Type |
Details |
Score |
Allele |
Name: |
host response to SARS QTL 8, log titer; WSB/EiJ |
Allele Type: |
QTL |
|
|
•
•
•
•
•
|
Allele |
Name: |
host response to SARS QTL 8, log titer; NOD/ShiLtJ |
Allele Type: |
QTL |
|
|
•
•
•
•
•
|
Allele |
Name: |
host response to SARS QTL 4, vascular cuffing; CAST/EiJ |
Allele Type: |
QTL |
|
|
•
•
•
•
•
|
Publication |
First Author: |
Law PY |
Year: |
2006 |
Journal: |
FEBS Lett |
Title: |
Expression and functional characterization of the putative protein 8b of the severe acute respiratory syndrome-associated coronavirus. |
Volume: |
580 |
Issue: |
15 |
Pages: |
3643-8 |
|
•
•
•
•
•
|
Publication |
First Author: |
Keng CT |
Year: |
2006 |
Journal: |
Virology |
Title: |
The human severe acute respiratory syndrome coronavirus (SARS-CoV) 8b protein is distinct from its counterpart in animal SARS-CoV and down-regulates the expression of the envelope protein in infected cells. |
Volume: |
354 |
Issue: |
1 |
Pages: |
132-42 |
|
•
•
•
•
•
|
Publication |
First Author: |
Pereira F |
Year: |
2020 |
Journal: |
Infect Genet Evol |
Title: |
Evolutionary dynamics of the SARS-CoV-2 ORF8 accessory gene. |
Volume: |
85 |
|
Pages: |
104525 |
|
•
•
•
•
•
|
Publication |
First Author: |
Mohammad S |
Year: |
2020 |
Journal: |
Pathogens |
Title: |
SARS-CoV-2 ORF8 and SARS-CoV ORF8ab: Genomic Divergence and Functional Convergence. |
Volume: |
9 |
Issue: |
9 |
|
|
•
•
•
•
•
|
Publication |
First Author: |
Chan JF |
Year: |
2020 |
Journal: |
Lancet |
Title: |
A familial cluster of pneumonia associated with the 2019 novel coronavirus indicating person-to-person transmission: a study of a family cluster. |
Volume: |
395 |
Issue: |
10223 |
Pages: |
514-523 |
|
•
•
•
•
•
|
Publication |
First Author: |
Zhang Y |
Year: |
2021 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
The ORF8 protein of SARS-CoV-2 mediates immune evasion through down-regulating MHC-Ι. |
Volume: |
118 |
Issue: |
23 |
|
|
•
•
•
•
•
|
Publication |
First Author: |
Geng H |
Year: |
2021 |
Journal: |
Front Immunol |
Title: |
SARS-CoV-2 ORF8 Forms Intracellular Aggregates and Inhibits IFNγ-Induced Antiviral Gene Expression in Human Lung Epithelial Cells. |
Volume: |
12 |
|
Pages: |
679482 |
|
•
•
•
•
•
|
Publication |
First Author: |
Qiu M |
Year: |
2005 |
Journal: |
Microbes Infect |
Title: |
Antibody responses to individual proteins of SARS coronavirus and their neutralization activities. |
Volume: |
7 |
Issue: |
5-6 |
Pages: |
882-9 |
|
•
•
•
•
•
|
Publication |
First Author: |
Moshynskyy I |
Year: |
2007 |
Journal: |
Virus Res |
Title: |
Intracellular localization of the SARS coronavirus protein 9b: evidence of active export from the nucleus. |
Volume: |
127 |
Issue: |
1 |
Pages: |
116-21 |
|
•
•
•
•
•
|
Publication |
First Author: |
von Grotthuss M |
Year: |
2003 |
Journal: |
Cell |
Title: |
mRNA cap-1 methyltransferase in the SARS genome. |
Volume: |
113 |
Issue: |
6 |
Pages: |
701-2 |
|
•
•
•
•
•
|
Publication |
First Author: |
Meier C |
Year: |
2006 |
Journal: |
Structure |
Title: |
The crystal structure of ORF-9b, a lipid binding protein from the SARS coronavirus. |
Volume: |
14 |
Issue: |
7 |
Pages: |
1157-65 |
|
•
•
•
•
•
|
Publication |
First Author: |
Gralinski LE |
Year: |
2015 |
Journal: |
PLoS Genet |
Title: |
Genome Wide Identification of SARS-CoV Susceptibility Loci Using the Collaborative Cross. |
Volume: |
11 |
Issue: |
10 |
Pages: |
e1005504 |
|
•
•
•
•
•
|
Publication |
First Author: |
Liu SJ |
Year: |
2006 |
Journal: |
Vaccine |
Title: |
Immunological characterizations of the nucleocapsid protein based SARS vaccine candidates. |
Volume: |
24 |
Issue: |
16 |
Pages: |
3100-8 |
|
•
•
•
•
•
|
Publication |
First Author: |
Wu F |
Year: |
2020 |
Journal: |
Nature |
Title: |
A new coronavirus associated with human respiratory disease in China. |
Volume: |
579 |
Issue: |
7798 |
Pages: |
265-269 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
512
|
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Tan J |
Year: |
2009 |
Journal: |
PLoS Pathog |
Title: |
The SARS-unique domain (SUD) of SARS coronavirus contains two macrodomains that bind G-quadruplexes. |
Volume: |
5 |
Issue: |
5 |
Pages: |
e1000428 |
|
•
•
•
•
•
|
Publication |
First Author: |
Orduz D |
Year: |
2015 |
Journal: |
Elife |
Title: |
Interneurons and oligodendrocyte progenitors form a structured synaptic network in the developing neocortex. |
Volume: |
4 |
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Imbert I |
Year: |
2006 |
Journal: |
EMBO J |
Title: |
A second, non-canonical RNA-dependent RNA polymerase in SARS coronavirus. |
Volume: |
25 |
Issue: |
20 |
Pages: |
4933-42 |
|
•
•
•
•
•
|
Publication |
First Author: |
Luo H |
Year: |
2005 |
Journal: |
Biochemistry |
Title: |
SR-rich motif plays a pivotal role in recombinant SARS coronavirus nucleocapsid protein multimerization. |
Volume: |
44 |
Issue: |
46 |
Pages: |
15351-8 |
|
•
•
•
•
•
|
Publication |
First Author: |
Johnson MA |
Year: |
2010 |
Journal: |
J Mol Biol |
Title: |
SARS coronavirus unique domain: three-domain molecular architecture in solution and RNA binding. |
Volume: |
400 |
Issue: |
4 |
Pages: |
724-42 |
|
•
•
•
•
•
|
Publication |
First Author: |
Lin X |
Year: |
2021 |
Journal: |
iScience |
Title: |
ORF8 contributes to cytokine storm during SARS-CoV-2 infection by activating IL-17 pathway. |
Volume: |
24 |
Issue: |
4 |
Pages: |
102293 |
|
•
•
•
•
•
|
Publication |
First Author: |
Li W |
Year: |
2003 |
Journal: |
Nature |
Title: |
Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus. |
Volume: |
426 |
Issue: |
6965 |
Pages: |
450-4 |
|
•
•
•
•
•
|
Publication |
First Author: |
Wong SK |
Year: |
2004 |
Journal: |
J Biol Chem |
Title: |
A 193-amino acid fragment of the SARS coronavirus S protein efficiently binds angiotensin-converting enzyme 2. |
Volume: |
279 |
Issue: |
5 |
Pages: |
3197-201 |
|
•
•
•
•
•
|
Publication |
First Author: |
Belouzard S |
Year: |
2009 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites. |
Volume: |
106 |
Issue: |
14 |
Pages: |
5871-6 |
|
•
•
•
•
•
|
Publication |
First Author: |
Teoh KT |
Year: |
2010 |
Journal: |
Mol Biol Cell |
Title: |
The SARS coronavirus E protein interacts with PALS1 and alters tight junction formation and epithelial morphogenesis. |
Volume: |
21 |
Issue: |
22 |
Pages: |
3838-52 |
|
•
•
•
•
•
|
Publication |
First Author: |
Surya W |
Year: |
2018 |
Journal: |
Biochim Biophys Acta Biomembr |
Title: |
Structural model of the SARS coronavirus E channel in LMPG micelles. |
Volume: |
1860 |
Issue: |
6 |
Pages: |
1309-1317 |
|
•
•
•
•
•
|
Publication |
First Author: |
Ma Y |
Year: |
2015 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Structural basis and functional analysis of the SARS coronavirus nsp14-nsp10 complex. |
Volume: |
112 |
Issue: |
30 |
Pages: |
9436-41 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kamitani W |
Year: |
2009 |
Journal: |
Nat Struct Mol Biol |
Title: |
A two-pronged strategy to suppress host protein synthesis by SARS coronavirus Nsp1 protein. |
Volume: |
16 |
Issue: |
11 |
Pages: |
1134-40 |
|
•
•
•
•
•
|
Publication |
First Author: |
Sakai Y |
Year: |
2017 |
Journal: |
Virology |
Title: |
Two-amino acids change in the nsp4 of SARS coronavirus abolishes viral replication. |
Volume: |
510 |
|
Pages: |
165-174 |
|
•
•
•
•
•
|
Publication |
First Author: |
Guarino LA |
Year: |
2005 |
Journal: |
J Mol Biol |
Title: |
Mutational analysis of the SARS virus Nsp15 endoribonuclease: identification of residues affecting hexamer formation. |
Volume: |
353 |
Issue: |
5 |
Pages: |
1106-17 |
|
•
•
•
•
•
|
Publication |
First Author: |
Song W |
Year: |
2018 |
Journal: |
PLoS Pathog |
Title: |
Cryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2. |
Volume: |
14 |
Issue: |
8 |
Pages: |
e1007236 |
|
•
•
•
•
•
|
Publication |
First Author: |
Graham RL |
Year: |
2006 |
Journal: |
Adv Exp Med Biol |
Title: |
The nsp2 proteins of mouse hepatitis virus and SARS coronavirus are dispensable for viral replication. |
Volume: |
581 |
|
Pages: |
67-72 |
|
•
•
•
•
•
|
Allele |
Name: |
angiotensin converting enzyme 2; endonuclease-mediated mutation 1, Maria Cecilia C Canesso |
Allele Type: |
Endonuclease-mediated |
Attribute String: |
Humanized sequence |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Publication |
First Author: |
Akerström S |
Year: |
2007 |
Journal: |
Antiviral Res |
Title: |
Inhibition of SARS-CoV replication cycle by small interference RNAs silencing specific SARS proteins, 7a/7b, 3a/3b and S. |
Volume: |
73 |
Issue: |
3 |
Pages: |
219-27 |
|
•
•
•
•
•
|
Publication |
First Author: |
Huang C |
Year: |
2011 |
Journal: |
PLoS Pathog |
Title: |
SARS coronavirus nsp1 protein induces template-dependent endonucleolytic cleavage of mRNAs: viral mRNAs are resistant to nsp1-induced RNA cleavage. |
Volume: |
7 |
Issue: |
12 |
Pages: |
e1002433 |
|
•
•
•
•
•
|
Publication |
First Author: |
Minakshi R |
Year: |
2009 |
Journal: |
PLoS One |
Title: |
The SARS Coronavirus 3a protein causes endoplasmic reticulum stress and induces ligand-independent downregulation of the type 1 interferon receptor. |
Volume: |
4 |
Issue: |
12 |
Pages: |
e8342 |
|
•
•
•
•
•
|
Publication |
First Author: |
Gralinski LE |
Year: |
2017 |
Journal: |
G3 (Bethesda) |
Title: |
Allelic Variation in the Toll-Like Receptor Adaptor Protein Ticam2 Contributes to SARS-Coronavirus Pathogenesis in Mice. |
Volume: |
7 |
Issue: |
6 |
Pages: |
1653-1663 |
|
•
•
•
•
•
|
Publication |
First Author: |
Marra MA |
Year: |
2003 |
Journal: |
Science |
Title: |
The Genome sequence of the SARS-associated coronavirus. |
Volume: |
300 |
Issue: |
5624 |
Pages: |
1399-404 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
This is a family of unknown function found in SARS and SARS-like coronaviruses. It includes uncharacterised protein 14 from SARS coronavirus 2 (SARS-CoV-2), Human SARS coronavirus (SARS-CoV) and Bat coronavirus Rp3/2004 (SARS-like coronavirus Rp3) []. In SARS-CoV, Orf14 is completely contained within the ORF encoding the nucleocapsid protein (N) []. In SARS-CoV-2 uncharacterised protein 14 is predicted to contain one transmembrane helix. |
|
•
•
•
•
•
|
Publication |
First Author: |
Hänel K |
Year: |
2006 |
Journal: |
J Biomed Sci |
Title: |
Solution structure of the X4 protein coded by the SARS related coronavirus reveals an immunoglobulin like fold and suggests a binding activity to integrin I domains. |
Volume: |
13 |
Issue: |
3 |
Pages: |
281-93 |
|
•
•
•
•
•
|
Allele |
Name: |
transgene insertion AC70, Chien-Te K Tseng |
Allele Type: |
Transgenic |
Attribute String: |
Humanized sequence, Inserted expressed sequence |
|
•
•
•
•
•
|
Allele |
Name: |
signal transducer and activator of transcription 1; targeted mutation 1, Robert D Schreiber |
Allele Type: |
Targeted |
Attribute String: |
Null/knockout |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
human |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Transgene |
Type: |
transgene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Allele |
Name: |
transgene insertion 2, Stanley Perlman |
Allele Type: |
Transgenic |
Attribute String: |
Humanized sequence, Inserted expressed sequence |
|
•
•
•
•
•
|
Transgene |
Type: |
transgene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Allele |
Name: |
transgene insertion 1, Ralph Baric |
Allele Type: |
Transgenic |
Attribute String: |
Inserted expressed sequence |
|
•
•
•
•
•
|
Allele |
Name: |
transgene insertion 1, Chuan Qin |
Allele Type: |
Transgenic |
Attribute String: |
Humanized sequence, Inserted expressed sequence |
|
•
•
•
•
•
|
Transgene |
Type: |
transgene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Genotype |
Symbol: |
Stat1/Stat1 |
Background: |
129S6/SvEv-Stat1/Tac |
Zygosity: |
hm |
Has Mutant Allele: |
true |
|
•
•
•
•
•
|
Genotype |
Symbol: |
Tg(CAG-ACE2)AC70Ctkt/? |
Background: |
either: (involves: BALB/c * C3H/HeJ * C57BL/6J) or (involves: C3H/HeJ * C57BL/6 * C57BL/6J) |
Zygosity: |
ot |
Has Mutant Allele: |
true |
|
•
•
•
•
•
|
Genotype |
Symbol: |
Tg(Ace2-ACE2)1Cqin/? |
Background: |
involves: ICR |
Zygosity: |
ot |
Has Mutant Allele: |
true |
|
•
•
•
•
•
|
Genotype |
Symbol: |
Tg(K18-ACE2)2Prlmn/? |
Background: |
involves: C57BL/6J * SJL/J |
Zygosity: |
ot |
Has Mutant Allele: |
true |
|
•
•
•
•
•
|
Genotype |
|
Background: |
CC053/Unc |
Zygosity: |
ot |
Has Mutant Allele: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Xu K |
Year: |
2009 |
Journal: |
Virology |
Title: |
Severe acute respiratory syndrome coronavirus accessory protein 9b is a virion-associated protein. |
Volume: |
388 |
Issue: |
2 |
Pages: |
279-85 |
|
•
•
•
•
•
|
Publication |
First Author: |
Sharma K |
Year: |
2011 |
Journal: |
PLoS One |
Title: |
SARS-CoV 9b protein diffuses into nucleus, undergoes active Crm1 mediated nucleocytoplasmic export and triggers apoptosis when retained in the nucleus. |
Volume: |
6 |
Issue: |
5 |
Pages: |
e19436 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
This is a family of proteins found in SARS and SARS-like coronaviruses. It includes Protein 9b from SARS coronavirus 2 (SARS-CoV-2), Human SARS coronavirus (SARS-CoV) and Bat coronaviruses.Protein 9b is one of 8 accessory proteins in SARS-CoV []. The gene (ORF 9b, also known as ORF13) that encodes this protein is included within the nucleocapsid (N) gene (alternative ORF) []. Data suggest that protein 9b is a structural component of SARS-CoV virions and functions as an unusual lipid binding protein [, ].SARS-CoV ORF-9b has been shown to localise to the outer mitochondrial membrane and to target mitochondrial antiviral signalling proteins (MAVS), suppressing innate immunity [, , ]. Antibodies against SARS-CoV ORF-9b have been found in patients, demonstrating that it is produced during infection [, ].Protein 9b from SARS CoV comprises 98 amino acids. Its structure has a novel fold which forms a dimeric tent-like beta structure with an amphipathic surface, and a central hydrophobic cavity that binds lipidmolecules []. This cavity is likely to be involved in membrane attachment [].Protein 9b is a group-specific protein of SARS coronavirus (CoV). The sequence of ORF-9b is well conserved in different SARS isolates, however, there is little homology between Protein 9b from SARS-CoV and the I protein (Protein 9b homologue) present in other coronaviruses [, , ]. |
|
•
•
•
•
•
|
Publication |
First Author: |
Hammond RG |
Year: |
2017 |
Journal: |
Protein Sci |
Title: |
SARS-unique fold in the Rousettus bat coronavirus HKU9. |
Volume: |
26 |
Issue: |
9 |
Pages: |
1726-1737 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
This entry represents the SUD-C domain of Rousettus bat coronavirus (CoV) HKU9 non-structural protein 3 (NSP3) and other NSP3s from betacoronaviruses in the nobecovirus subgenera (D lineage).NSP3 of SARS coronavirus includes a SARS-unique domain (SUD) consisting of three globular domains separated by short linker peptide segments: SUD-N, SUD-M, and SUD-C. SUD-N and SUD-M are macro domains which bind G-quadruplexes (unusual nucleic-acid structures formed by consecutive guanosine nucleotides) []. SUD is not as specific to SARS CoV as originally thought and is also found in Rousettus bat CoV HKU9 and related bat CoVs []. Similar to SARS SUD-C, Rousettus bat CoV HKU9 SUD-C (HKU9 C), also adopts a frataxin-like fold that has structural similarity to DNA-binding domains of DNA-modifying enzymes. However, there is little sequence similarity between the two domains. SARS SUD-C has been shown to bind to single-stranded RNA and recognize purine bases more strongly than pyrimidine bases; it also regulates the RNA binding behavior of the SARS SUD-M macrodomain. It is not known whether HKU9 C functions in the same way []. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
This entry represents the SUD-C of Middle East respiratory syndrome-related (MERS) coronavirus (CoV) NSP3 and other NSP3s from betacoronaviruses in the merbecovirus subgenera (C lineage), including several bat-CoVs such as Tylonycteris bat CoV HKU4, Pipistrellus bat CoV HKU5, and Hypsugo bat CoV HKU25.NSP3 of SARS coronavirus includes a SARS-unique domain (SUD) consisting of three globular domains separated by short linker peptide segments: SUD-N, SUD-M, and SUD-C. SUD-N and SUD-M are macro domains which bind G-quadruplexes (unusual nucleic-acid structures formed by consecutive guanosine nucleotides) []. SUD is not as specific to SARS CoV as originally thought and is also found in MERS and related bat coronaviruses. Similar to SARS SUD-C, Tylonycteris bat-CoV HKU4 SUD-C (HKU4 C), a member of the MERS SUD-C group, also adopts a frataxin-like fold that has structural similarity to DNA-binding domains of DNA-modifying enzymes. However, there is little sequence similarity between the two domains. SARS SUD-C has been shown to bind to single-stranded RNA and recognise purine bases more strongly than pyrimidine bases; it also regulates the RNA binding behaviour of the SARS SUD-M macrodomain. It is not known whether MERS SUD-C or HKU4 C functions in the same way [, ]. |
|
•
•
•
•
•
|
Transgene |
Type: |
transgene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Genotype |
Symbol: |
Tg(FOXJ1-ACE2)1Rba/? |
Background: |
involves: C3H * C57BL/6 |
Zygosity: |
ot |
Has Mutant Allele: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Deng L |
Year: |
2018 |
Journal: |
Viruses |
Title: |
Suppression of NF-κB Activity: A Viral Immune Evasion Mechanism. |
Volume: |
10 |
Issue: |
8 |
|
|
•
•
•
•
•
|
Publication |
First Author: |
Zhang L |
Year: |
2018 |
Journal: |
Autophagy |
Title: |
Viral strategies for triggering and manipulating mitophagy. |
Volume: |
14 |
Issue: |
10 |
Pages: |
1665-1673 |
|
•
•
•
•
•
|
Publication |
First Author: |
Shi CS |
Year: |
2014 |
Journal: |
J Immunol |
Title: |
SARS-coronavirus open reading frame-9b suppresses innate immunity by targeting mitochondria and the MAVS/TRAF3/TRAF6 signalosome. |
Volume: |
193 |
Issue: |
6 |
Pages: |
3080-9 |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
human |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Homologous_superfamily |
Description: |
This superfamily represents a domain found in SARS and bat coronaviruses, which is about 70 amino acids in length. PL2pro is a domain of the non-structural protein NSP3, found associated with various other coronavirus proteins due to the polyprotein nature of most viral translation. The domain performs three of the cleavages required to separate the translated polyprotein into its distinct proteins []. Structurally, this domain consists of two α-helices and seven β-strands arranged into an antiparallel β-sheet. |
|
•
•
•
•
•
|
Publication |
First Author: |
Chen Y |
Year: |
2015 |
Journal: |
J Biol Chem |
Title: |
X-ray Structural and Functional Studies of the Three Tandemly Linked Domains of Non-structural Protein 3 (nsp3) from Murine Hepatitis Virus Reveal Conserved Functions. |
Volume: |
290 |
Issue: |
42 |
Pages: |
25293-306 |
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•
•
•
•
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Protein Domain |
Type: |
Domain |
Description: |
MHV NSP3 contains a DPUP that is located N-terminal to the ubiquitin-like domain 2 (Ubl2) and papain-like protease 2 (PLP2) catalytic domain. It is structurally similar to the Severe Acute Respiratory Syndrome (SARS) CoV unique domain C (SUD-C), adopting a frataxin-like fold that has structural similarity to DNA-binding domains of DNA-modifying enzymes. SUD-C is also located N-terminal to Ubl2 and PLP2 in SARS NSP3, similar to the DPUP of MHV NSP3; however, unlike DPUP, it is preceded by SUD-N and SUD-M macrodomains that are absent in MHV NSP3. Though structurally similar, there is little sequence similarity between DPUP and SUD-C. SARS SUD-C has been shown to bind to single-stranded RNA and recognize purine bases more strongly than pyrimidine bases; it also regulates the RNA binding behavior of the SARS SUD-M macrodomain. It is not known whether DPUP functions in the same way [].This entry represents the DPUP (domain preceding Ubl2 and PLP2) of murine hepatitis virus (MHV) non-structural protein 3 (NSP3) and other NSP3s from betacoronaviruses in the embecovirus subgenera (A lineage), including human CoV OC43, rabbit CoV HKU14 and porcine hemagglutinating encephalomyelitis virus (HEV), among others. |
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Publication |
First Author: |
Neuman BW |
Year: |
2008 |
Journal: |
J Virol |
Title: |
Proteomics analysis unravels the functional repertoire of coronavirus nonstructural protein 3. |
Volume: |
82 |
Issue: |
11 |
Pages: |
5279-94 |
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•
•
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•
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Publication |
First Author: |
Mann BJ |
Year: |
2022 |
Journal: |
bioRxiv |
Title: |
Adenosine A2A receptor (A2AR) agonists improve survival in K28-hACE2 mice following SARS-CoV-2 infection. |
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Publication |
First Author: |
Roberts A |
Year: |
2005 |
Journal: |
J Virol |
Title: |
Aged BALB/c mice as a model for increased severity of severe acute respiratory syndrome in elderly humans. |
Volume: |
79 |
Issue: |
9 |
Pages: |
5833-8 |
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•
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•
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Publication |
First Author: |
Hogan RJ |
Year: |
2004 |
Journal: |
J Virol |
Title: |
Resolution of primary severe acute respiratory syndrome-associated coronavirus infection requires Stat1. |
Volume: |
78 |
Issue: |
20 |
Pages: |
11416-21 |
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Protein Domain |
Type: |
Family |
Description: |
This entry includes the ORF8 gene products (also known as NS8, accessory protein 8) from human SARS coronavirus (SARS-CoV), SARS-CoV-2, Bat coronavirus HKU3 and pangolin coronaviruses [].ORF8 is an accessory protein that is not shared by all members of subgenus sarbecovirus. The presence and location of ORF8 in the SARS-CoV-2 genome has led its classification with SARS-CoV [, ]. ORF8 is a potential pathogenicity factor which evolves rapidly to counter the immune response and facilitate the transmission between hosts []. ORF8 has been suggested to be one of the relevant genes in the study of human adaptation of the virus [, ].The ORF8 protein is a fast-evolving protein in SARS-related CoVs, with a tendency to recombine and undergo deletions. During the early phases of the SARS (SARS-CoV) epidemic in 2002, human isolates were found to possess a unique continuous ORF8 with 366 nucleotides and a predicted protein with 122 amino acids. During the middle and late phases of the SARS epidemic, two functional ORFs (ORF8a and ORF8b) were emerged; they are predicted to encode two small proteins, 8a with 39 amino acids and 8b with 84 amino acids. Interestingly, SARS-CoV-2 ORF8 has not undergone any significantly measurable deletion events, so its function as a full-length protein might be more important to its pathogenicity []. ORF8 plays a role in modulating host immune response []which may act by down-regulating major histocompatibility complex class I (MHC-I) []. It may inhibit expression of some members of the IFN-stimulated gene (ISG) family including hosts IGF2BP1/ZBP1, MX1 and MX2, and DHX58 []. ORF8 also binds to IL17RA receptor, leading to IL17 pathway activation and an increased secretion of pro-inflammatory factors, contributing to cytokine storm during COVID-19 infection []. |
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Protein Domain |
Type: |
Family |
Description: |
This subfamily includes the ORF8 immunoglobulin (Ig) domain proteins of bat coronavirus Rf1 (Bat SARS CoV Rf1) and Bat CoV 273/2005, which have been classified previously as type II ORF8 proteins.ORF8 is an accessory protein that is not shared by all members of subgenus sarbecovirus. The presence and location of ORF8 in the SARS-CoV-2 genome has led its classification with SARS-CoV [, ]. ORF8 is a potential pathogenicity factor which evolves rapidly to counter the immune response and facilitate the transmission between hosts []. ORF8 has been suggested to be one of the relevant genes in the study of human adaptation of the virus [, ].The ORF8 protein is a fast-evolving protein in SARS-related CoVs, with a tendency to recombine and undergo deletions. During the early phases of the SARS (SARS-CoV) epidemic in 2002, human isolates were found to possess a unique continuous ORF8 with 366 nucleotides and a predicted protein with 122 amino acids. During the middle and late phases of the SARS epidemic, two functional ORFs (ORF8a and ORF8b) were emerged; they are predicted to encode two small proteins, 8a with 39 amino acids and 8b with 84 amino acids. Interestingly, SARS-CoV-2 ORF8 has not undergone any significantly measurable deletion events, so its function as a full-length protein might be more important to its pathogenicity []. ORF8 plays a role in modulating host immune response []which may act by down-regulating major histocompatibility complex class I (MHC-I) []. It may inhibit expression of some members of the IFN-stimulated gene (ISG) family including hosts IGF2BP1/ZBP1, MX1 and MX2, and DHX58 []. ORF8 also binds to IL17RA receptor, leading to IL17 pathway activation and an increased secretion of pro-inflammatory factors, contributing to cytokine storm during COVID-19 infection []. |
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Publication |
First Author: |
Nakandakari-Higa S |
Year: |
2022 |
Journal: |
Front Immunol |
Title: |
A minimally-edited mouse model for infection with multiple SARS-CoV-2 strains. |
Volume: |
13 |
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Pages: |
1007080 |
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•
•
•
•
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Publication |
First Author: |
Imai Y |
Year: |
2008 |
Journal: |
Cell |
Title: |
Identification of oxidative stress and Toll-like receptor 4 signaling as a key pathway of acute lung injury. |
Volume: |
133 |
Issue: |
2 |
Pages: |
235-49 |
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•
•
•
•
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Publication |
First Author: |
Zumla A |
Year: |
2016 |
Journal: |
Nat Rev Drug Discov |
Title: |
Coronaviruses - drug discovery and therapeutic options. |
Volume: |
15 |
Issue: |
5 |
Pages: |
327-47 |
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•
•
•
•
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Publication |
First Author: |
Netland J |
Year: |
2010 |
Journal: |
Virology |
Title: |
Immunization with an attenuated severe acute respiratory syndrome coronavirus deleted in E protein protects against lethal respiratory disease. |
Volume: |
399 |
Issue: |
1 |
Pages: |
120-128 |
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•
•
•
•
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Publication |
First Author: |
Menachery VD |
Year: |
2016 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
SARS-like WIV1-CoV poised for human emergence. |
Volume: |
113 |
Issue: |
11 |
Pages: |
3048-53 |
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•
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Publication |
First Author: |
Morales-Nebreda L |
Year: |
2021 |
Journal: |
JCI Insight |
Title: |
Aging imparts cell-autonomous dysfunction to regulatory T cells during recovery from influenza pneumonia. |
Volume: |
6 |
Issue: |
6 |
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•
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•
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Publication |
First Author: |
Channappanavar R |
Year: |
2016 |
Journal: |
Cell Host Microbe |
Title: |
Dysregulated Type I Interferon and Inflammatory Monocyte-Macrophage Responses Cause Lethal Pneumonia in SARS-CoV-Infected Mice. |
Volume: |
19 |
Issue: |
2 |
Pages: |
181-93 |
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•
•
•
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Publication |
First Author: |
Klemm T |
Year: |
2020 |
Journal: |
EMBO J |
Title: |
Mechanism and inhibition of the papain-like protease, PLpro, of SARS-CoV-2. |
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Pages: |
e106275 |
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Publication |
First Author: |
Subbarao K |
Year: |
2004 |
Journal: |
J Virol |
Title: |
Prior infection and passive transfer of neutralizing antibody prevent replication of severe acute respiratory syndrome coronavirus in the respiratory tract of mice. |
Volume: |
78 |
Issue: |
7 |
Pages: |
3572-7 |
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•
•
•
•
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Publication |
First Author: |
Subbarao K |
Year: |
2006 |
Journal: |
Trends Microbiol |
Title: |
Is there an ideal animal model for SARS? |
Volume: |
14 |
Issue: |
7 |
Pages: |
299-303 |
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•
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•
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Publication |
First Author: |
Day CW |
Year: |
2009 |
Journal: |
Virology |
Title: |
A new mouse-adapted strain of SARS-CoV as a lethal model for evaluating antiviral agents in vitro and in vivo. |
Volume: |
395 |
Issue: |
2 |
Pages: |
210-22 |
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•
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•
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Publication |
First Author: |
Hou YJ |
Year: |
2020 |
Journal: |
Cell |
Title: |
SARS-CoV-2 Reverse Genetics Reveals a Variable Infection Gradient in the Respiratory Tract. |
Volume: |
182 |
Issue: |
2 |
Pages: |
429-446.e14 |
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•
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Publication |
First Author: |
Kumar S |
Year: |
2020 |
Journal: |
Virusdisease |
Title: |
Selection of animal models for COVID-19 research. |
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Pages: |
1-6 |
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Protein Domain |
Type: |
Homologous_superfamily |
Description: |
This superfamily represents the N-terminal region of the SUD domain (SUD-N or Mac2) found in non-structural protein NSP3, the product of ORF1a in group 2 (beta) coronaviruses. It is found in human SARS-CoV and SARS-CoV-2 polyprotein 1a and 1ab, and in related coronavirus polyproteins [].Non-structural protein Nsp3 contains at least seven different functional modules within its 1922-amino-acid polypeptide chain. One of these is the so-called SARS (severe acute respiratory syndrome)-unique domain (SUD), a stretch of about 338 residues that is completely absent from any other coronavirus. The SUD domain may be responsible for the high pathogenicity of the SARS coronavirus, compared to other viruses of this family [, ]. Later, the NSP3 of MHV was shown by X-ray crystallography to contain a SUD-C-like fold, so it is no longer appropriate to call this domain "SARS-unique". This region has been renamed into "Domain Preceding Ubl2 and PL2pro"(DPUP) []. NSP3 has been shown to bind to viral RNA, nucleocapsid protein, as well as other viral proteins, and participates in polyprotein processing. It is a multifunctional protein comprising up to 16 different domains and regions []. SUD(core) exhibits a two-domain architecture. The N-terminal subdomain (SUD-N) and the C-terminal subdomain of SUDcore, also named middle SUD subdomain, or SUD-M [, ]. SUD-N has been shown to be dispensable for the SARS-CoV replication/transcription complex within the context of a SARS-CoV replicon []. SUD consists of three globular domains separated by short linker peptide segments: SUD-N, SUD-M, and SUD-C []. Among these, SUD-N and SUD-M are macrodomains. The SUD-N domain is a related macrodomain which also binds G-quadruplexes []. While SUD-N is specific to the NSP3 of SARS and betacoronaviruses of the sarbecovirus subgenera (B lineage), SUD-M is present in most NSP3 proteins except the NSP3 from betacoronaviruses of the embecovirus subgenera (A lineage). SUD-M, despite its name, is not specific to SARS. SUD-C adopts a frataxin-like fold, has structural similarity to DNA-binding domains of DNA-modifying enzymes, binds single-stranded RNA, and regulates the RNA binding behavior of the SUD-M macrodomain. SARS-CoV Nsp3 contains a third macrodomain (the X-domain). The X-domain may function as a module binding poly(ADP-ribose); however, SUD-N and SUD-M do not bind ADP-ribose, as the triple glycine sequence involved in its binding is not conserved in these []. |
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Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
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Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
Mus caroli |
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•
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Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
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•
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Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
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•
•
•
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Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
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•
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Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
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