&rft.date=2003-05&rft_id=info:pmid/12730501&rft_id=info:doi/10.1126/science.1085953&rft_id=info:bibcode/2003Sci...300.1399M&rft.aulast=Marra&rft.aufirst=MA&rft.au=Jones,+SJ&rft.au=Astell,+CR&rft.au=Holt,+RA&rft.au=Brooks-Wilson,+A&rft.au=Butterfield,+YS&rft.au=Khattra,+J&rft.au=Asano,+JK&rft.au=Barber,+SA&rft.au=Chan,+SY&rft.au=Cloutier,+A&rft.au=Coughlin,+SM&rft.au=Freeman,+D&rft.au=Girn,+N&rft.au=Griffith,+OL&rft.au=Leach,+SR&rft.au=Mayo,+M&rft.au=McDonald,+H&rft.au=Montgomery,+SB&rft.au=Pandoh,+PK&rft.au=Petrescu,+AS&rft.au=Robertson,+AG&rft.au=Schein,+JE&rft.au=Siddiqui,+A&rft.au=Smailus,+DE&rft.au=Stott,+JM&rft.au=Yang,+GS&rft.au=Plummer,+F&rft.au=Andonov,+A&rft.au=Artsob,+H&rft.au=Bastien,+N&rft.au=Bernard,+K&rft.au=Booth,+TF&rft.au=Bowness,+D&rft.au=Czub,+M&rft.au=Drebot,+M&rft.au=Fernando,+L&rft.au=Flick,+R&rft.au=Garbutt,+M&rft.au=Gray,+M&rft.au=Grolla,+A&rft.au=Jones,+S&rft.au=Feldmann,+H&rft.au=Meyers,+A&rft.au=Kabani,+A&rft.au=Li,+Y&rft.au=Normand,+S&rft.au=Stroher,+U&rft.au=Tipples,+GA&rft.au=Tyler,+S&rft.au=Vogrig,+R&rft.au=Ward,+D&rft.au=Watson,+B&rft.au=Brunham,+RC&rft.au=Krajden,+M&rft.au=Petric,+M&rft.au=Skowronski,+DM&rft.au=Upton,+C&rft.au=Roper,+RL&rft_id=https://doi.org/10.1126%2Fscience.1085953&rfr_id=info:sid/en.wikipedia.org:SARS-related+coronavirus" class="Z3988">
* 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 14974326.991-1004&rft.date=2003-08&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7159028#id-name=PMC&rft_id=https://api.semanticscholar.org/CorpusID:14974326#id-name=S2CID&rft_id=info:doi/10.1016/S0022-2836(03)00865-9&rft_id=https://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.319.7007#id-name=CiteSeerX&rft_id=info:pmid/12927536&rft.aulast=Snijder&rft.aufirst=EJ&rft.au=Bredenbeek,+PJ&rft.au=Dobbe,+JC&rft.au=Thiel,+V&rft.au=Ziebuhr,+J&rft.au=Poon,+LL&rft.au=Guan,+Y&rft.au=Rozanov,+M&rft.au=Spaan,+WJ&rft.au=Gorbalenya,+AE&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7159028&rfr_id=info:sid/en.wikipedia.org:SARS-related+coronavirus" class="Z3988">
* 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 16891412.12546-51&rft.date=2006-08&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1531645#id-name=PMC&rft_id=info:pmid/16891412&rft_id=info:doi/10.1073/pnas.0605438103&rft_id=info:bibcode/2006PNAS..10312546Y&rft.aulast=Yount&rft.aufirst=B&rft.au=Roberts,+RS&rft.au=Lindesmith,+L&rft.au=Baric,+RS&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1531645&rfr_id=info:sid/en.wikipedia.org:SARS-related+coronavirus" class="Z3988">
* 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 Betacoronavirus pandemicum at Wikimedia Commons
* 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)

* v
* t
* e

Taxonomy of the Coronaviridae

Higher taxonomy: Riboviria > Orthornavirae > Pisuviricota > Pisoniviricetes > Nidovirales > Cornidovirineae > Coronaviridae

Orthocoronavirinae

Alphacoronavirus|

| Colacovirus|

* Bat coronavirus CDPHE15

Decacovirus|

* Bat coronavirus HKU10
* Rhinolophus ferrumequinum alphacoronavirus HuB-2013

Duvinacovirus|

* Human coronavirus 229E

Luchacovirus|

* Lucheng Rn rat coronavirus

Minacovirus|

* Mink coronavirus 1

Minunacovirus|

* Miniopterus bat coronavirus 1
* Miniopterus bat coronavirus HKU8

Myotacovirus|

* Myotis ricketti alphacoronavirus Sax-2011

Nyctacovirus|

* Nyctalus velutinus alphacoronavirus SC-2013
* Pipistrellus kuhlii coronavirus 3398

Pedacovirus|

* Porcine epidemic diarrhea virus
* Scotophilus bat coronavirus 512

Rhinacovirus|

* Rhinolophus bat coronavirus HKU2

Setracovirus|

* Human coronavirus NL63
* NL63-related bat coronavirus strain BtKYNL63-9b

Soracovirus|

* Sorex araneus coronavirus T14

Sunacovirus|

* Suncus murinus coronavirus X74

Tegacovirus|

* Alphacoronavirus 1
* Feline coronavirus
* Canine coronavirus
* Canine coronavirus HuPn-2018
* Transmissible gastroenteritis virus

Betacoronavirus|

| Embecovirus|

* Betacoronavirus 1
* Bovine coronavirus
* Human coronavirus OC43
* China Rattus coronavirus HKU24
* Human coronavirus HKU1
* Murine coronavirus
* Rat coronavirus
* Myodes coronavirus 2JL14

Hibecovirus|

* Bat Hp-betacoronavirus Zhejiang2013

Merbecovirus|

* Hedgehog coronavirus 1
* Middle East respiratory syndrome-related coronavirus
* London1_novel CoV/2012
* MERS coronavirus EMC/2012
* Pipistrellus bat coronavirus HKU5
* Tylonycteris bat coronavirus HKU4

Nobecovirus|

* Eidolon bat coronavirus C704
* Rousettus bat coronavirus GCCDC1
* Rousettus bat coronavirus HKU9

Sarbecovirus|

* SARS-related coronavirus
* SARS-CoV-1
* SARS-CoV-2
* Variants
* BANAL-52
* Bat SARS-like coronavirus WIV1
* RacCS203
* RaTG13
* RmYN02
* RpYN06
* SHC014-CoV

Gammacoronavirus|

| Brangacovirus|

* Goose coronavirus CB17

Cegacovirus|

* Beluga whale coronavirus SW1

Igacovirus|

* Avian coronavirus
* Avian coronavirus 9203
* Duck coronavirus 2714

Deltacoronavirus|

| Andecovirus|

* Wigeon coronavirus HKU20

Buldecovirus|

* Bulbul coronavirus HKU11
* Common moorhen coronavirus HKU21
* Coronavirus HKU15
* Munia coronavirus HKU13
* White-eye coronavirus HKU16

Herdecovirus|

* Night heron coronavirus HKU19

Letovirinae

| Alphaletovirus|

| Milecovirus|

* Microhyla letovirus 1

Source: ICTV ––  Wikispecies

* v
* t
* e

Severe acute respiratory syndrome (SARS)

* SARS-CoV-1
* SARSr-CoV

General topics|

* 2002–2004 SARS outbreak
* Outbreak among healthcare workers
* List of medical professionals who died
* Air China Flight 112
* SARS conspiracy theory

People|

* Zhong Nanshan
* Ab Osterhaus
* Joanna Tse
* Carlo Urbani
* Jiang Yanyong

In popular culture|

* Plague City: SARS in Toronto
* Molson Canadian Rocks for Toronto
* 1:99 Concert
* Contagion
* SARS Wars

Related articles|

* Coronavirus
* Global alert
* Health in China
* MERS
* MERS-CoV
* COVID-19
* SARS-CoV-2
* pandemic

* v
* t
* e

Infectious diseases – viral systemic diseases

Oncovirus|

DNA virus
HBV

Hepatocellular carcinoma
HPV

Cervical cancer
Anal cancer
Penile cancer
Vulvar cancer
Vaginal cancer
Oropharyngeal cancer
KSHV

Kaposi's sarcoma
EBV

Nasopharyngeal carcinoma
Burkitt's lymphoma
Hodgkin lymphoma
Follicular dendritic cell sarcoma
Extranodal NK/T-cell lymphoma, nasal type
MCPyV

Merkel-cell carcinoma

RNA virus
HCV

Hepatocellular carcinoma
Splenic marginal zone lymphoma
HTLV-I

Adult T-cell leukemia/lymphoma

Immune disorders|

* HIV
* AIDS

Central
nervous system|

| Encephalitis/
meningitis|

DNA virus
Human polyomavirus 2

Progressive multifocal leukoencephalopathy

RNA virus
MeV

Subacute sclerosing panencephalitis
LCV

Lymphocytic choriomeningitis
Arbovirus encephalitis
Orthomyxoviridae (probable)

Encephalitis lethargica

Rabies
Chandipura vesiculovirus
Herpesviral meningitis
Ramsay Hunt syndrome type 2

|

Myelitis|

* Poliovirus
* Poliomyelitis
* Post-polio syndrome
* HTLV-I
* Tropical spastic paraparesis

Eye|

* Cytomegalovirus
* Cytomegalovirus retinitis
* HSV
* Herpes of the eye

Cardiovascular|

* CBV
* Pericarditis
* Myocarditis

Respiratory system/
acute viral
nasopharyngitis/
viral pneumonia|

| DNA virus|

* Epstein–Barr virus
* EBV infection/Infectious mononucleosis
* Cytomegalovirus

|

RNA virus|

* IV: Human coronavirus 229E/NL63/HKU1/OC43
* Common cold
* MERS coronavirus
* Middle East respiratory syndrome
* SARS coronavirus
* Severe acute respiratory syndrome
* SARS-CoV-2
* COVID-19

* V, Orthomyxoviridae: Influenza virus A/B/C/D
* Influenza/Avian influenza

* V, Paramyxoviridae: Human parainfluenza viruses
* Parainfluenza
* Human orthopneumovirus
* hMPV

Human
digestive system|

| Pharynx/Esophagus|

* MuV
* Mumps
* Cytomegalovirus
* Cytomegalovirus esophagitis

|

Gastroenteritis/
diarrhea|

DNA virus
Adenovirus

Adenovirus infection

RNA virus
Rotavirus (Gastroenteritis)
Norovirus
Astrovirus
Coronavirus

Hepatitis|

DNA virus
HBV (B)

RNA virus
CBV
HAV (A)
HCV (C)
HDV (D)
HEV (E)

Pancreatitis|

* CBV

Urogenital|

* BK virus
* MuV
* Mumps

* v
* t
* e

Zoonotic viral diseases (A80–B34, 042–079)

Arthropod
-borne|

| Mosquito
-borne|

| Bunyavirales|

* Arbovirus encephalitides: Batai virus
* BATV
* Bwamba Fever
* BWAV
* California encephalitis
* CEV
* Jamestown Canyon encephalitis
* La Crosse encephalitis
* LACV
* Tahyna virus
* TAHV
* Tete virus

* Viral hemorrhagic fevers: Bunyamwera fever
* BUNV
* Ngari virus
* NRIV
* Rift Valley fever
* RVFV

|

Flaviviridae|

* Arbovirus encephalitides: Japanese encephalitis
* JEV
* Australian encephalitis
* MVEV
* KUNV
* Saint Louis encephalitis
* SLEV
* Usutu virus
* USUV
* West Nile fever
* WNV

* Viral hemorrhagic fevers: Dengue fever
* DENV-1-4
* Yellow fever
* YFV
* Zika fever
* ZIKV

Togaviridae|

* Arbovirus encephalitides: Eastern equine encephalomyelitis
* EEEV
* Western equine encephalomyelitis
* WEEV
* Venezuelan equine encephalomyelitis
* VEEV
* Chikungunya
* CHIKV
* O'nyong'nyong fever
* ONNV
* Pogosta disease
* Sindbis virus
* Ross River fever
* RRV
* Semliki Forest virus

Reoviridae|

* Banna virus encephalitis

Tick
-borne|

| Bunyavirales|

* Viral hemorrhagic fevers: Crimean–Congo hemorrhagic fever (CCHFV)
* Heartland virus
* Severe fever with thrombocytopenia syndrome (Huaiyangshan banyangvirus)
* Tete virus
* Arbovirus encephalitides: Bhanja virus

|

Flaviviridae|

* Arbovirus encephalitides: Tick-borne encephalitis
* TBEV
* Powassan encephalitis
* POWV
* Viral hemorrhagic fevers: Omsk hemorrhagic fever
* OHFV
* Kyasanur Forest disease
* KFDV
* AHFV
* Langat virus
* LGTV

Orthomyxoviridae|

* Bourbon virus

Reoviridae|

* Colorado tick fever
* CTFV
* Kemerovo tickborne viral fever

Sandfly
-borne|

| Bunyavirales|

* Adria virus (ADRV)
* Oropouche fever
* Oropouche virus
* Pappataci fever
* Toscana virus
* Sandfly fever Naples virus

|

Rhabdoviridae|

* Chandipura virus

Mammal
-borne|

| Rodent
-borne|

| Arenaviridae|

* Viral hemorrhagic fevers: Lassa fever
* LASV
* Venezuelan hemorrhagic fever
* GTOV
* Argentine hemorrhagic fever
* JUNV
* Brazilian hemorrhagic fever
* SABV
* Bolivian hemorrhagic fever
* MACV
* LUJV
* CHPV

|

Bunyavirales|

* Hemorrhagic fever with renal syndrome
* DOBV
* HTNV
* PUUV
* SEOV
* AMRV
* THAIV
* Hantavirus pulmonary syndrome
* ANDV
* SNV

Herpesviridae|

* Murid gammaherpesvirus 4

Bat
-borne|

| Filoviridae|

* Ebola virus disease
* BDBV
* SUDV
* TAFV
* ZEBOV
* Marburg virus disease
* MARV
* RAVV

|

Rhabdoviridae|

* Rabies
* ABLV
* MOKV
* DUVV
* LBV
* CHPV

Paramyxoviridae|

* Henipavirus encephalitis
* HeV
* NiV

Coronaviridae|

* MERS-CoV
* SARS-related coronavirus
* SARS-CoV
* SARS-CoV-2

Primate
-borne|

| Herpesviridae|

* B virus

|

Retroviridae|

* Simian foamy virus
* HTLV-1
* HTLV-2

Poxviridae|

* Tanapox
* Yaba monkey tumor virus

Multiple
vectors|

| Rhabdoviridae|

* Rabies
* RABV
* Mokola virus

|

Poxviridae|

* Monkeypox

Taxon identifiers

Severe acute respiratory syndrome-related coronavirus|

* Wikidata: Q278567
* Wikispecies: Betacoronavirus pandemicum
* CoL: 4X3K4
* EoL: 11621416
* GBIF: 10069196
* IRMNG: 11460764
* NCBI: 227859

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