The Experts below are selected from a list of 1332 Experts worldwide ranked by ideXlab platform
Alexander E Gorbalenya - One of the best experts on this subject based on the ideXlab platform.
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the species severe acute respiratory syndrome related coronavirus classifying 2019 ncov and naming it sars cov 2
Nature microbiology, 2020Co-Authors: Alexander E GorbalenyaAbstract:The present outbreak of a coronavirus-associated acute respiratory disease called coronavirus disease 19 (COVID-19) is the third documented spillover of an animal coronavirus to humans in only two decades that has resulted in a major epidemic. The Coronaviridae Study Group (CSG) of the International Committee on Taxonomy of Viruses, which is responsible for developing the classification of viruses and taxon nomenclature of the family Coronaviridae, has assessed the placement of the human pathogen, tentatively named 2019-nCoV, within the Coronaviridae. Based on phylogeny, taxonomy and established practice, the CSG recognizes this virus as forming a sister clade to the prototype human and bat severe acute respiratory syndrome coronaviruses (SARS-CoVs) of the species Severe acute respiratory syndrome-related coronavirus, and designates it as SARS-CoV-2. In order to facilitate communication, the CSG proposes to use the following naming convention for individual isolates: SARS-CoV-2/host/location/isolate/date. While the full spectrum of clinical manifestations associated with SARS-CoV-2 infections in humans remains to be determined, the independent zoonotic transmission of SARS-CoV and SARS-CoV-2 highlights the need for studying viruses at the species level to complement research focused on individual pathogenic viruses of immediate significance. This will improve our understanding of virus–host interactions in an ever-changing environment and enhance our preparedness for future outbreaks.
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the severe acute respiratory syndrome coronavirus replicative protein nsp9 is a single stranded rna binding subunit unique in the rna virus world
Proceedings of the National Academy of Sciences of the United States of America, 2004Co-Authors: Marie-pierre Egloff, Helene Dutartre, Eric J. Snijder, Francois Ferron, Corinne Rancurel, Alexander E Gorbalenya, Sonia Longhi, Christian Cambillau, Valerie Campanacci, Bruno CanardAbstract:The recently identified etiological agent of the severe acute respiratory syndrome (SARS) belongs to Coronaviridae (CoV), a family of viruses replicating by a poorly understood mechanism. Here, we report the crystal structure at 2.7-A resolution of nsp9, a hitherto uncharacterized subunit of the SARS-CoV replicative polyproteins. We show that SARS-CoV nsp9 is a single-stranded RNA-binding protein displaying a previously unreported, oligosaccharide/oligonucleotide fold-like fold. The presence of this type of protein has not been detected in the replicative complexes of RNA viruses, and its presence may reflect the unique and complex CoV viral replication/transcription machinery.
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a comparative sequence analysis to revise the current taxonomy of the family Coronaviridae
Archives of Virology, 2003Co-Authors: J M Gonzalez, Alexander E Gorbalenya, Paulino Gomezpuertas, D Cavanagh, Luis EnjuanesAbstract:The Coronaviridae family, comprising the Coronavirus and Torovirus genera, is part of the Nidovirales order that also includes two other families, Arteriviridae and Roniviridae. Based on genetic and serological relationships, groups 1, 2 and 3 were previously recognized in the Coronavirus genus. In this report we present results of comparative sequence analysis of the spike (S), envelope (E), membrane (M), and nucleoprotein (N) structural proteins, and the two most conserved replicase domains, putative RNA-dependent RNA polymerase (RdRp) and RNA helicase (HEL), aimed at a revision of the Coronaviridae taxonomy. The results of pairwise comparisons involving structural and replicase proteins of the Coronavirus genus were consistent and produced percentages of sequence identities that were distributed in discontinuous clusters. Inter-group pairwise scores formed a single cluster in the lowest percentile. No homologs of the N and E proteins have been found outside coronaviruses, and the only (very) distant homologs of S and M proteins were identified in toroviruses. Intragroup sequence conservation was higher, although for some pairs, especially those from the most diverse group 1, scores were close or even overlapped with those from the intergroup comparisons. Phylogenetic analysis of six proteins using a neighbor-joining algorithm confirmed three coronavirus groups. Comparative sequence analysis of RdRp and HEL domains were extended to include arterivirus and ronivirus homologs. The pairwise scores between sequences of the genera Coronavirus and Torovirus (22-25% and 21-25%) were found to be very close to or overlapped with the value ranges (12 to 22% and 17 to 25%) obtained for interfamily pairwise comparisons, but were much smaller than values derived from pairwise comparisons within the Coronavirus genus (63-71% and 59-67%). Phylogenetic analysis confirmed toroviruses and coronaviruses to be separated by a large distance that is comparable to those between established nidovirus families. Based on comparison of these scores with those derived from analysis of separate ranks of several multi-genera virus families, like the Picornaviridae, a revision of the Coronaviridae taxonomy is proposed. We suggest the Coronavirus and Torovirus genera to be re-defined as two subfamilies within the Coronavirdae or two families within Nidovirales, and the current three informal coronavirus groups to be converted into three genera within the Coronaviridae.
Po Tien - One of the best experts on this subject based on the ideXlab platform.
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following the rule formation of the 6 helix bundle of the fusion core from severe acute respiratory syndrome coronavirus spike protein and identification of potent peptide inhibitors
Biochemical and Biophysical Research Communications, 2004Co-Authors: Gengfu Xiao, Yanhui Xu, Fang Yuan, Congyi Zheng, David K Cole, John I Bell, Po TienAbstract:Severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV) is a newly identified member of Family Coronaviridae. Coronavirus envelope spike protein S is a class I viral fusion protein which is characterized by the existence of two heptad repeat regions (HR1 and HR2) (forming a complex called fusion core). Here we report that by using in vitro bio-engineering techniques, SARS-CoV HR1 and HR2 bind to each other and form a typical 6-helix bundle. The HR2, either as a synthetic peptide or as a GST-fusion polypeptide, is a potent inhibitor of virus entry. The results do show that SARS-CoV follows the general fusion mechanism of class I viruses and this lays the ground for identification of virus fusion/entry inhibitors for this devastating emerging virus.
Bruno Canard - One of the best experts on this subject based on the ideXlab platform.
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the severe acute respiratory syndrome coronavirus replicative protein nsp9 is a single stranded rna binding subunit unique in the rna virus world
Proceedings of the National Academy of Sciences of the United States of America, 2004Co-Authors: Marie-pierre Egloff, Helene Dutartre, Eric J. Snijder, Francois Ferron, Corinne Rancurel, Alexander E Gorbalenya, Sonia Longhi, Christian Cambillau, Valerie Campanacci, Bruno CanardAbstract:The recently identified etiological agent of the severe acute respiratory syndrome (SARS) belongs to Coronaviridae (CoV), a family of viruses replicating by a poorly understood mechanism. Here, we report the crystal structure at 2.7-A resolution of nsp9, a hitherto uncharacterized subunit of the SARS-CoV replicative polyproteins. We show that SARS-CoV nsp9 is a single-stranded RNA-binding protein displaying a previously unreported, oligosaccharide/oligonucleotide fold-like fold. The presence of this type of protein has not been detected in the replicative complexes of RNA viruses, and its presence may reflect the unique and complex CoV viral replication/transcription machinery.
Marie-pierre Egloff - One of the best experts on this subject based on the ideXlab platform.
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the severe acute respiratory syndrome coronavirus replicative protein nsp9 is a single stranded rna binding subunit unique in the rna virus world
Proceedings of the National Academy of Sciences of the United States of America, 2004Co-Authors: Marie-pierre Egloff, Helene Dutartre, Eric J. Snijder, Francois Ferron, Corinne Rancurel, Alexander E Gorbalenya, Sonia Longhi, Christian Cambillau, Valerie Campanacci, Bruno CanardAbstract:The recently identified etiological agent of the severe acute respiratory syndrome (SARS) belongs to Coronaviridae (CoV), a family of viruses replicating by a poorly understood mechanism. Here, we report the crystal structure at 2.7-A resolution of nsp9, a hitherto uncharacterized subunit of the SARS-CoV replicative polyproteins. We show that SARS-CoV nsp9 is a single-stranded RNA-binding protein displaying a previously unreported, oligosaccharide/oligonucleotide fold-like fold. The presence of this type of protein has not been detected in the replicative complexes of RNA viruses, and its presence may reflect the unique and complex CoV viral replication/transcription machinery.
Helene Dutartre - One of the best experts on this subject based on the ideXlab platform.
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the crystal structures of chikungunya and venezuelan equine encephalitis virus nsp3 macro domains define a conserved adenosine binding pocket
Journal of Virology, 2009Co-Authors: Helene Dutartre, Helene Malet, Bruno Coutard, S Jamal, Nicolas Papageorgiou, Maarit Neuvonen, Tero Ahola, Naomi L ForresterAbstract:Macro domains (also called "X domains") constitute a protein module family present in all kingdoms of life, including viruses of the Coronaviridae and Togaviridae families. Crystal structures of the macro domain from the Chikungunya virus (an "Old World" alphavirus) and the Venezuelan equine encephalitis virus (a "New World" alphavirus) were determined at resolutions of 1.65 and 2.30 A, respectively. These domains are active as adenosine di-phosphoribose 1''-phosphate phosphatases. Both the Chikungunya and the Venezuelan equine encephalitis virus macro domains are ADP-ribose binding modules, as revealed by structural and functional analysis. A single aspartic acid conserved through all macro domains is responsible for the specific binding of the adenine base. Sequence-unspecific binding to long, negatively charged polymers such as poly(ADP-ribose), DNA, and RNA is observed and attributed to positively charged patches outside of the active site pocket, as judged by mutagenesis and binding studies. The crystal structure of the Chikungunya virus macro domain with an RNA trimer shows a binding mode utilizing the same adenine-binding pocket as ADP-ribose, but avoiding the ADP-ribose 1''-phosphate phosphatase active site. This leaves the AMP binding site as the sole common feature in all macro domains.
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the severe acute respiratory syndrome coronavirus replicative protein nsp9 is a single stranded rna binding subunit unique in the rna virus world
Proceedings of the National Academy of Sciences of the United States of America, 2004Co-Authors: Marie-pierre Egloff, Helene Dutartre, Eric J. Snijder, Francois Ferron, Corinne Rancurel, Alexander E Gorbalenya, Sonia Longhi, Christian Cambillau, Valerie Campanacci, Bruno CanardAbstract:The recently identified etiological agent of the severe acute respiratory syndrome (SARS) belongs to Coronaviridae (CoV), a family of viruses replicating by a poorly understood mechanism. Here, we report the crystal structure at 2.7-A resolution of nsp9, a hitherto uncharacterized subunit of the SARS-CoV replicative polyproteins. We show that SARS-CoV nsp9 is a single-stranded RNA-binding protein displaying a previously unreported, oligosaccharide/oligonucleotide fold-like fold. The presence of this type of protein has not been detected in the replicative complexes of RNA viruses, and its presence may reflect the unique and complex CoV viral replication/transcription machinery.
