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Alan D T Barrett - One of the best experts on this subject based on the ideXlab platform.
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solution structure of the Envelope Protein domain iii of dengue 4 virus
Virology, 2007Co-Authors: David E Volk, David W. C. Beasley, Alan D T Barrett, Yi Chien Lee, Varatharasa Thiviyanathan, Gregory D Gromowski, Ashley R Lamb, David G. GorensteinAbstract:The disease dengue (DEN) is caused by four serologically related viruses termed DEN1, DEN2, DEN3 and DEN4. The structure of the ectodomain of the Envelope Protein has been determined previously for DEN2 and DEN3 viruses. Using NMR spectroscopic methods, we solved the solution structure of domain III (ED3), the receptor-binding domain, of the Envelope Protein of DEN4 virus, human strain 703-4. The structure shows that the nine amino acid changes in ED3 that separate the sylvatic and human DEN4 strains are surface exposed. Important structural differences between DEN4-rED3 and ED3 domains of DEN2, DEN3 and other flaviviruses are discussed.
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a mutation in the Envelope Protein fusion loop attenuates mouse neuroinvasiveness of the ny99 strain of west nile virus
Virology, 2006Co-Authors: Shuliu Zhang, Alan D T Barrett, Claire Y H Huang, Richard M Kinney, Li Li, Sara E Woodson, David W. C. BeasleyAbstract:Substitutions were engineered individually and in combinations at the fusion loop, receptor-binding domain and a stem-helix structure of the Envelope Protein of a West Nile virus strain, NY99, and their effects on mouse virulence and presentation of epitopes recognized by monoclonal antibodies (MAbs) were assessed. A single substitution within the fusion loop (L107F) attenuated mouse neuroinvasiveness of NY99. No substitutions attenuated NY99 neurovirulence. The L107F mutation also abolished binding of a non-neutralizing MAb, 3D9, whose epitope had not been previously identified. MAb 3D9 was subsequently shown to be broadly cross-reactive with other flaviviruses, consistent with binding near the highly conserved fusion loop.
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structure of the Envelope Protein domain iii of omsk hemorrhagic fever virus
Virology, 2006Co-Authors: David E Volk, Leonard Chavez, Michael R Holbrook, David W. C. Beasley, Alan D T Barrett, David G. GorensteinAbstract:We have solved the NMR solution structure of domain III from the Omsk hemorrhagic fever virus Envelope Protein and report the first sequencing of the Guriev strain of this virus. Important structural differences between tick-borne flaviviruses, such as OHFV and TBE, and mosquito-borne flaviviruses, such as West Nile virus, are discussed.
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Envelope Protein glycosylation status influences mouse neuroinvasion phenotype of genetic lineage 1 west nile virus strains
Journal of Virology, 2005Co-Authors: David W. C. Beasley, Gregory D Gromowski, Melissa C Whiteman, Shuliu Zhang, Claire Y H Huang, B Schneider, Darci R Smith, Stephen Higgs, Richard M Kinney, Alan D T BarrettAbstract:The introduction of West Nile virus (WNV) into North America has been associated with relatively high rates of neurological disease and death in humans, birds, horses, and some other animals. Previous studies identified strains in both genetic lineage 1 and genetic lineage 2, including North American isolates of lineage 1, that were highly virulent in a mouse neuroinvasion model, while other strains were avirulent or significantly attenuated (D. W. C. Beasley, L. Li, M. T. Suderman, and A. D. T. Barrett, Virology 296:17-23, 2002). To begin to elucidate the basis for these differences, we compared a highly virulent New York 1999 (NY99) isolate with a related Old World lineage 1 strain, An4766 (ETH76a), which is attenuated for mouse neuroinvasion. Genomic sequencing of ETH76a revealed a relatively small number of nucleotide (5.1%) and amino acid (0.6%) differences compared with NY99. These differences were located throughout the genome and included five amino acid differences in the Envelope Protein gene. Substitution of premembrane and Envelope genes of ETH76a into a NY99 infectious clone backbone yielded a virus with altered in vitro growth characteristics and a mouse virulence phenotype comparable to ETH76a. Further site-specific mutagenesis studies revealed that the altered phenotype was primarily mediated via loss of Envelope Protein glycosylation and that this was associated with altered stability of the virion at mildly acidic pH. Therefore, the enhanced virulence of North American WNV strains compared with other Old World lineage 1 strains is at least partly mediated by Envelope Protein glycosylation.
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identification of neutralizing epitopes within structural domain iii of the west nile virus Envelope Protein
Journal of Virology, 2002Co-Authors: David W. C. Beasley, Alan D T BarrettAbstract:Using a panel of neutralizing monoclonal antibodies, we have mapped epitopes in domain III of the Envelope Protein of the New York strain of West Nile virus. The ability of monoclonal antibodies that recognize these epitopes to neutralize virus appeared to differ between lineage I and II West Nile virus strains, and epitopes were located on the upper surface of domain III at residues E307, E330, and E332.
David W. C. Beasley - One of the best experts on this subject based on the ideXlab platform.
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solution structure of the Envelope Protein domain iii of dengue 4 virus
Virology, 2007Co-Authors: David E Volk, David W. C. Beasley, Alan D T Barrett, Yi Chien Lee, Varatharasa Thiviyanathan, Gregory D Gromowski, Ashley R Lamb, David G. GorensteinAbstract:The disease dengue (DEN) is caused by four serologically related viruses termed DEN1, DEN2, DEN3 and DEN4. The structure of the ectodomain of the Envelope Protein has been determined previously for DEN2 and DEN3 viruses. Using NMR spectroscopic methods, we solved the solution structure of domain III (ED3), the receptor-binding domain, of the Envelope Protein of DEN4 virus, human strain 703-4. The structure shows that the nine amino acid changes in ED3 that separate the sylvatic and human DEN4 strains are surface exposed. Important structural differences between DEN4-rED3 and ED3 domains of DEN2, DEN3 and other flaviviruses are discussed.
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a mutation in the Envelope Protein fusion loop attenuates mouse neuroinvasiveness of the ny99 strain of west nile virus
Virology, 2006Co-Authors: Shuliu Zhang, Alan D T Barrett, Claire Y H Huang, Richard M Kinney, Li Li, Sara E Woodson, David W. C. BeasleyAbstract:Substitutions were engineered individually and in combinations at the fusion loop, receptor-binding domain and a stem-helix structure of the Envelope Protein of a West Nile virus strain, NY99, and their effects on mouse virulence and presentation of epitopes recognized by monoclonal antibodies (MAbs) were assessed. A single substitution within the fusion loop (L107F) attenuated mouse neuroinvasiveness of NY99. No substitutions attenuated NY99 neurovirulence. The L107F mutation also abolished binding of a non-neutralizing MAb, 3D9, whose epitope had not been previously identified. MAb 3D9 was subsequently shown to be broadly cross-reactive with other flaviviruses, consistent with binding near the highly conserved fusion loop.
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structure of the Envelope Protein domain iii of omsk hemorrhagic fever virus
Virology, 2006Co-Authors: David E Volk, Leonard Chavez, Michael R Holbrook, David W. C. Beasley, Alan D T Barrett, David G. GorensteinAbstract:We have solved the NMR solution structure of domain III from the Omsk hemorrhagic fever virus Envelope Protein and report the first sequencing of the Guriev strain of this virus. Important structural differences between tick-borne flaviviruses, such as OHFV and TBE, and mosquito-borne flaviviruses, such as West Nile virus, are discussed.
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Envelope Protein glycosylation status influences mouse neuroinvasion phenotype of genetic lineage 1 west nile virus strains
Journal of Virology, 2005Co-Authors: David W. C. Beasley, Gregory D Gromowski, Melissa C Whiteman, Shuliu Zhang, Claire Y H Huang, B Schneider, Darci R Smith, Stephen Higgs, Richard M Kinney, Alan D T BarrettAbstract:The introduction of West Nile virus (WNV) into North America has been associated with relatively high rates of neurological disease and death in humans, birds, horses, and some other animals. Previous studies identified strains in both genetic lineage 1 and genetic lineage 2, including North American isolates of lineage 1, that were highly virulent in a mouse neuroinvasion model, while other strains were avirulent or significantly attenuated (D. W. C. Beasley, L. Li, M. T. Suderman, and A. D. T. Barrett, Virology 296:17-23, 2002). To begin to elucidate the basis for these differences, we compared a highly virulent New York 1999 (NY99) isolate with a related Old World lineage 1 strain, An4766 (ETH76a), which is attenuated for mouse neuroinvasion. Genomic sequencing of ETH76a revealed a relatively small number of nucleotide (5.1%) and amino acid (0.6%) differences compared with NY99. These differences were located throughout the genome and included five amino acid differences in the Envelope Protein gene. Substitution of premembrane and Envelope genes of ETH76a into a NY99 infectious clone backbone yielded a virus with altered in vitro growth characteristics and a mouse virulence phenotype comparable to ETH76a. Further site-specific mutagenesis studies revealed that the altered phenotype was primarily mediated via loss of Envelope Protein glycosylation and that this was associated with altered stability of the virion at mildly acidic pH. Therefore, the enhanced virulence of North American WNV strains compared with other Old World lineage 1 strains is at least partly mediated by Envelope Protein glycosylation.
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identification of neutralizing epitopes within structural domain iii of the west nile virus Envelope Protein
Journal of Virology, 2002Co-Authors: David W. C. Beasley, Alan D T BarrettAbstract:Using a panel of neutralizing monoclonal antibodies, we have mapped epitopes in domain III of the Envelope Protein of the New York strain of West Nile virus. The ability of monoclonal antibodies that recognize these epitopes to neutralize virus appeared to differ between lineage I and II West Nile virus strains, and epitopes were located on the upper surface of domain III at residues E307, E330, and E332.
Choy L Hew - One of the best experts on this subject based on the ideXlab platform.
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characterization of a novel Envelope Protein wsv010 of shrimp white spot syndrome virus and its interaction with a major viral structural Protein vp24
Virology, 2007Co-Authors: Jing Chen, Choy L HewAbstract:White spot syndrome virus is one of the most serious viral pathogens causing huge mortality in shrimp farming. Here we report characterization of WSV010, a novel structural Protein identified by our recent shotgun proteomics study. Its ORF contains 294 nucleotides encoding 97 amino acids. Transcription analysis using RT-PCR showed that wsv010 is a late gene. Localization analyses by Western blot and immunoelectron microscopy demonstrated that WSV010 is a viral Envelope Protein. Furthermore, the pull-down assay revealed that WSV010 could interact with VP24, which is a major Envelope Protein. Since WSV010 lacks a transmembrane domain, these results suggest that WSV010 may anchor to the Envelope through interaction with VP24. Previous studies indicated that VP24 could also interact with VP28 and VP26. Therefore, we propose that VP24 may act as a linker Protein to associate these Envelope Proteins together to form a complex, which may play an important role in viral morphogenesis and viral infection.
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identification and localization of a prawn white spot syndrome virus gene that encodes an Envelope Protein
Journal of General Virology, 2002Co-Authors: Xiaobo Zhang, Canhua Huang, Choy L HewAbstract:Among the important challenges to shrimp aquaculture worldwide are the diseases caused by viruses, in particular by white spot syndrome virus (WSSV), which has a genome estimated to contain 305 kb. By analysis and comparison of the WSSV genomic DNA and cDNA libraries, an ORF (vp28 gene) was identified. The gene, encoding a novel 204-amino-acid Protein, was expressed in Escherichia coli and purified. A specific antibody was raised using the purified VP28 Protein. After inoculation of healthy adult Penaeus monodon shrimp with WSSV, the gene transcript and VP28 Protein were first detected at low levels at 6 and 18 h post-infection, respectively. These experiments suggest that it might be a late gene. Immuno-electron microscopy with gold-labelled antibody revealed that the gold particles were distributed in the outer Envelope of WSSV virions and showed that vp28 encodes a virus Envelope Protein.
Xiaobo Zhang - One of the best experts on this subject based on the ideXlab platform.
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identification and localization of a prawn white spot syndrome virus gene that encodes an Envelope Protein
Journal of General Virology, 2002Co-Authors: Xiaobo Zhang, Canhua Huang, Choy L HewAbstract:Among the important challenges to shrimp aquaculture worldwide are the diseases caused by viruses, in particular by white spot syndrome virus (WSSV), which has a genome estimated to contain 305 kb. By analysis and comparison of the WSSV genomic DNA and cDNA libraries, an ORF (vp28 gene) was identified. The gene, encoding a novel 204-amino-acid Protein, was expressed in Escherichia coli and purified. A specific antibody was raised using the purified VP28 Protein. After inoculation of healthy adult Penaeus monodon shrimp with WSSV, the gene transcript and VP28 Protein were first detected at low levels at 6 and 18 h post-infection, respectively. These experiments suggest that it might be a late gene. Immuno-electron microscopy with gold-labelled antibody revealed that the gold particles were distributed in the outer Envelope of WSSV virions and showed that vp28 encodes a virus Envelope Protein.
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transcription and identification of an Envelope Protein gene p22 from shrimp white spot syndrome virus
Journal of General Virology, 2002Co-Authors: Xiaobo Zhang, Canhua Huang, Xun XuAbstract:White spot syndrome virus (WSSV) is one of the most virulent pathogens causing high mortality in shrimp. In the present study, an open reading frame (termed the p22 gene) was revealed from a WSSV cDNA library. The gene was expressed as a fusion Protein with glutathione S-transferase (GST) in Escherichia coli and purified. Specific antibody was raised using the purified fusion Protein (GST–P22). Temporal analysis showed that the p22 gene was a late gene. After binding between purified WSSV virions and anti-GST–P22 IgG followed by labelling with gold-labelled secondary antibody, the gold particles, under a transmission electron microscope, could be found along the outer Envelope of WSSV virions. This experiment suggests that the p22 gene encodes an Envelope Protein of the virus.
Jyawei Cheng - One of the best experts on this subject based on the ideXlab platform.
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structural basis of a flavivirus recognized by its neutralizing antibody solution structure of the domain iii of the japanese encephalitis virus Envelope Protein
Journal of Biological Chemistry, 2003Co-Authors: Kuenphon Wu, Chihwei Wu, Yaping Tsao, Suhchin Wu, Jyawei ChengAbstract:Abstract The flavivirus Envelope Protein is the dominant antigen in eliciting neutralizing antibodies and plays an important role in inducing immunologic responses in the infected host. We have determined the solution structure of the major antigenic domain (domain III) of the Japanese encephalitis virus (JEV) Envelope Protein. The JEV domain III forms a β-barrel type structure composed of six antiparallel β-strands resembling the immunoglobulin constant domain. We have also identified epitopes of the JEV domain III to its neutralizing antibody by chemical shift perturbation measurements. Site-directed mutagenesis experiments are performed to confirm the NMR results. Our study provides a structural basis for understanding the mechanism of immunologic protection and for rational design of vaccines effective against flaviviruses.
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structural basis of a flavivirus recognized by its neutralizing antibody solution structure of the domain iii of the japanese encephalitis virus Envelope Protein
Journal of Biological Chemistry, 2003Co-Authors: Yaping Tsao, Tingwei Kuo, Yuanchao Lou, Cheng Wen Lin, Jyawei ChengAbstract:The flavivirus Envelope Protein is the dominant antigen in eliciting neutralizing antibodies and plays an important role in inducing immunologic responses in the infected host. We have determined the solution structure of the major antigenic domain (domain III) of the Japanese encephalitis virus (JEV) Envelope Protein. The JEV domain III forms a beta-barrel type structure composed of six antiparallel beta-strands resembling the immunoglobulin constant domain. We have also identified epitopes of the JEV domain III to its neutralizing antibody by chemical shift perturbation measurements. Site-directed mutagenesis experiments are performed to confirm the NMR results. Our study provides a structural basis for understanding the mechanism of immunologic protection and for rational design of vaccines effective against flaviviruses.