The Experts below are selected from a list of 1257 Experts worldwide ranked by ideXlab platform
Victoria Ley - One of the best experts on this subject based on the ideXlab platform.
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Heparan sulphate mediates Swine Vesicular Disease virus attachment to the host cell
Journal of General Virology, 2004Co-Authors: Estela Escribano-romero, Miguel Angel Jiménez-clavero, Paula Gomes, Juan Antonio García-ranea, Victoria LeyAbstract:Heparan sulphate (HS) has been found to serve as receptor for initial cell binding of numerous viruses. Different glycosaminoglycans (GAGs), including heparin and HS, were analysed for their ability to bind Swine Vesicular Disease virus (SVDV), a picornavirus with close homology to human coxsackie B5 virus. Binding of SVDV was established by heparin-affinity chromatography. In addition, infection of IB-RS-2 epithelial porcine cells was inhibited by treating the virus with soluble HS, heparin, and chondroitin sulphate B (CS-B), as well as by enzymic digestion of cell surface GAGs. Analysis of the infection course showed that SVDV uses cellular HS for its binding to the cell surface and that this interaction occurs during attachment of the virus, prior to its internalization into the cell. Sequence analysis of SVDV variants selected for their lack of sensitivity to heparin inhibition in vitro led to the identification of two residues (A2135V and I1266K) potentially involved in heparin/HS interaction. The location of these residues in a three-dimensional model shows that they are clustered in a well-exposed region of the capsid, providing a physical mechanism that could account for the heparin-binding phenotype.
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STRUCTURE OF Swine Vesicular Disease VIRUS: MAPPING OF CHANGES OCCURRING DURING ADAPTATION OF HUMAN COXSACKIE B5 VIRUS TO INFECT Swine
Journal of virology, 2003Co-Authors: Núria Verdaguer, Miguel Angel Jiménez-clavero, Ignacio Fita, Victoria LeyAbstract:The structure of Swine Vesicular Disease virus (SVDV) was solved and refined at a 3.0-Aresolution by X-ray crystallography to gain information about the role of sequence changes that occurred as this virus evolved from the parental human pathogen coxsackievirus B5 (CVB5). These amino acid substitutions can be clustered in five distinct regions: (i) the antigenic sites, (ii) the hydrophobic pocket of the VP1 -sandwich, (iii) the putative CAR binding site, (iv) the putative heparan sulfate binding site, and (v) the fivefold axis. The VP1 pocket is occupied by a branched pocket factor, apparently different from that present in the closely related virus CVB3 and in other picornaviruses. This finding may be relevant for the design of new antiviral compounds against this site. Density consistent with the presence of ions was observed on the fivefold and threefold axes. The structure also provided an accurate description of the putative receptor binding sites. Swine Vesicular Disease virus (SVDV) is a member of the Enterovirus genus, within the Picornaviridae family. It causes a highly contagious Disease of pigs that spreads rapidly by direct contact among infected animals and by environmental contam- ination (12). It is not a severe Disease, although the similarity between the lesions it causes and those produced by foot-and- mouth Disease (FMD) has led to it being considered econom- ically important, and routine surveillance is maintained in Eu- ropean countries (reviewed in reference 13). The Disease was first described in Italy in 1966 (38), and numerous outbreaks have since occurred in Europe and Asia. SVDV is a porcine variant of the human pathogen coxsack-
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Crystallization and preliminary X-ray analysis of Swine Vesicular Disease virus (SVDV).
Acta Crystallographica Section D Biological Crystallography, 2003Co-Authors: Miguel Angel Jiménez-clavero, Victoria Ley, Ignacio Fita, Núria VerdaguerAbstract:Three different crystal forms of the Swine Vesicular Disease virus (SVDV), isolate SPA/2/'93, were obtained by the hanging-drop vapour-diffusion technique using ammonium sulfate and sodium/potassium phosphate as precipitants. Monoclinic crystals, space group C2, with unit-cell parameters a = 473.7, b = 385.3, c = 472.8 A, beta = 100.4 degrees, contain one virus pArticle in the crystal asymmetric unit and diffract to 3.0 A resolution. A second type of crystals had a cubic morphology and diffracted beyond 2.6 A resolution. These crystals belong to a primitive orthorhombic space group, with unit-cell parameters a = 319.6, b = 353.8, c = 377.7 A, and contain half a virus pArticle in the asymmetric unit. A third type of crystals, with a prismatic shape and belonging to space group I222, was also obtained under similar crystallization conditions. These latter crystals, with unit-cell parameters a = 318.3, b = 349.9, c = 371.7 A, diffract to at least 3.0 A resolution and contain 15 protomers per asymmetric unit; this requires that three perpendicular crystal twofold axes coincide with three of the viral pArticles' dyad axes.
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The N-Terminal Region of the VP1 Protein of Swine Vesicular Disease Virus Contains a Neutralization Site That Arises upon Cell Attachment and Is Involved in Viral Entry
Journal of virology, 2001Co-Authors: Miguel Angel Jiménez-clavero, Estela Escribano-romero, A. J. Douglas, Victoria LeyAbstract:The N-terminal region of VP1 of Swine Vesicular Disease virus (SVDV) is highly antigenic in Swine, despite its internal location in the capsid. Here we show that antibodies to this region can block infection and that allowing the virus to attach to cells increases this blockage significantly. The results indicate that upon binding to the cell, SVDV capsid undergoes a conformational change that is temperature independent and that exposes the N terminus of VP1. This process makes this region accessible to antibodies which block virus entry.
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Immune Recognition of Swine Vesicular Disease Virus Structural Proteins: Novel Antigenic Regions That Are Not Exposed in the Capsid
Virology, 2000Co-Authors: Miguel Angel Jiménez-clavero, Juan Antonio García-ranea, A. J. Douglas, T. Lavery, Victoria LeyAbstract:Swine Vesicular Disease virus (SVDV) is an enterovirus of the Picornaviridae family that belongs to the coxsackievirus B group. A number of antigenic sites have been identified in SVDV by analysis of neutralizing monoclonal antibody-resistant mutants and shown to be exposed on the surface of the capsid. In this paper we have identified seven new immunodominant antigenic regions in SVDV capsid proteins by a peptide scanning method, using a panel of sera from infected pigs. When these antigenic regions were located in the capsid by using a computer-generated three-dimensional model of the virion, one was readily exposed on the surface of the virus and the remaining sites were located facing the inner side of the capsid shell, at subunit contacts, or in the interior of the subunit structure.
Xiangtao Liu - One of the best experts on this subject based on the ideXlab platform.
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Expression and immunological analysis of capsid protein precursor of Swine Vesicular Disease virus HK/70
Virologica Sinica, 2010Co-Authors: Hong Tian, Haixue Zheng, Youjun Shang, Shuang-hui Ying, Xiangtao LiuAbstract:VP1, a capsid protein of Swine Vesicular Disease virus, was cloned from the SVDV HK/70 strain and inserted into retroviral vector pBABE puro, and expressed in PK15 cells by an retroviral expression system. The ability of the VP1 protein to induce an immune response was then evaluated in guinea pigs. Western blot and ELISA results indicated that the VP1 protein can be recognized by SVDV positive serum, Furthermore, anti-SVDV specific antibodies and lymphocyte proliferation were elicited and increased by VP1 protein after vaccination. These results encourage further work towards the development of a vaccine against SVDV infection.
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expression and immunological analysis of capsid protein precursor of Swine Vesicular Disease virus hk 70
Virologica Sinica, 2010Co-Authors: Hong Tian, Haixue Zheng, Youjun Shang, Shuang-hui Ying, Xiangtao LiuAbstract:VP1, a capsid protein of Swine Vesicular Disease virus, was cloned from the SVDV HK/70 strain and inserted into retroviral vector pBABE puro, and expressed in PK15 cells by an retroviral expression system. The ability of the VP1 protein to induce an immune response was then evaluated in guinea pigs. Western blot and ELISA results indicated that the VP1 protein can be recognized by SVDV positive serum, Furthermore, anti-SVDV specific antibodies and lymphocyte proliferation were elicited and increased by VP1 protein after vaccination. These results encourage further work towards the development of a vaccine against SVDV infection.
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Infective viruses produced from full-length complementary DNA of Swine Vesicular Disease viruses HK/70 strain.
Chinese science bulletin = Kexue tongbao, 2006Co-Authors: Haixue Zheng, Xiangtao Liu, Youjun Shang, Xing-wen Bai, Ye Jin, Shiqi Sun, Guo Huichen, Hong Tian, Xia FengAbstract:The full-length cDNA clone of Swine Vesicular Disease virus HK/70 strain named pSVOK12 was constructed in order to study the antigenicity, replication, maturation and pathogenicity of Swine Vesicular Disease virus. In vitro transcription RNA from pSVOK12 transfected IBRS-2 cells and the recovered virus RNA were isolated and sequenced, then indirect hemagglutination test, indirect immunofluorescence assays, eleectron microscope test, 50% tissue culture infecting dose (TCID50) assays and mouse virulence studies were performed to study the antigenicity and virulence of the recovered virus. The result showed that the infectious clones we obtained and the virus derived from pSVOK12 had the same biological properties as the parental strain HK/70. The full-length infectious cDNA clone, pSVOK12, will be very useful in studies of the antigenicity, virulence, pathogenesis, maturation and replication of SVDV.
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infective viruses produced from full length complementary dna of Swine Vesicular Disease viruses hk 70 strain
Chinese Science Bulletin, 2006Co-Authors: Haixue Zheng, Xiangtao Liu, Youjun Shang, Xing-wen Bai, Ye Jin, Shiqi Sun, Hong Tian, Xia Feng, Huichen Guo, Shuanghui YinAbstract:The full-length cDNA clone of Swine Vesicular Disease virus HK/70 strain named pSVOK12 was constructed in order to study the antigenicity, replication, maturation and pathogenicity of Swine Vesicular Disease virus. In vitro transcription RNA from pSVOK12 transfected IBRS-2 cells and the recovered virus RNA were isolated and sequenced, then indirect hemagglutination test, indirect immunofluorescence assays, eleectron microscope test, 50% tissue culture infecting dose (TCID50) assays and mouse virulence studies were performed to study the antigenicity and virulence of the recovered virus. The result showed that the infectious clones we obtained and the virus derived from pSVOK12 had the same biological properties as the parental strain HK/70. The full-length infectious cDNA clone, pSVOK12, will be very useful in studies of the antigenicity, virulence, pathogenesis, maturation and replication of SVDV.
Miguel Angel Jiménez-clavero - One of the best experts on this subject based on the ideXlab platform.
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Heparan sulphate mediates Swine Vesicular Disease virus attachment to the host cell
Journal of General Virology, 2004Co-Authors: Estela Escribano-romero, Miguel Angel Jiménez-clavero, Paula Gomes, Juan Antonio García-ranea, Victoria LeyAbstract:Heparan sulphate (HS) has been found to serve as receptor for initial cell binding of numerous viruses. Different glycosaminoglycans (GAGs), including heparin and HS, were analysed for their ability to bind Swine Vesicular Disease virus (SVDV), a picornavirus with close homology to human coxsackie B5 virus. Binding of SVDV was established by heparin-affinity chromatography. In addition, infection of IB-RS-2 epithelial porcine cells was inhibited by treating the virus with soluble HS, heparin, and chondroitin sulphate B (CS-B), as well as by enzymic digestion of cell surface GAGs. Analysis of the infection course showed that SVDV uses cellular HS for its binding to the cell surface and that this interaction occurs during attachment of the virus, prior to its internalization into the cell. Sequence analysis of SVDV variants selected for their lack of sensitivity to heparin inhibition in vitro led to the identification of two residues (A2135V and I1266K) potentially involved in heparin/HS interaction. The location of these residues in a three-dimensional model shows that they are clustered in a well-exposed region of the capsid, providing a physical mechanism that could account for the heparin-binding phenotype.
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STRUCTURE OF Swine Vesicular Disease VIRUS: MAPPING OF CHANGES OCCURRING DURING ADAPTATION OF HUMAN COXSACKIE B5 VIRUS TO INFECT Swine
Journal of virology, 2003Co-Authors: Núria Verdaguer, Miguel Angel Jiménez-clavero, Ignacio Fita, Victoria LeyAbstract:The structure of Swine Vesicular Disease virus (SVDV) was solved and refined at a 3.0-Aresolution by X-ray crystallography to gain information about the role of sequence changes that occurred as this virus evolved from the parental human pathogen coxsackievirus B5 (CVB5). These amino acid substitutions can be clustered in five distinct regions: (i) the antigenic sites, (ii) the hydrophobic pocket of the VP1 -sandwich, (iii) the putative CAR binding site, (iv) the putative heparan sulfate binding site, and (v) the fivefold axis. The VP1 pocket is occupied by a branched pocket factor, apparently different from that present in the closely related virus CVB3 and in other picornaviruses. This finding may be relevant for the design of new antiviral compounds against this site. Density consistent with the presence of ions was observed on the fivefold and threefold axes. The structure also provided an accurate description of the putative receptor binding sites. Swine Vesicular Disease virus (SVDV) is a member of the Enterovirus genus, within the Picornaviridae family. It causes a highly contagious Disease of pigs that spreads rapidly by direct contact among infected animals and by environmental contam- ination (12). It is not a severe Disease, although the similarity between the lesions it causes and those produced by foot-and- mouth Disease (FMD) has led to it being considered econom- ically important, and routine surveillance is maintained in Eu- ropean countries (reviewed in reference 13). The Disease was first described in Italy in 1966 (38), and numerous outbreaks have since occurred in Europe and Asia. SVDV is a porcine variant of the human pathogen coxsack-
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Crystallization and preliminary X-ray analysis of Swine Vesicular Disease virus (SVDV).
Acta Crystallographica Section D Biological Crystallography, 2003Co-Authors: Miguel Angel Jiménez-clavero, Victoria Ley, Ignacio Fita, Núria VerdaguerAbstract:Three different crystal forms of the Swine Vesicular Disease virus (SVDV), isolate SPA/2/'93, were obtained by the hanging-drop vapour-diffusion technique using ammonium sulfate and sodium/potassium phosphate as precipitants. Monoclinic crystals, space group C2, with unit-cell parameters a = 473.7, b = 385.3, c = 472.8 A, beta = 100.4 degrees, contain one virus pArticle in the crystal asymmetric unit and diffract to 3.0 A resolution. A second type of crystals had a cubic morphology and diffracted beyond 2.6 A resolution. These crystals belong to a primitive orthorhombic space group, with unit-cell parameters a = 319.6, b = 353.8, c = 377.7 A, and contain half a virus pArticle in the asymmetric unit. A third type of crystals, with a prismatic shape and belonging to space group I222, was also obtained under similar crystallization conditions. These latter crystals, with unit-cell parameters a = 318.3, b = 349.9, c = 371.7 A, diffract to at least 3.0 A resolution and contain 15 protomers per asymmetric unit; this requires that three perpendicular crystal twofold axes coincide with three of the viral pArticles' dyad axes.
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The N-Terminal Region of the VP1 Protein of Swine Vesicular Disease Virus Contains a Neutralization Site That Arises upon Cell Attachment and Is Involved in Viral Entry
Journal of virology, 2001Co-Authors: Miguel Angel Jiménez-clavero, Estela Escribano-romero, A. J. Douglas, Victoria LeyAbstract:The N-terminal region of VP1 of Swine Vesicular Disease virus (SVDV) is highly antigenic in Swine, despite its internal location in the capsid. Here we show that antibodies to this region can block infection and that allowing the virus to attach to cells increases this blockage significantly. The results indicate that upon binding to the cell, SVDV capsid undergoes a conformational change that is temperature independent and that exposes the N terminus of VP1. This process makes this region accessible to antibodies which block virus entry.
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Immune Recognition of Swine Vesicular Disease Virus Structural Proteins: Novel Antigenic Regions That Are Not Exposed in the Capsid
Virology, 2000Co-Authors: Miguel Angel Jiménez-clavero, Juan Antonio García-ranea, A. J. Douglas, T. Lavery, Victoria LeyAbstract:Swine Vesicular Disease virus (SVDV) is an enterovirus of the Picornaviridae family that belongs to the coxsackievirus B group. A number of antigenic sites have been identified in SVDV by analysis of neutralizing monoclonal antibody-resistant mutants and shown to be exposed on the surface of the capsid. In this paper we have identified seven new immunodominant antigenic regions in SVDV capsid proteins by a peptide scanning method, using a panel of sera from infected pigs. When these antigenic regions were located in the capsid by using a computer-generated three-dimensional model of the virion, one was readily exposed on the surface of the virus and the remaining sites were located facing the inner side of the capsid shell, at subunit contacts, or in the interior of the subunit structure.
Hong Tian - One of the best experts on this subject based on the ideXlab platform.
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Expression and immunological analysis of capsid protein precursor of Swine Vesicular Disease virus HK/70
Virologica Sinica, 2010Co-Authors: Hong Tian, Haixue Zheng, Youjun Shang, Shuang-hui Ying, Xiangtao LiuAbstract:VP1, a capsid protein of Swine Vesicular Disease virus, was cloned from the SVDV HK/70 strain and inserted into retroviral vector pBABE puro, and expressed in PK15 cells by an retroviral expression system. The ability of the VP1 protein to induce an immune response was then evaluated in guinea pigs. Western blot and ELISA results indicated that the VP1 protein can be recognized by SVDV positive serum, Furthermore, anti-SVDV specific antibodies and lymphocyte proliferation were elicited and increased by VP1 protein after vaccination. These results encourage further work towards the development of a vaccine against SVDV infection.
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expression and immunological analysis of capsid protein precursor of Swine Vesicular Disease virus hk 70
Virologica Sinica, 2010Co-Authors: Hong Tian, Haixue Zheng, Youjun Shang, Shuang-hui Ying, Xiangtao LiuAbstract:VP1, a capsid protein of Swine Vesicular Disease virus, was cloned from the SVDV HK/70 strain and inserted into retroviral vector pBABE puro, and expressed in PK15 cells by an retroviral expression system. The ability of the VP1 protein to induce an immune response was then evaluated in guinea pigs. Western blot and ELISA results indicated that the VP1 protein can be recognized by SVDV positive serum, Furthermore, anti-SVDV specific antibodies and lymphocyte proliferation were elicited and increased by VP1 protein after vaccination. These results encourage further work towards the development of a vaccine against SVDV infection.
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Infective viruses produced from full-length complementary DNA of Swine Vesicular Disease viruses HK/70 strain.
Chinese science bulletin = Kexue tongbao, 2006Co-Authors: Haixue Zheng, Xiangtao Liu, Youjun Shang, Xing-wen Bai, Ye Jin, Shiqi Sun, Guo Huichen, Hong Tian, Xia FengAbstract:The full-length cDNA clone of Swine Vesicular Disease virus HK/70 strain named pSVOK12 was constructed in order to study the antigenicity, replication, maturation and pathogenicity of Swine Vesicular Disease virus. In vitro transcription RNA from pSVOK12 transfected IBRS-2 cells and the recovered virus RNA were isolated and sequenced, then indirect hemagglutination test, indirect immunofluorescence assays, eleectron microscope test, 50% tissue culture infecting dose (TCID50) assays and mouse virulence studies were performed to study the antigenicity and virulence of the recovered virus. The result showed that the infectious clones we obtained and the virus derived from pSVOK12 had the same biological properties as the parental strain HK/70. The full-length infectious cDNA clone, pSVOK12, will be very useful in studies of the antigenicity, virulence, pathogenesis, maturation and replication of SVDV.
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infective viruses produced from full length complementary dna of Swine Vesicular Disease viruses hk 70 strain
Chinese Science Bulletin, 2006Co-Authors: Haixue Zheng, Xiangtao Liu, Youjun Shang, Xing-wen Bai, Ye Jin, Shiqi Sun, Hong Tian, Xia Feng, Huichen Guo, Shuanghui YinAbstract:The full-length cDNA clone of Swine Vesicular Disease virus HK/70 strain named pSVOK12 was constructed in order to study the antigenicity, replication, maturation and pathogenicity of Swine Vesicular Disease virus. In vitro transcription RNA from pSVOK12 transfected IBRS-2 cells and the recovered virus RNA were isolated and sequenced, then indirect hemagglutination test, indirect immunofluorescence assays, eleectron microscope test, 50% tissue culture infecting dose (TCID50) assays and mouse virulence studies were performed to study the antigenicity and virulence of the recovered virus. The result showed that the infectious clones we obtained and the virus derived from pSVOK12 had the same biological properties as the parental strain HK/70. The full-length infectious cDNA clone, pSVOK12, will be very useful in studies of the antigenicity, virulence, pathogenesis, maturation and replication of SVDV.
Haixue Zheng - One of the best experts on this subject based on the ideXlab platform.
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Expression and immunological analysis of capsid protein precursor of Swine Vesicular Disease virus HK/70
Virologica Sinica, 2010Co-Authors: Hong Tian, Haixue Zheng, Youjun Shang, Shuang-hui Ying, Xiangtao LiuAbstract:VP1, a capsid protein of Swine Vesicular Disease virus, was cloned from the SVDV HK/70 strain and inserted into retroviral vector pBABE puro, and expressed in PK15 cells by an retroviral expression system. The ability of the VP1 protein to induce an immune response was then evaluated in guinea pigs. Western blot and ELISA results indicated that the VP1 protein can be recognized by SVDV positive serum, Furthermore, anti-SVDV specific antibodies and lymphocyte proliferation were elicited and increased by VP1 protein after vaccination. These results encourage further work towards the development of a vaccine against SVDV infection.
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expression and immunological analysis of capsid protein precursor of Swine Vesicular Disease virus hk 70
Virologica Sinica, 2010Co-Authors: Hong Tian, Haixue Zheng, Youjun Shang, Shuang-hui Ying, Xiangtao LiuAbstract:VP1, a capsid protein of Swine Vesicular Disease virus, was cloned from the SVDV HK/70 strain and inserted into retroviral vector pBABE puro, and expressed in PK15 cells by an retroviral expression system. The ability of the VP1 protein to induce an immune response was then evaluated in guinea pigs. Western blot and ELISA results indicated that the VP1 protein can be recognized by SVDV positive serum, Furthermore, anti-SVDV specific antibodies and lymphocyte proliferation were elicited and increased by VP1 protein after vaccination. These results encourage further work towards the development of a vaccine against SVDV infection.
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Infective viruses produced from full-length complementary DNA of Swine Vesicular Disease viruses HK/70 strain.
Chinese science bulletin = Kexue tongbao, 2006Co-Authors: Haixue Zheng, Xiangtao Liu, Youjun Shang, Xing-wen Bai, Ye Jin, Shiqi Sun, Guo Huichen, Hong Tian, Xia FengAbstract:The full-length cDNA clone of Swine Vesicular Disease virus HK/70 strain named pSVOK12 was constructed in order to study the antigenicity, replication, maturation and pathogenicity of Swine Vesicular Disease virus. In vitro transcription RNA from pSVOK12 transfected IBRS-2 cells and the recovered virus RNA were isolated and sequenced, then indirect hemagglutination test, indirect immunofluorescence assays, eleectron microscope test, 50% tissue culture infecting dose (TCID50) assays and mouse virulence studies were performed to study the antigenicity and virulence of the recovered virus. The result showed that the infectious clones we obtained and the virus derived from pSVOK12 had the same biological properties as the parental strain HK/70. The full-length infectious cDNA clone, pSVOK12, will be very useful in studies of the antigenicity, virulence, pathogenesis, maturation and replication of SVDV.
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infective viruses produced from full length complementary dna of Swine Vesicular Disease viruses hk 70 strain
Chinese Science Bulletin, 2006Co-Authors: Haixue Zheng, Xiangtao Liu, Youjun Shang, Xing-wen Bai, Ye Jin, Shiqi Sun, Hong Tian, Xia Feng, Huichen Guo, Shuanghui YinAbstract:The full-length cDNA clone of Swine Vesicular Disease virus HK/70 strain named pSVOK12 was constructed in order to study the antigenicity, replication, maturation and pathogenicity of Swine Vesicular Disease virus. In vitro transcription RNA from pSVOK12 transfected IBRS-2 cells and the recovered virus RNA were isolated and sequenced, then indirect hemagglutination test, indirect immunofluorescence assays, eleectron microscope test, 50% tissue culture infecting dose (TCID50) assays and mouse virulence studies were performed to study the antigenicity and virulence of the recovered virus. The result showed that the infectious clones we obtained and the virus derived from pSVOK12 had the same biological properties as the parental strain HK/70. The full-length infectious cDNA clone, pSVOK12, will be very useful in studies of the antigenicity, virulence, pathogenesis, maturation and replication of SVDV.
