SARS coronavirus

Summary

Alias: Human coronavirus (strain SARS), SARS virus, HCoV-SARS, Severe acute respiratory syndrome coronavirus

Top Publications

  1. Marra M, Jones S, Astell C, Holt R, Brooks Wilson A, Butterfield Y, et al. The Genome sequence of the SARS-associated coronavirus. Science. 2003;300:1399-404 pubmed
    ..The genome sequence will aid in the diagnosis of SARS virus infection in humans and potential animal hosts (using polymerase chain reaction and immunological tests), in the ..
  2. Teoh K, Siu Y, Chan W, Schlüter M, Liu C, Peiris J, et al. The SARS coronavirus E protein interacts with PALS1 and alters tight junction formation and epithelial morphogenesis. Mol Biol Cell. 2010;21:3838-52 pubmed publisher
    ..We speculate that hijacking of PALS1 by SARS-CoV E plays a determinant role in the disruption of the lung epithelium in SARS patients. ..
  3. Chang C, Sue S, Yu T, Hsieh C, Tsai C, Chiang Y, et al. Modular organization of SARS coronavirus nucleocapsid protein. J Biomed Sci. 2006;13:59-72 pubmed
    ..This study provides information on the domain structure partition of SARS-CoV N protein and insights into the differing roles of structured and disordered regions in coronavirus nucleocapsid proteins. ..
  4. Broer R, Boson B, Spaan W, Cosset F, Corver J. Important role for the transmembrane domain of severe acute respiratory syndrome coronavirus spike protein during entry. J Virol. 2006;80:1302-10 pubmed
    The spike protein (S) of severe acute respiratory syndrome coronavirus (SARS-CoV) is responsible for receptor binding and membrane fusion...
  5. Guillen J, Pérez Berná A, Moreno M, Villalain J. Identification of the membrane-active regions of the severe acute respiratory syndrome coronavirus spike membrane glycoprotein using a 16/18-mer peptide scan: implications for the viral fusion mechanism. J Virol. 2005;79:1743-52 pubmed
    We have identified the membrane-active regions of the severe acute respiratory syndrome coronavirus (SARS CoV) spike glycoprotein by determining the effect on model membrane integrity of a 16/18-mer SARS CoV spike glycoprotein peptide ..
  6. Chan C, Siu K, Chin K, Yuen K, Zheng B, Jin D. Modulation of the unfolded protein response by the severe acute respiratory syndrome coronavirus spike protein. J Virol. 2006;80:9279-87 pubmed
    ..Taken together, our findings suggest that SARS-CoV S protein specifically modulates the UPR to facilitate viral replication. ..
  7. Obitsu S, Ahmed N, Nishitsuji H, Hasegawa A, Nakahama K, Morita I, et al. Potential enhancement of osteoclastogenesis by severe acute respiratory syndrome coronavirus 3a/X1 protein. Arch Virol. 2009;154:1457-64 pubmed publisher
    b>Severe acute respiratory syndrome coronavirus (SARS-CoV) causes a lung disease with high mortality...
  8. Li W, Zhang C, Sui J, Kuhn J, Moore M, Luo S, et al. Receptor and viral determinants of SARS-coronavirus adaptation to human ACE2. EMBO J. 2005;24:1634-43 pubmed
    Human angiotensin-converting enzyme 2 (ACE2) is a functional receptor for SARS coronavirus (SARS-CoV). Here we identify the SARS-CoV spike (S)-protein-binding site on ACE2...
  9. Yang Z, Werner H, Kong W, Leung K, Traggiai E, Lanzavecchia A, et al. Evasion of antibody neutralization in emerging severe acute respiratory syndrome coronaviruses. Proc Natl Acad Sci U S A. 2005;102:797-801 pubmed
    Molecular characterization of the severe acute respiratory syndrome coronavirus has revealed genetic diversity among isolates...

More Information

Publications103 found, 100 shown here

  1. Duquerroy S, Vigouroux A, Rottier P, Rey F, Bosch B. Central ions and lateral asparagine/glutamine zippers stabilize the post-fusion hairpin conformation of the SARS coronavirus spike glycoprotein. Virology. 2005;335:276-85 pubmed
    ..Here, we report the X-ray structure of a previously characterized HR1/HR2 complex of the severe acute respiratory syndrome coronavirus spike protein...
  2. Lu W, Zheng B, Xu K, Schwarz W, Du L, Wong C, et al. Severe acute respiratory syndrome-associated coronavirus 3a protein forms an ion channel and modulates virus release. Proc Natl Acad Sci U S A. 2006;103:12540-5 pubmed
    ..This finding will help to explain the highly pathogenic nature of SARS-CoV and to develop new strategies for treatment of SARS infection. ..
  3. Padhan K, Minakshi R, Towheed M, Jameel S. Severe acute respiratory syndrome coronavirus 3a protein activates the mitochondrial death pathway through p38 MAP kinase activation. J Gen Virol. 2008;89:1960-9 pubmed publisher
    The molecular mechanisms governing severe acute respiratory syndrome coronavirus-induced pathology are not fully understood. Virus infection and some individual viral proteins, including the 3a protein, induce apoptosis...
  4. Chang C, Hsu Y, Chang Y, Chao F, Wu M, Huang Y, et al. Multiple nucleic acid binding sites and intrinsic disorder of severe acute respiratory syndrome coronavirus nucleocapsid protein: implications for ribonucleocapsid protein packaging. J Virol. 2009;83:2255-64 pubmed publisher
    The nucleocapsid protein (N) of the severe acute respiratory syndrome coronavirus (SARS-CoV) packages the viral genomic RNA and is crucial for viability. However, the RNA-binding mechanism is poorly understood...
  5. Tan Y. The Severe Acute Respiratory Syndrome (SARS)-coronavirus 3a protein may function as a modulator of the trafficking properties of the spike protein. Virol J. 2005;2:5 pubmed
    ..Modulation by this unique pathway could confer certain advantages during the replication of the severe acute respiratory syndrome-coronavirus. ..
  6. McBride C, Li J, Machamer C. The cytoplasmic tail of the severe acute respiratory syndrome coronavirus spike protein contains a novel endoplasmic reticulum retrieval signal that binds COPI and promotes interaction with membrane protein. J Virol. 2007;81:2418-28 pubmed
    Like other coronaviruses, severe acute respiratory syndrome coronavirus (SARS CoV) assembles at and buds into the lumen of the endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC)...
  7. Chen C, Chang C, Chang Y, Sue S, Bai H, Riang L, et al. Structure of the SARS coronavirus nucleocapsid protein RNA-binding dimerization domain suggests a mechanism for helical packaging of viral RNA. J Mol Biol. 2007;368:1075-86 pubmed
    ..Packing of the octamers in the crystal forms two parallel, basic helical grooves, which may be oligonucleotide attachment sites, and suggests a mechanism for helical RNA packaging in the virus. ..
  8. Watanabe R, Matsuyama S, Shirato K, Maejima M, Fukushi S, Morikawa S, et al. Entry from the cell surface of severe acute respiratory syndrome coronavirus with cleaved S protein as revealed by pseudotype virus bearing cleaved S protein. J Virol. 2008;82:11985-91 pubmed publisher
    ..Those results indicate that SARS-CoV with a cleaved S protein is able to enter cells directly from the cell surface and agree with the previous observation of the protease-mediated cell surface entry of SARS-CoV. ..
  9. Belouzard S, Chu V, Whittaker G. Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites. Proc Natl Acad Sci U S A. 2009;106:5871-6 pubmed publisher
    ..In the case of the severe acute respiratory syndrome coronavirus (SARS-CoV), it has been shown that virus entry requires the endosomal protease cathepsin L; ..
  10. Tan Y, Fielding B, Goh P, Shen S, Tan T, Lim S, et al. Overexpression of 7a, a protein specifically encoded by the severe acute respiratory syndrome coronavirus, induces apoptosis via a caspase-dependent pathway. J Virol. 2004;78:14043-7 pubmed
    Besides genes that are homologous to proteins found in other coronaviruses, the severe acute respiratory syndrome coronavirus genome also contains nine other potential open reading frames...
  11. Petit C, Melancon J, Chouljenko V, Colgrove R, Farzan M, Knipe D, et al. Genetic analysis of the SARS-coronavirus spike glycoprotein functional domains involved in cell-surface expression and cell-to-cell fusion. Virology. 2005;341:215-30 pubmed
    ..This genetic analysis reveals that the SARS-CoV S glycoprotein contains extracellular domains that regulate cell fusion as well as distinct endodomains that function in intracellular transport, cell-surface expression, and cell fusion. ..
  12. Peng T, Lee K, Tarn W. Phosphorylation of the arginine/serine dipeptide-rich motif of the severe acute respiratory syndrome coronavirus nucleocapsid protein modulates its multimerization, translation inhibitory activity and cellular localization. FEBS J. 2008;275:4152-63 pubmed publisher
    ..In the present study, we demonstrate that the severe acute respiratory syndrome coronavirus nucleocapsid protein is phosphorylated primarily within the RS-rich region in cells and by SR ..
  13. Chan C, Tsoi H, Chan W, Zhai S, Wong C, Yao X, et al. The ion channel activity of the SARS-coronavirus 3a protein is linked to its pro-apoptotic function. Int J Biochem Cell Biol. 2009;41:2232-9 pubmed publisher
    ..As ion channel activity has been reported to regulate apoptosis in different pathologic conditions, finding ways to modulate the ion channel activity may offer a new direction toward the inhibition of apoptosis triggered by SARS-CoV. ..
  14. Thiel V, Ivanov K, Putics A, Hertzig T, Schelle B, Bayer S, et al. Mechanisms and enzymes involved in SARS coronavirus genome expression. J Gen Virol. 2003;84:2305-15 pubmed
    ..Here, we determined the sequence of SARS coronavirus (SARS-CoV), isolate Frankfurt 1, and characterized key RNA elements and protein functions involved in viral ..
  15. Snijder E, Bredenbeek P, Dobbe J, Thiel V, Ziebuhr J, Poon L, et al. Unique and conserved features of genome and proteome of SARS-coronavirus, an early split-off from the coronavirus group 2 lineage. J Mol Biol. 2003;331:991-1004 pubmed
    The genome organization and expression strategy of the newly identified severe acute respiratory syndrome coronavirus (SARS-CoV) were predicted using recently published genome sequences...
  16. He R, Dobie F, Ballantine M, Leeson A, Li Y, Bastien N, et al. Analysis of multimerization of the SARS coronavirus nucleocapsid protein. Biochem Biophys Res Commun. 2004;316:476-83 pubmed
    ..The genome of SARS Coronavirus (SARS-CoV) has recently been sequenced, and a number of genes identified, including that of the nucleocapsid ..
  17. Surjit M, Liu B, Kumar P, Chow V, Lal S. The nucleocapsid protein of the SARS coronavirus is capable of self-association through a C-terminal 209 amino acid interaction domain. Biochem Biophys Res Commun. 2004;317:1030-6 pubmed
    ..In this report we have cloned the N gene of the SARS coronavirus, and studied its property of self-association to form dimers...
  18. Xu Y, Lou Z, Liu Y, Pang H, Tien P, Gao G, et al. Crystal structure of severe acute respiratory syndrome coronavirus spike protein fusion core. J Biol Chem. 2004;279:49414-9 pubmed
    b>Severe acute respiratory syndrome coronavirus is a newly emergent virus responsible for a recent outbreak of an atypical pneumonia...
  19. Nal B, Chan C, Kien F, Siu L, Tse J, Chu K, et al. Differential maturation and subcellular localization of severe acute respiratory syndrome coronavirus surface proteins S, M and E. J Gen Virol. 2005;86:1423-34 pubmed
  20. Yu I, Gustafson C, Diao J, Burgner J, Li Z, Zhang J, et al. Recombinant severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein forms a dimer through its C-terminal domain. J Biol Chem. 2005;280:23280-6 pubmed
    ..These results suggest that the N protein oligomerization involves the C-terminal residues 285-422, and this region is a good target for mutagenic studies to disrupt N protein self-association and virion assembly. ..
  21. Chang C, Sue S, Yu T, Hsieh C, Tsai C, Chiang Y, et al. The dimer interface of the SARS coronavirus nucleocapsid protein adapts a porcine respiratory and reproductive syndrome virus-like structure. FEBS Lett. 2005;579:5663-8 pubmed
    We have employed NMR to investigate the structure of SARS coronavirus nucleocapsid protein dimer. We found that the secondary structure of the dimerization domain consists of five alpha helices and a beta-hairpin...
  22. Surjit M, Liu B, Chow V, Lal S. The nucleocapsid protein of severe acute respiratory syndrome-coronavirus inhibits the activity of cyclin-cyclin-dependent kinase complex and blocks S phase progression in mammalian cells. J Biol Chem. 2006;281:10669-81 pubmed
    ..Down-regulation of E2F1 targets was also observed in SARS-CoV-infected VeroE6 cells. These data suggest that the S phase inhibitory activity of the N protein may have major significance during viral pathogenesis. ..
  23. Yu I, Oldham M, Zhang J, Chen J. Crystal structure of the severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein dimerization domain reveals evolutionary linkage between corona- and arteriviridae. J Biol Chem. 2006;281:17134-9 pubmed
    ..This finding provides structural evidence of the evolutionary link between Coronaviridae and Arteriviridae, suggesting that the N proteins of both viruses have a common origin. ..
  24. Corver J, Broer R, van Kasteren P, Spaan W. GxxxG motif of severe acute respiratory syndrome coronavirus spike glycoprotein transmembrane domain is not involved in trimerization and is not important for entry. J Virol. 2007;81:8352-5 pubmed
    ..In addition, the capability of S to mediate entry of SARS S-pseudotyped particles overall was affected moderately in the mutant proteins, also arguing for a nonvital role for the GxxxG motif in SARS coronavirus entry.
  25. Beniac D, deVarennes S, Andonov A, He R, Booth T. Conformational reorganization of the SARS coronavirus spike following receptor binding: implications for membrane fusion. PLoS ONE. 2007;2:e1082 pubmed
    The SARS coronavirus (SARS-CoV) spike is the largest known viral spike molecule, and shares a similar function with all class 1 viral fusion proteins...
  26. Wang S, Chang Y, Chen Y, Wang C. Severe acute respiratory syndrome coronavirus nucleocapsid protein confers ability to efficiently produce virus-like particles when substituted for the human immunodeficiency virus nucleocapsid domain. J Biomed Sci. 2008;15:719-29 pubmed publisher
    ..The results suggest that the domain conferring the ability to direct VLP assembly and release in SARS-CoV N is largely contained between residues 168 and 421. ..
  27. Siu Y, Teoh K, Lo J, Chan C, Kien F, Escriou N, et al. The M, E, and N structural proteins of the severe acute respiratory syndrome coronavirus are required for efficient assembly, trafficking, and release of virus-like particles. J Virol. 2008;82:11318-30 pubmed publisher
    ..Fluorescent VLPs will be used further to investigate the role of cellular machineries during SARS-CoV egress. ..
  28. Siu K, Kok K, Ng M, Poon V, Yuen K, Zheng B, et al. Severe acute respiratory syndrome coronavirus M protein inhibits type I interferon production by impeding the formation of TRAF3.TANK.TBK1/IKKepsilon complex. J Biol Chem. 2009;284:16202-9 pubmed publisher
    ..In this study we demonstrate that SARS coronavirus M protein inhibits gene transcription of type I interferons...
  29. Yang H, Yang M, Ding Y, Liu Y, Lou Z, Zhou Z, et al. The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitor. Proc Natl Acad Sci U S A. 2003;100:13190-5 pubmed
    A newly identified severe acute respiratory syndrome coronavirus (SARS-CoV), is the etiological agent responsible for the outbreak of SARS. The SARS-CoV main protease, which is a 33...
  30. Wang S, Chou T, Sakhatskyy P, Huang S, Lawrence J, Cao H, et al. Identification of two neutralizing regions on the severe acute respiratory syndrome coronavirus spike glycoprotein produced from the mammalian expression system. J Virol. 2005;79:1906-10 pubmed
    ..Two neutralizing domains were identified on the S protein, one at the N terminus (Ser12-Thr535) and the other near the C terminus (Arg797-Ile1192). ..
  31. Li F, Li W, Farzan M, Harrison S. Structure of SARS coronavirus spike receptor-binding domain complexed with receptor. Science. 2005;309:1864-8 pubmed
    The spike protein (S) of SARS coronavirus (SARS-CoV) attaches the virus to its cellular receptor, angiotensin-converting enzyme 2 (ACE2). A defined receptor-binding domain (RBD) on S mediates this interaction. The crystal structure at 2...
  32. Luo H, Ye F, Chen K, Shen X, Jiang H. SR-rich motif plays a pivotal role in recombinant SARS coronavirus nucleocapsid protein multimerization. Biochemistry. 2005;44:15351-8 pubmed
    The nucleocapsid (N) protein of SARS coronavirus (SARS-CoV) is reported to function in encapsidating the viral genomic RNA into helical nucleocapsid, and its self-association is believed to be vital in coating the viral genomic RNA...
  33. Petit C, Chouljenko V, Iyer A, Colgrove R, Farzan M, Knipe D, et al. Palmitoylation of the cysteine-rich endodomain of the SARS-coronavirus spike glycoprotein is important for spike-mediated cell fusion. Virology. 2007;360:264-74 pubmed
    ..These results show that the S cytoplasmic domain is palmitoylated and that palmitoylation of the membrane proximal cysteine clusters I and II may be important for S-mediated cell fusion. ..
  34. Yuan X, Yao Z, Wu J, Zhou Y, Shan Y, Dong B, et al. G1 phase cell cycle arrest induced by SARS-CoV 3a protein via the cyclin D3/pRb pathway. Am J Respir Cell Mol Biol. 2007;37:9-19 pubmed
    ..These results indicate that SARS-CoV 3a protein, through limiting the expression of cyclin D3, may inhibit Rb phosphorylation, which in turn leads to a block in the G1 phase of the cell cycle and an inhibition of cell proliferation. ..
  35. Tan Y, Tan T, Lee M, Tham P, Gunalan V, Druce J, et al. Induction of apoptosis by the severe acute respiratory syndrome coronavirus 7a protein is dependent on its interaction with the Bcl-XL protein. J Virol. 2007;81:6346-55 pubmed
    The severe acute respiratory syndrome coronavirus (SARS-CoV) 7a protein, which is not expressed by other known coronaviruses, can induce apoptosis in various cell lines...
  36. Padhan K, Tanwar C, Hussain A, Hui P, Lee M, Cheung C, et al. Severe acute respiratory syndrome coronavirus Orf3a protein interacts with caveolin. J Gen Virol. 2007;88:3067-77 pubmed
    The orf3a (also called X1 or U274) gene is the largest unique open reading frame in the severe acute respiratory syndrome coronavirus genome and has been proposed to encode a protein with three transmembrane domains and a large ..
  37. Lu Y, Neo T, Liu D, Tam J. Importance of SARS-CoV spike protein Trp-rich region in viral infectivity. Biochem Biophys Res Commun. 2008;371:356-60 pubmed publisher
    ..In contrast, Phe-substituted mutants are able to restore 10-25% infectivity comparing to the wild-type. The results suggest that the Trp-rich region of S protein is essential for SARS-CoV infectivity. ..
  38. Takeda M, Chang C, Ikeya T, Güntert P, Chang Y, Hsu Y, et al. Solution structure of the c-terminal dimerization domain of SARS coronavirus nucleocapsid protein solved by the SAIL-NMR method. J Mol Biol. 2008;380:608-22 pubmed publisher
    The C-terminal domain (CTD) of the severe acute respiratory syndrome coronavirus (SARS-CoV) nucleocapsid protein (NP) contains a potential RNA-binding region in its N-terminal portion and also serves as a dimerization domain by forming a ..
  39. Kam Y, Okumura Y, Kido H, Ng L, Bruzzone R, Altmeyer R. Cleavage of the SARS coronavirus spike glycoprotein by airway proteases enhances virus entry into human bronchial epithelial cells in vitro. PLoS ONE. 2009;4:e7870 pubmed publisher
    ..the susceptibility of a recombinant native full-length S-protein trimer (triSpike) of the severe acute respiratory syndrome coronavirus (SARS-CoV) to cleavage by various airway proteases...
  40. Minakshi R, Padhan K, Rani M, Khan N, Ahmad F, Jameel S. The SARS Coronavirus 3a protein causes endoplasmic reticulum stress and induces ligand-independent downregulation of the type 1 interferon receptor. PLoS ONE. 2009;4:e8342 pubmed publisher
    The Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV) is reported to cause apoptosis of infected cells and several of its proteins including the 3a accessory protein, are pro-apoptotic...
  41. Liao Y, Lescar J, Tam J, Liu D. Expression of SARS-coronavirus envelope protein in Escherichia coli cells alters membrane permeability. Biochem Biophys Res Commun. 2004;325:374-80 pubmed publisher
    ..This is the first report demonstrating that a coronavirus-encoded protein could modify membrane permeability in E. coli cells...
  42. Kong W, Xu L, Stadler K, Ulmer J, Abrignani S, Rappuoli R, et al. Modulation of the immune response to the severe acute respiratory syndrome spike glycoprotein by gene-based and inactivated virus immunization. J Virol. 2005;79:13915-23 pubmed
    ..The use of inactivated SARS virus with MF59 enhanced the CD4 and antibody response even after gene-based vaccination...
  43. Diemer C, Schneider M, Seebach J, Quaas J, Fr sner G, Sch tzl H, et al. Cell type-specific cleavage of nucleocapsid protein by effector caspases during SARS coronavirus infection. J Mol Biol. 2008;376:23-34 pubmed publisher
    ..These data suggest a correlation among the replication cycle of SARS-CoV, subcellular localization of N, induction of apoptosis, and the subsequent activation of caspases leading to cleavage of N...
  44. Han M, Yan W, Huang Y, Yao H, Wang Z, Xi D, et al. The nucleocapsid protein of SARS-CoV induces transcription of hfgl2 prothrombinase gene dependent on C/EBP alpha. J Biochem. 2008;144:51-62 pubmed publisher
    ..The results showed that N protein of SARS-CoV induced hfgl2 gene transcription dependent on the transcription factor C/EBP alpha, which maybe contribute to the development of thrombosis in SARS. ..
  45. Guillen J, Pérez Berná A, Moreno M, Villalain J. A second SARS-CoV S2 glycoprotein internal membrane-active peptide. Biophysical characterization and membrane interaction. Biochemistry. 2008;47:8214-24 pubmed publisher
    The severe acute respiratory syndrome coronavirus (SARS-CoV) envelope spike (S) glycoprotein, a class I viral fusion protein, is responsible for the fusion between the membranes of the virus and the target cell...
  46. Miknis Z, Donaldson E, Umland T, Rimmer R, Baric R, Schultz L. Severe acute respiratory syndrome coronavirus nsp9 dimerization is essential for efficient viral growth. J Virol. 2009;83:3007-18 pubmed publisher
    The severe acute respiratory syndrome coronavirus (SARS-CoV) devotes a significant portion of its genome to producing nonstructural proteins required for viral replication...
  47. Báez Santos Y, St John S, Mesecar A. The SARS-coronavirus papain-like protease: structure, function and inhibition by designed antiviral compounds. Antiviral Res. 2015;115:21-38 pubmed publisher
    ..This paper forms part of a series of invited articles in Antiviral Research on "From SARS to MERS: 10years of research on highly pathogenic human coronaviruses." ..
  48. Reid C, Airo A, Hobman T. The Virus-Host Interplay: Biogenesis of +RNA Replication Complexes. Viruses. 2015;7:4385-413 pubmed publisher
    ..This review summarizes current knowledge of critical host factors recruited to or demonstrated to be involved in the biogenesis and stabilization of +RNA virus VRCs. ..
  49. McDermott J, Mitchell H, Gralinski L, Eisfeld A, Josset L, Bankhead A, et al. The effect of inhibition of PP1 and TNF? signaling on pathogenesis of SARS coronavirus. BMC Syst Biol. 2016;10:93 pubmed
    ..To investigate this dichotomy in severe acute respiratory syndrome coronavirus (SARS-CoV), we developed a transcriptional network model of SARS-CoV infection in mice and ..
  50. Strating J, van Kuppeveld F. Viral rewiring of cellular lipid metabolism to create membranous replication compartments. Curr Opin Cell Biol. 2017;47:24-33 pubmed publisher
  51. Zhao G, Shi S, Yang Y, Peng J. M and N proteins of SARS coronavirus induce apoptosis in HPF cells. Cell Biol Toxicol. 2006;22:313-22 pubmed publisher
  52. Schaecher S, Mackenzie J, Pekosz A. The ORF7b protein of severe acute respiratory syndrome coronavirus (SARS-CoV) is expressed in virus-infected cells and incorporated into SARS-CoV particles. J Virol. 2007;81:718-31 pubmed publisher
    ..ORF7b localizes to the Golgi compartment and is incorporated into SARS-CoV particles. We therefore conclude that the ORF7b protein is not only an accessory protein but a structural component of the SARS-CoV virion...
  53. Deng Y, Liu J, Zheng Q, Yong W, Lu M. Structures and polymorphic interactions of two heptad-repeat regions of the SARS virus S2 protein. Structure. 2006;14:889-99 pubmed publisher
    Entry of SARS coronavirus into its target cell requires large-scale structural transitions in the viral spike (S) glycoprotein in order to induce fusion of the virus and cell membranes...
  54. Fang H, Chen Y, Li M, Wu M, Chang C, Chang C, et al. Thermostability of the N-terminal RNA-binding domain of the SARS-CoV nucleocapsid protein: experiments and numerical simulations. Biophys J. 2009;96:1892-901 pubmed publisher
    ..It was shown that the strand beta(1) from the N-terminal folds last and unfolds first, while the remaining beta-strands fold/unfold cooperatively. ..
  55. Liu J, Cao C, Ma Q. [Study on interaction between SARS-CoV N and MAP19]. Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi. 2009;25:777-9 pubmed
    b>Severe acute respiratory syndrome coronavirus (SARS-CoV) is the etiological agent of SARS, an emerging disease characterized by atypical pneumonia...
  56. Ter Meulen J, van den Brink E, Poon L, Marissen W, Leung C, Cox F, et al. Human monoclonal antibody combination against SARS coronavirus: synergy and coverage of escape mutants. PLoS Med. 2006;3:e237 pubmed publisher
    Experimental animal data show that protection against severe acute respiratory syndrome coronavirus (SARS-CoV) infection with human monoclonal antibodies (mAbs) is feasible...
  57. Oostra M, te Lintelo E, Deijs M, Verheije M, Rottier P, de Haan C. Localization and membrane topology of coronavirus nonstructural protein 4: involvement of the early secretory pathway in replication. J Virol. 2007;81:12323-36 pubmed publisher
  58. Miyoshi Akiyama T, Ishida I, Fukushi M, Yamaguchi K, Matsuoka Y, Ishihara T, et al. Fully human monoclonal antibody directed to proteolytic cleavage site in severe acute respiratory syndrome (SARS) coronavirus S protein neutralizes the virus in a rhesus macaque SARS model. J Infect Dis. 2011;203:1574-81 pubmed publisher
    ..is still no effective method to prevent or treat severe acute respiratory syndrome (SARS), which is caused by SARS coronavirus (CoV)...
  59. Chen I, Chang S, Wu H, Yu T, Wei W, Lin S, et al. Upregulation of the chemokine (C-C motif) ligand 2 via a severe acute respiratory syndrome coronavirus spike-ACE2 signaling pathway. J Virol. 2010;84:7703-12 pubmed publisher
    b>Severe acute respiratory syndrome coronavirus (SARS-CoV) was identified to be the causative agent of SARS with atypical pneumonia. Angiotensin-converting enzyme 2 (ACE2) is the major receptor for SARS-CoV...
  60. Chang C, Chen C, Chiang M, Hsu Y, Huang T. Transient oligomerization of the SARS-CoV N protein--implication for virus ribonucleoprotein packaging. PLoS ONE. 2013;8:e65045 pubmed publisher
    The nucleocapsid (N) phosphoprotein of the severe acute respiratory syndrome coronavirus (SARS-CoV) packages the viral genome into a helical ribonucleocapsid and plays a fundamental role during viral self-assembly...
  61. Azzi A, Lin S. Human SARS-coronavirus RNA-dependent RNA polymerase: activity determinants and nucleoside analogue inhibitors. Proteins. 2004;57:12-4 pubmed publisher
  62. Keng C, Zhang A, Shen S, Lip K, Fielding B, Tan T, et al. Amino acids 1055 to 1192 in the S2 region of severe acute respiratory syndrome coronavirus S protein induce neutralizing antibodies: implications for the development of vaccines and antiviral agents. J Virol. 2005;79:3289-96 pubmed publisher
    The spike (S) protein of the severe acute respiratory syndrome coronavirus (SARS-CoV) interacts with cellular receptors to mediate membrane fusion, allowing viral entry into host cells; hence it is recognized as the primary target of ..
  63. Hsieh Y, Li H, Chen S, Lo S. Interactions between M protein and other structural proteins of severe, acute respiratory syndrome-associated coronavirus. J Biomed Sci. 2008;15:707-17 pubmed publisher
    ..A model for the interactions between SARS-CoV M protein and other structural proteins is proposed. This study helps us better understand protein-protein interactions during viral assembly of SARS-CoV...
  64. Zhou Y, Lu K, Pfefferle S, Bertram S, Glowacka I, Drosten C, et al. A single asparagine-linked glycosylation site of the severe acute respiratory syndrome coronavirus spike glycoprotein facilitates inhibition by mannose-binding lectin through multiple mechanisms. J Virol. 2010;84:8753-64 pubmed publisher
    ..Thus, binding of MBL to SARS-S may interfere with other early pre- or postreceptor-binding events necessary for efficient viral entry...
  65. Hu Y, Li W, Gao T, Cui Y, Jin Y, Li P, et al. The Severe Acute Respiratory Syndrome Coronavirus Nucleocapsid Inhibits Type I Interferon Production by Interfering with TRIM25-Mediated RIG-I Ubiquitination. J Virol. 2017;91: pubmed publisher
    ..The outcomes of these findings indicate the function of the coronavirus N protein in modulating the host's initial innate immune response. ..
  66. Netesova N, Belavin P, Seregina E, Ignat ev G, Sandakhchiev L. Cloning, expression, and purification of the nucleocapsid protein of SARS coronavirus. Dokl Biochem Biophys. 2004;397:239-41 pubmed
  67. Leth Larsen R, Zhong F, Chow V, Holmskov U, Lu J. The SARS coronavirus spike glycoprotein is selectively recognized by lung surfactant protein D and activates macrophages. Immunobiology. 2007;212:201-11 pubmed publisher
    The severe acute respiratory syndrome coronavirus (SARS-CoV) infects host cells with its surface glycosylated spike-protein (S-protein)...
  68. Kumar P, Gunalan V, Liu B, Chow V, Druce J, Birch C, et al. The nonstructural protein 8 (nsp8) of the SARS coronavirus interacts with its ORF6 accessory protein. Virology. 2007;366:293-303 pubmed publisher
    ..To the best of our knowledge, this is the first report of the interaction between a SARS-CoV accessory protein and nsp8 and our findings suggest that ORF6 protein may play a role in virus replication...
  69. Zhao X, Nicholls J, Chen Y. Severe acute respiratory syndrome-associated coronavirus nucleocapsid protein interacts with Smad3 and modulates transforming growth factor-beta signaling. J Biol Chem. 2008;283:3272-80 pubmed publisher
    ..Our results reveal a novel mode of Smad3 action in a Smad4-independent manner and may lead to successful strategies for SARS treatment by targeting the TGF-beta signaling molecules...
  70. Glowacka I, Bertram S, M ller M, Allen P, Soilleux E, Pfefferle S, et al. Evidence that TMPRSS2 activates the severe acute respiratory syndrome coronavirus spike protein for membrane fusion and reduces viral control by the humoral immune response. J Virol. 2011;85:4122-34 pubmed publisher
    The spike (S) protein of the severe acute respiratory syndrome coronavirus (SARS-CoV) can be proteolytically activated by cathepsins B and L upon viral uptake into target cell endosomes...
  71. Sakai Y, Kawachi K, Terada Y, Omori H, Matsuura Y, Kamitani W. Two-amino acids change in the nsp4 of SARS coronavirus abolishes viral replication. Virology. 2017;510:165-174 pubmed publisher
    ..These findings provide clues to the mechanism of the replication/transcription complex assembly of SARS-CoV and could reveal an antiviral target for the treatment of betacoronavirus infection. ..
  72. Zhang X, Wang J, Zhang Y, Chen M, Zhang W, Yang S, et al. [Expression, purification and identification of recombinant SARS coronavirus membrane protein]. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2003;35:1140-4 pubmed
    ..The soluble parts of the cell crude extract were then partially purified by MBP affinity chromatography. The purified protein will be used for the studies on M protein's structure and the development of diagnostic method of SARS...
  73. Yuan X, Wu J, Shan Y, Yao Z, Dong B, Chen B, et al. SARS coronavirus 7a protein blocks cell cycle progression at G0/G1 phase via the cyclin D3/pRb pathway. Virology. 2006;346:74-85 pubmed publisher
    ..Accumulation of hypo- or non-phosphorylated pRb thus prevents cell cycle progression at G0/G1 phase...
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    The severe acute respiratory syndrome coronavirus (SARS-CoV) open reading frame 3a protein has recently been shown to be a structural protein...
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    ..We hypothesise that the N-protein uses these signals to traffic to and from the nucleolus and the cytoplasm...
  76. Lee T, Cherney M, Liu J, James K, Powers J, Eltis L, et al. Crystal structures reveal an induced-fit binding of a substrate-like Aza-peptide epoxide to SARS coronavirus main peptidase. J Mol Biol. 2007;366:916-32 pubmed publisher
    The SARS coronavirus main peptidase (SARS-CoV M(pro)) plays an essential role in the life-cycle of the virus and is a primary target for the development of anti-SARS agents...
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    ..We characterized the structures of N-NTD from severe acute respiratory syndrome coronavirus (SARS-CoV) in two crystal forms, at 1.17 A (monoclinic) and at 1...
  78. Huang C, Peters C, Makino S. Severe acute respiratory syndrome coronavirus accessory protein 6 is a virion-associated protein and is released from 6 protein-expressing cells. J Virol. 2007;81:5423-6 pubmed publisher
    Analysis of severe acute respiratory syndrome coronavirus (SCoV) by either sucrose gradient equilibrium centrifugation or a virus capture assay using an anti-SCoV S protein antibody demonstrated that the SCoV 6 protein, which is one of ..
  79. Fukushi S, Mizutani T, Sakai K, Saijo M, Taguchi F, Yokoyama M, et al. Amino acid substitutions in the s2 region enhance severe acute respiratory syndrome coronavirus infectivity in rat angiotensin-converting enzyme 2-expressing cells. J Virol. 2007;81:10831-4 pubmed publisher
    To clarify the molecular basis of severe acute respiratory syndrome coronavirus (SARS-CoV) adaptation to different host species, we serially passaged SARS-CoV in rat angiotensin-converting enzyme 2 (ACE2)-expressing cells...
  80. Schaecher S, Diamond M, Pekosz A. The transmembrane domain of the severe acute respiratory syndrome coronavirus ORF7b protein is necessary and sufficient for its retention in the Golgi complex. J Virol. 2008;82:9477-91 pubmed publisher
    The severe acute respiratory syndrome coronavirus (SARS-CoV) ORF7b (also called 7b) protein is an integral membrane protein that is translated from a bicistronic open reading frame encoded within subgenomic RNA 7...
  81. Tan J, Vonrhein C, Smart O, Bricogne G, Bollati M, Kusov Y, et al. The SARS-unique domain (SUD) of SARS coronavirus contains two macrodomains that bind G-quadruplexes. PLoS Pathog. 2009;5:e1000428 pubmed publisher
    ..SARS) in 2003, the three-dimensional structures of several of the replicase/transcriptase components of SARS coronavirus (SARS-CoV), the non-structural proteins (Nsps), have been determined...
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    The causative agent of severe acute respiratory syndrome, SARS coronavirus (SARS-CoV) genome encodes several unique group specific accessory proteins with unknown functions...
  83. Siqueira A, Lima A, de Souza R, Santos A, Vianez Júnior J, Gonçalves E. In silico analysis of the cyanobacterial lectin scytovirin: new insights into binding properties. Mol Biol Rep. 2017;44:353-358 pubmed publisher
    Scytovirin is a lectin isolated from the cyanobacterium Scytonema varium that has shown activity against HIV, SARS coronavirus and Zaire Ebola virus...
  84. Surjit M, Liu B, Jameel S, Chow V, Lal S. The SARS coronavirus nucleocapsid protein induces actin reorganization and apoptosis in COS-1 cells in the absence of growth factors. Biochem J. 2004;383:13-8 pubmed publisher
    ..The complete genome of the SARS-CoV (SARS coronavirus) has since been sequenced...
  85. Kuri T, Eriksson K, Putics A, Z st R, Snijder E, Davidson A, et al. The ADP-ribose-1''-monophosphatase domains of severe acute respiratory syndrome coronavirus and human coronavirus 229E mediate resistance to antiviral interferon responses. J Gen Virol. 2011;92:1899-905 pubmed publisher
    ..Here, we report that genetically engineered mutants of severe acute respiratory syndrome coronavirus (SARS-CoV) and human coronavirus 229E (HCoV-229E) expressing ADRP-deficient macrodomains ..
  86. Verdi B guena C, Nieto Torres J, Alcaraz A, DeDiego M, Torres J, Aguilella V, et al. Coronavirus E protein forms ion channels with functionally and structurally-involved membrane lipids. Virology. 2012;432:485-94 pubmed publisher
    ..These results suggested that the lipids are functionally involved in E protein ion channel activity, forming a protein-lipid pore, a novel concept for CoV E protein ion channel entity...
  87. Yasui F, Kohara M, Kitabatake M, Nishiwaki T, Fujii H, Tateno C, et al. Phagocytic cells contribute to the antibody-mediated elimination of pulmonary-infected SARS coronavirus. Virology. 2014;454-455:157-68 pubmed publisher
    ..The objective of the present work was to identify, using SARS coronavirus (SARS-CoV) mouse infection models, immune factors responsible for clearing of the virus...
  88. Liu W, Zhao M, Liu K, Xu K, Wong G, Tan W, et al. T-cell immunity of SARS-CoV: Implications for vaccine development against MERS-CoV. Antiviral Res. 2017;137:82-92 pubmed publisher
    ..Virus transmission in humans was quickly halted by public health measures and human infections of SARS coronavirus (SARS-CoV) have not been observed since...
  89. Gui M, Song W, Zhou H, Xu J, Chen S, Xiang Y, et al. Cryo-electron microscopy structures of the SARS-CoV spike glycoprotein reveal a prerequisite conformational state for receptor binding. Cell Res. 2017;27:119-129 pubmed publisher
    ..This phenomenon could be extended to other betacoronaviruses utilizing CTD1 of the S1 subunit for receptor binding, which provides new insights into the intermediate states of coronavirus pre-fusion spike trimer during infection. ..
  90. Venkataraman T, Frieman M. The role of epidermal growth factor receptor (EGFR) signaling in SARS coronavirus-induced pulmonary fibrosis. Antiviral Res. 2017;143:142-150 pubmed publisher
    ..be occasionally seen as a consequence to several respiratory viral infections but is much more common after a SARS coronavirus (SARS-CoV) infection...
  91. Goldberg T, Bennett A, Kityo R, Kuhn J, Chapman C. Kanyawara Virus: A Novel Rhabdovirus Infecting Newly Discovered Nycteribiid Bat Flies Infesting Previously Unknown Pteropodid Bats in Uganda. Sci Rep. 2017;7:5287 pubmed publisher
    Bats are natural reservoir hosts of highly virulent pathogens such as Marburg virus, Nipah virus, and SARS coronavirus. However, little is known about the role of bat ectoparasites in transmitting and maintaining such viruses...
  92. Hu B, Zeng L, Yang X, Ge X, Zhang W, Li B, et al. Discovery of a rich gene pool of bat SARS-related coronaviruses provides new insights into the origin of SARS coronavirus. PLoS Pathog. 2017;13:e1006698 pubmed publisher
    ..However, these bat SARSr-CoVs show sequence differences from SARS coronavirus (SARS-CoV) in different genes (S, ORF8, ORF3, etc) and are considered unlikely to represent the direct ..