Characterization of a Novel Coronavirus Associated with Severe Acute Respiratory Syndrome

Rota, Paul A.; Oberste, M. Steven; Monroe, Stephan S.; Nix, W. Allan; Campagnoli, Raymond P.; Icenogle, Joseph P.; Peñaranda, Silvia; Bankamp, Bettina; Maher, Kaija; Chen, Min Hsin; Tong, Suxiong; Tamin, Azaibi; Lowe, Luis; Frace, Michael; DeRisi, Joseph L.; Chen, Qi; Wang, David; Erdman, Dean D.; Peret, Teresa C. T.; Burns, Cara C.; Ksiazek, Thomas G.; Rollin, Pierre E.; Sanchez, Anthony; Liffick, Stephanie; Holloway, Brian; Limor, Josef; McCaustland, Karen A.; Olsen-Rasmussen, Mellissa; Fouchier, Ron A. M.; Günther, Stephan; Osterhaus, Albert D. M. E.; Drosten, Christian; Pallansch, Mark A.; Anderson, Larry J.; Bellini, William J.

doi:10.1126/science.1085952

Cited by 2,303 publications

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References 16 publications

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“…This region is proximal to a predicted TM domain (Figure 2A), which was identified using the WW octanol hydrophobicity scale that allows for the identification of TM helices of membrane proteins with very high accuracy (73). On the basis of these observations, it is unlikely that the aromatic domain is part of the TM anchor as previously predicted by Rota et al (6), rather, as described for the aromatic domains of HIV-1 and EboV (10,55,56,58), this region is most likely an independent domain proximal to the TM anchor of the S2 subunit.…”

Section: Resultsmentioning

confidence: 52%

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The Aromatic Domain of the Coronavirus Class I Viral Fusion Protein Induces Membrane Permeabilization: Putative Role during Viral Entry

et al. 2004

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Coronavirus (CoV) entry is mediated by the viral spike (S) glycoprotein, a class I viral fusion protein. During viral and target cell membrane fusion, the heptad repeat (HR) regions of the S2 subunit assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes; however, the exact mechanism is unclear. Here, we characterize an aromatic amino acid rich region within the ectodomain of the S2 subunit that both partitions into lipid membranes and has the capacity to perturb lipid vesicle integrity. Circular dichroism analysis indicated that peptides analogous to the aromatic domains of the severe acute respiratory syndrome (SARS)-CoV, mouse hepatitis virus (MHV) and the human CoV OC43 S2 subunits, did not have a propensity for a defined secondary structure. These peptides strongly partitioned into lipid membranes and induced lipid vesicle permeabilization at peptide/lipid ratios of 1:100 in two independent leakage assays. Thus, partitioning of the peptides into the lipid interface is sufficient to disorganize membrane integrity. Our study of the S2 aromatic domain of three CoVs provides supportive evidence for a functional role of this region. We propose that, when aligned with the fusion peptide and transmembrane domains during membrane apposition, the aromatic domain of the CoV S protein functions to perturb the target cell membrane and provides a continuous track of hydrophobic surface, resulting in lipid-membrane fusion and subsequent viral nucleocapsid entry.

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Section: Resultsmentioning

confidence: 52%

“…Downloaded by TULANE UNIV on August 13, 2009 part of the TM anchor (6). In Figure 1, we depict the aromatic domain as separate from the TM anchor based on WW interfacial and octanol hydrophobicity plots of the C-terminal end of the SARS-CoV S2 subunit (Figure 2A).…”

Section: Discussionmentioning

confidence: 99%

The Aromatic Domain of the Coronavirus Class I Viral Fusion Protein Induces Membrane Permeabilization: Putative Role during Viral Entry

et al. 2004

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Cell Research | www.cell-research.com Antiviral effects of IFN-α against MHV-1 220 npg ORIGINAL ARTICLE

IntroductionIn March 2003, a number of laboratories independently reported the isolation and characterization of a novel coronavirus (CoV) from specimens of patients with severe acute respiratory syndrome (SARS) [1,2]. Although an effective therapeutic strategy against SARS has yet to be developed, interferons (IFN) are recognized to play critical roles in host resistance to viral infection [3][4][5][6], thereby implicating them as potential candidates for SARS CoV treatment.

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confidence: 99%

Characterization of the antiviral effects of interferon-α against a SARS-like coronoavirus infection in vitro

et al. 2006

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Cell Research | www.cell-research.com Antiviral effects of IFN-α against MHV-1 220 npg ORIGINAL ARTICLE IntroductionIn March 2003, a number of laboratories independently reported the isolation and characterization of a novel coronavirus (CoV) from specimens of patients with severe acute respiratory syndrome (SARS) [1,2]. Although an effective therapeutic strategy against SARS has yet to be developed, interferons (IFN) are recognized to play critical roles in host resistance to viral infection [3][4][5][6], thereby implicating them as potential candidates for SARS CoV treatment. IFNs inhibit viral infection by directly interfering with viral replication and by inducing both an innate and adaptive immune response to infection. IFN-αs are effective in the treatment of hepatitis B and C [7,8] and respiratory coronavirus infections unrelated to the Urbani strain of SARS-CoV [9][10][11][12]. , and combinations of 18] are effective in inhibiting SARS-CoV replication in vitro. Moreover, it was reported that macacque monkeys were protected from infection with SARS CoV by treatment with .IFN alfacon-1 (Infergen, Intermune Corp, Brisbane, California), a synthetic IFN-α designed to represent a consensus , has been shown in both cell culture systems [21] and comparative clinical trials [22] to inhibit viral replication more potently than other IFN-αs. Based on these findings, a pilot study to evaluate the potential clinical benefit and safety of IFN alfacon-1 in SARS treatment was conducted by our laboratory. Interferon (IFN)-αs bind to and activate their cognate cell surface receptor to invoke an antiviral response in target cells. Well-described receptor-mediated signaling events result in transcriptional regulation of IFN sensitive genes, effectors of this antiviral response. Results from a pilot study to evaluate the clinical efficacy of IFN-α treatment of SARS patients provided evidence for IFN-inducible resolution of disease. In this report we examined the contribution of IFN-inducible phosphorylation-activation of specific signaling effectors to protection from infection by a SARS-related murine coronavirus, MHV-1. As anticipated, the earliest receptor-activation event, Jak1 phosphorylation, is critical for IFN-inducible protection from MHV-1 infection. Additionally, we provide evidence for the contribution of two kinases, the MAP kinase p38MAPK, and protein kinase C (PKC) d to antiviral protection from MHV-1 infection. Notably, our data suggest that MHV-1 infection, as for the Urbani SARS coronoavirus, inhibits an IFN response, inferred from the lack of activation of pkr and 2'5'-oas, genes associated with mediating the antiviral activities of IFN-αs. To identify potential target genes that are activated downstream of the IFN-inducible signaling effectors we identified, and that mediate protection from coronavirus infection, we examined the gene expression profiles in the peripheral blood mononuclear cells of SARS patients who received IFN treatment. A subset of differentially regulated genes were distinguished with...

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“…Coronaviruses are currently classified into four distinct groups based on sequence analysis and genome structure and on the antigenic relationships [101,139,150]. The coronavirus structural proteins include the spike glycoprotein, the membrane glycoprotein and the nucleocapsid protein.…”

Section: Canine Respiratory Coronavirusmentioning

confidence: 99%

Canine respiratory viruses

2007

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-Acute contagious respiratory disease (kennel cough) is commonly described in dogs worldwide. The disease appears to be multifactorial and a number of viral and bacterial pathogens have been reported as potential aetiological agents, including canine parainfluenza virus, canine adenovirus and Bordetella bronchiseptica, as well as mycoplasmas, Streptococcus equi subsp. zooepidemicus, canine herpesvirus and reovirus-1,-2 and -3. Enhancement of pathogenicity by multiple infections can result in more severe clinical forms. In addition, acute respiratory diseases associated with infection by influenza A virus, and group I and II coronaviruses, have been described recently in dogs. Host species shifts and tropism changes are likely responsible for the onset of these new pathogens. The importance of the viral agents in the kennel cough complex is discussed.

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Characterization of a Novel Coronavirus Associated with Severe Acute Respiratory Syndrome

Cited by 2,303 publications

References 16 publications

The Aromatic Domain of the Coronavirus Class I Viral Fusion Protein Induces Membrane Permeabilization: Putative Role during Viral Entry

The Aromatic Domain of the Coronavirus Class I Viral Fusion Protein Induces Membrane Permeabilization: Putative Role during Viral Entry

Characterization of the antiviral effects of interferon-α against a SARS-like coronoavirus infection in vitro

Canine respiratory viruses

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