The Experts below are selected from a list of 33228 Experts worldwide ranked by ideXlab platform
Shinji Makino - One of the best experts on this subject based on the ideXlab platform.
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interplay between coronavirus a cytoplasmic rna virus and nonsense mediated mrna decay pathway
Proceedings of the National Academy of Sciences of the United States of America, 2018Co-Authors: Masami Wada, Krishna Narayanan, Kumari Lokugamage, Keisuke Nakagawa, Shinji MakinoAbstract:Coronaviruses (CoVs), including severe acute respiratory syndrome CoV and Middle East respiratory syndrome CoV, are enveloped RNA viruses that carry a large positive-sense single-stranded RNA genome and cause a variety of diseases in humans and domestic animals. Very little is known about the host pathways that regulate the stability of CoV mRNAs, which carry some unusual features. Nonsense-mediated decay (NMD) is a eukaryotic RNA surveillance pathway that detects mRNAs harboring aberrant features and targets them for degradation. Although CoV mRNAs are of cytoplasmic origin, the presence of several NMD-inducing features (including multiple ORFs with internal termination codons that create a long 3′ untranslated region) in CoV mRNAs led us to explore the interplay between the NMD pathway and CoVs. Our study using murine hepatitis virus as a model CoV showed that CoV mRNAs are recognized by the NMD pathway as a substrate, resulting in their degradation. Furthermore, CoV replication induced the inhibition of the NMD pathway, and N Protein (a Viral Structural Protein) had an NMD inhibitory function that protected Viral mRNAs from rapid decay. Our data further suggest that the NMD pathway interferes with optimal Viral replication by degrading Viral mRNAs early in infection, before sufficient accumulation of N Protein. Our study presents clear evidence for the biological importance of the NMD pathway in controlling the stability of mRNAs and the efficiency of replication of a cytoplasmic RNA virus.
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Severe Acute Respiratory Syndrome Coronavirus 7a Accessory Protein Is a Viral Structural Protein
Journal of Virology, 2006Co-Authors: Cheng Huang, Naoto Ito, Chien-te K. Tseng, Shinji MakinoAbstract:Severe acute respiratory syndrome coronavirus (SCoV) 7a Protein is one of the Viral accessory Proteins. In expressing cells, 7a Protein exhibits a variety of biological activities, including induction of apoptosis, activation of the mitogen-activated Protein kinase signaling pathway, inhibition of host Protein translation, and suppression of cell growth progression. Analysis of SCoV particles that were purified by either sucrose gradient equilibrium centrifugation or a virus capture assay, in which intact SCoV particles were specifically immunoprecipitated by anti-S Protein monoclonal antibody, demonstrated that 7a Protein was associated with purified SCoV particles. Coexpression of 7a Protein with SCoV S, M, N, and E Proteins resulted in production of virus-like particles (VLPs) carrying 7a Protein, while 7a Protein was not released from cells expressing 7a Protein alone. Although interaction between 7a Protein and another SCoV accessory Protein, 3a, has been reported, 3a Protein was dispensable for assembly of 7a Protein into VLPs. S Protein was not required for the 7a Protein incorporation into VLPs, and yet 7a Protein interacted with S Protein in coexpressing cells. These data established that, in addition to 3a Protein, 7a Protein was a SCoV accessory Protein identified as a SCoV Structural Protein.
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severe acute respiratory syndrome coronavirus 3a Protein is a Viral Structural Protein
Journal of Virology, 2005Co-Authors: Naoto Ito, Eric C Mossel, Krishna Narayanan, Clarence J. Peters, Taisuke Inoue, Vsevolod L. Popov, Cheng Huang, Shinji MakinoAbstract:The present study showed the association of a severe acute respiratory syndrome coronavirus (SCoV) accessory Protein, 3a, with plasma membrane and intracellular SCoV particles in infected cells. 3a Protein appeared to undergo posttranslational modifications in infected cells and was incorporated into SCoV particles, establishing that 3a Protein was a SCoV Structural Protein.
S M Matsui - One of the best experts on this subject based on the ideXlab platform.
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analysis of astrovirus serotype 1 rna identification of the Viral rna dependent rna polymerase motif and expression of a Viral Structural Protein
Journal of Virology, 1994Co-Authors: T L Lewis, Harry B Greenberg, John E Herrmann, L S Smith, S M MatsuiAbstract:We report the results from sequence analysis and expression studies of the gastroenteritis agent astrovirus serotype 1. We have cloned and sequenced 5,944 nucleotides (nt) of the estimated 7.2-kb RNA genome and have identified three open reading frames (ORFs). ORF-3, at the 39 end, is 2,361 nt in length and is fully encoded in both the genomic and subgenomic Viral RNAs. Expression of ORF-3 in vitro yields an 87-kDa Protein that is immunoprecipitated with a monoclonal antibody specific for Viral capsids. This Protein comigrates with an authentic 87-kDa astrovirus Protein immunoprecipitated from infected cells, indicating that this region encodes a Viral Structural Protein. The adjacent upstream ORF (ORF-2) is 1,557 nt in length and contains a Viral RNA-dependent RNA polymerase motif. The Viral RNA-dependent RNA polymerase motifs from four astrovirus serotypes are compared. Partial sequence (2,018 nt) of the most 59 ORF (ORF-1) reveals a 3C-like serine protease motif. The ORF-1 sequence is incomplete. These results indicate that the astrovirus genome is organized with nonStructural Proteins encoded at the 59 end and Structural Proteins at the 39 end. ORF-2 has no start methionine and is in the -1 frame compared with ORF-1. We present sequence evidence for a ribosomal frameshift mechanism for expression of the Viral polymerase. Images
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analysis of astrovirus serotype 1 rna identification of the Viral rna dependent rna polymerase motif and expression of a Viral Structural Protein
Journal of Virology, 1994Co-Authors: T L Lewis, Harry B Greenberg, John E Herrmann, L S Smith, S M MatsuiAbstract:Abstract We report the results from sequence analysis and expression studies of the gastroenteritis agent astrovirus serotype 1. We have cloned and sequenced 5,944 nucleotides (nt) of the estimated 7.2-kb RNA genome and have identified three open reading frames (ORFs). ORF-3, at the 3' end, is 2,361 nt in length and is fully encoded in both the genomic and subgenomic Viral RNAs. Expression of ORF-3 in vitro yields an 87-kDa Protein that is immunoprecipitated with a monoclonal antibody specific for Viral capsids. This Protein comigrates with an authentic 87-kDa astrovirus Protein immunoprecipitated from infected cells, indicating that this region encodes a Viral Structural Protein. The adjacent upstream ORF (ORF-2) is 1,557 nt in length and contains a Viral RNA-dependent RNA polymerase motif. The Viral RNA-dependent RNA polymerase motifs from four astrovirus serotypes are compared. Partial sequence (2,018 nt) of the most 5' ORF (ORF-1) reveals a 3C-like serine protease motif. The ORF-1 sequence is incomplete. These results indicate that the astrovirus genome is organized with nonStructural Proteins encoded at the 5' end and Structural Proteins at the 3' end. ORF-2 has no start methionine and is in the -1 frame compared with ORF-1. We present sequence evidence for a ribosomal frameshift mechanism for expression of the Viral polymerase.
Naoto Ito - One of the best experts on this subject based on the ideXlab platform.
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Severe Acute Respiratory Syndrome Coronavirus 7a Accessory Protein Is a Viral Structural Protein
Journal of Virology, 2006Co-Authors: Cheng Huang, Naoto Ito, Chien-te K. Tseng, Shinji MakinoAbstract:Severe acute respiratory syndrome coronavirus (SCoV) 7a Protein is one of the Viral accessory Proteins. In expressing cells, 7a Protein exhibits a variety of biological activities, including induction of apoptosis, activation of the mitogen-activated Protein kinase signaling pathway, inhibition of host Protein translation, and suppression of cell growth progression. Analysis of SCoV particles that were purified by either sucrose gradient equilibrium centrifugation or a virus capture assay, in which intact SCoV particles were specifically immunoprecipitated by anti-S Protein monoclonal antibody, demonstrated that 7a Protein was associated with purified SCoV particles. Coexpression of 7a Protein with SCoV S, M, N, and E Proteins resulted in production of virus-like particles (VLPs) carrying 7a Protein, while 7a Protein was not released from cells expressing 7a Protein alone. Although interaction between 7a Protein and another SCoV accessory Protein, 3a, has been reported, 3a Protein was dispensable for assembly of 7a Protein into VLPs. S Protein was not required for the 7a Protein incorporation into VLPs, and yet 7a Protein interacted with S Protein in coexpressing cells. These data established that, in addition to 3a Protein, 7a Protein was a SCoV accessory Protein identified as a SCoV Structural Protein.
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severe acute respiratory syndrome coronavirus 3a Protein is a Viral Structural Protein
Journal of Virology, 2005Co-Authors: Naoto Ito, Eric C Mossel, Krishna Narayanan, Clarence J. Peters, Taisuke Inoue, Vsevolod L. Popov, Cheng Huang, Shinji MakinoAbstract:The present study showed the association of a severe acute respiratory syndrome coronavirus (SCoV) accessory Protein, 3a, with plasma membrane and intracellular SCoV particles in infected cells. 3a Protein appeared to undergo posttranslational modifications in infected cells and was incorporated into SCoV particles, establishing that 3a Protein was a SCoV Structural Protein.
T L Lewis - One of the best experts on this subject based on the ideXlab platform.
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analysis of astrovirus serotype 1 rna identification of the Viral rna dependent rna polymerase motif and expression of a Viral Structural Protein
Journal of Virology, 1994Co-Authors: T L Lewis, Harry B Greenberg, John E Herrmann, L S Smith, S M MatsuiAbstract:We report the results from sequence analysis and expression studies of the gastroenteritis agent astrovirus serotype 1. We have cloned and sequenced 5,944 nucleotides (nt) of the estimated 7.2-kb RNA genome and have identified three open reading frames (ORFs). ORF-3, at the 39 end, is 2,361 nt in length and is fully encoded in both the genomic and subgenomic Viral RNAs. Expression of ORF-3 in vitro yields an 87-kDa Protein that is immunoprecipitated with a monoclonal antibody specific for Viral capsids. This Protein comigrates with an authentic 87-kDa astrovirus Protein immunoprecipitated from infected cells, indicating that this region encodes a Viral Structural Protein. The adjacent upstream ORF (ORF-2) is 1,557 nt in length and contains a Viral RNA-dependent RNA polymerase motif. The Viral RNA-dependent RNA polymerase motifs from four astrovirus serotypes are compared. Partial sequence (2,018 nt) of the most 59 ORF (ORF-1) reveals a 3C-like serine protease motif. The ORF-1 sequence is incomplete. These results indicate that the astrovirus genome is organized with nonStructural Proteins encoded at the 59 end and Structural Proteins at the 39 end. ORF-2 has no start methionine and is in the -1 frame compared with ORF-1. We present sequence evidence for a ribosomal frameshift mechanism for expression of the Viral polymerase. Images
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analysis of astrovirus serotype 1 rna identification of the Viral rna dependent rna polymerase motif and expression of a Viral Structural Protein
Journal of Virology, 1994Co-Authors: T L Lewis, Harry B Greenberg, John E Herrmann, L S Smith, S M MatsuiAbstract:Abstract We report the results from sequence analysis and expression studies of the gastroenteritis agent astrovirus serotype 1. We have cloned and sequenced 5,944 nucleotides (nt) of the estimated 7.2-kb RNA genome and have identified three open reading frames (ORFs). ORF-3, at the 3' end, is 2,361 nt in length and is fully encoded in both the genomic and subgenomic Viral RNAs. Expression of ORF-3 in vitro yields an 87-kDa Protein that is immunoprecipitated with a monoclonal antibody specific for Viral capsids. This Protein comigrates with an authentic 87-kDa astrovirus Protein immunoprecipitated from infected cells, indicating that this region encodes a Viral Structural Protein. The adjacent upstream ORF (ORF-2) is 1,557 nt in length and contains a Viral RNA-dependent RNA polymerase motif. The Viral RNA-dependent RNA polymerase motifs from four astrovirus serotypes are compared. Partial sequence (2,018 nt) of the most 5' ORF (ORF-1) reveals a 3C-like serine protease motif. The ORF-1 sequence is incomplete. These results indicate that the astrovirus genome is organized with nonStructural Proteins encoded at the 5' end and Structural Proteins at the 3' end. ORF-2 has no start methionine and is in the -1 frame compared with ORF-1. We present sequence evidence for a ribosomal frameshift mechanism for expression of the Viral polymerase.
Harry B Greenberg - One of the best experts on this subject based on the ideXlab platform.
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analysis of astrovirus serotype 1 rna identification of the Viral rna dependent rna polymerase motif and expression of a Viral Structural Protein
Journal of Virology, 1994Co-Authors: T L Lewis, Harry B Greenberg, John E Herrmann, L S Smith, S M MatsuiAbstract:We report the results from sequence analysis and expression studies of the gastroenteritis agent astrovirus serotype 1. We have cloned and sequenced 5,944 nucleotides (nt) of the estimated 7.2-kb RNA genome and have identified three open reading frames (ORFs). ORF-3, at the 39 end, is 2,361 nt in length and is fully encoded in both the genomic and subgenomic Viral RNAs. Expression of ORF-3 in vitro yields an 87-kDa Protein that is immunoprecipitated with a monoclonal antibody specific for Viral capsids. This Protein comigrates with an authentic 87-kDa astrovirus Protein immunoprecipitated from infected cells, indicating that this region encodes a Viral Structural Protein. The adjacent upstream ORF (ORF-2) is 1,557 nt in length and contains a Viral RNA-dependent RNA polymerase motif. The Viral RNA-dependent RNA polymerase motifs from four astrovirus serotypes are compared. Partial sequence (2,018 nt) of the most 59 ORF (ORF-1) reveals a 3C-like serine protease motif. The ORF-1 sequence is incomplete. These results indicate that the astrovirus genome is organized with nonStructural Proteins encoded at the 59 end and Structural Proteins at the 39 end. ORF-2 has no start methionine and is in the -1 frame compared with ORF-1. We present sequence evidence for a ribosomal frameshift mechanism for expression of the Viral polymerase. Images
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analysis of astrovirus serotype 1 rna identification of the Viral rna dependent rna polymerase motif and expression of a Viral Structural Protein
Journal of Virology, 1994Co-Authors: T L Lewis, Harry B Greenberg, John E Herrmann, L S Smith, S M MatsuiAbstract:Abstract We report the results from sequence analysis and expression studies of the gastroenteritis agent astrovirus serotype 1. We have cloned and sequenced 5,944 nucleotides (nt) of the estimated 7.2-kb RNA genome and have identified three open reading frames (ORFs). ORF-3, at the 3' end, is 2,361 nt in length and is fully encoded in both the genomic and subgenomic Viral RNAs. Expression of ORF-3 in vitro yields an 87-kDa Protein that is immunoprecipitated with a monoclonal antibody specific for Viral capsids. This Protein comigrates with an authentic 87-kDa astrovirus Protein immunoprecipitated from infected cells, indicating that this region encodes a Viral Structural Protein. The adjacent upstream ORF (ORF-2) is 1,557 nt in length and contains a Viral RNA-dependent RNA polymerase motif. The Viral RNA-dependent RNA polymerase motifs from four astrovirus serotypes are compared. Partial sequence (2,018 nt) of the most 5' ORF (ORF-1) reveals a 3C-like serine protease motif. The ORF-1 sequence is incomplete. These results indicate that the astrovirus genome is organized with nonStructural Proteins encoded at the 5' end and Structural Proteins at the 3' end. ORF-2 has no start methionine and is in the -1 frame compared with ORF-1. We present sequence evidence for a ribosomal frameshift mechanism for expression of the Viral polymerase.
