The Experts below are selected from a list of 285 Experts worldwide ranked by ideXlab platform

Eva Pérez-martín - One of the best experts on this subject based on the ideXlab platform.

  • Structure-based energetics of Protein interfaces guides foot-and-mouth disease virus vaccine design
    Nature Structural & Molecular Biology, 2015
    Co-Authors: Abhay Kotecha, Julian Seago, Alison Burman, Silvia Loureiro, Jingshan Ren, Claudine Porta, Helen M. Ginn, Terry Jackson, Katherine Scott, Eva Pérez-martín
    Abstract:

    Virus capsids are primed for disassembly, yet capsid integrity is key to generating a protective immune response. Foot-and-mouth disease virus (FMDV) capsids comprise identical Pentameric Protein subunits held together by tenuous noncovalent interactions and are often unstable. Chemically inactivated or recombinant empty capsids, which could form the basis of future vaccines, are even less stable than live virus. Here we devised a computational method to assess the relative stability of Protein-Protein interfaces and used it to design improved candidate vaccines for two poorly stable, but globally important, serotypes of FMDV: O and SAT2. We used a restrained molecular dynamics strategy to rank mutations predicted to strengthen the pentamer interfaces and applied the results to produce stabilized capsids. Structural analyses and stability assays confirmed the predictions, and vaccinated animals generated improved neutralizing-antibody responses to stabilized particles compared to parental viruses and wild-type capsids. Foot-and-mouth disease virus (FMDV) capsids are often unstable, thus limiting their use as vaccines. A computational method was used to strengthen Protein-Protein interfaces and engineer stabilized FMDV capsids, which generated improved antibody responses in vaccinated calves and guinea pigs.

  • Structure-based energetics of Protein interfaces guides foot-and-mouth disease virus vaccine design.
    Nature structural & molecular biology, 2015
    Co-Authors: Abhay Kotecha, Julian Seago, Katherine Anne Scott, Alison Burman, Silvia Loureiro, Jingshan Ren, Claudine Porta, Helen M. Ginn, Terry Jackson, Eva Pérez-martín
    Abstract:

    Virus capsids are primed for disassembly, yet capsid integrity is key to generating a protective immune response. Foot-and-mouth disease virus (FMDV) capsids comprise identical Pentameric Protein subunits held together by tenuous noncovalent interactions and are often unstable. Chemically inactivated or recombinant empty capsids, which could form the basis of future vaccines, are even less stable than live virus. Here we devised a computational method to assess the relative stability of Protein-Protein interfaces and used it to design improved candidate vaccines for two poorly stable, but globally important, serotypes of FMDV: O and SAT2. We used a restrained molecular dynamics strategy to rank mutations predicted to strengthen the pentamer interfaces and applied the results to produce stabilized capsids. Structural analyses and stability assays confirmed the predictions, and vaccinated animals generated improved neutralizing-antibody responses to stabilized particles compared to parental viruses and wild-type capsids.

Abhay Kotecha - One of the best experts on this subject based on the ideXlab platform.

  • Structure-based energetics of Protein interfaces guides foot-and-mouth disease virus vaccine design
    Nature Structural & Molecular Biology, 2015
    Co-Authors: Abhay Kotecha, Julian Seago, Alison Burman, Silvia Loureiro, Jingshan Ren, Claudine Porta, Helen M. Ginn, Terry Jackson, Katherine Scott, Eva Pérez-martín
    Abstract:

    Virus capsids are primed for disassembly, yet capsid integrity is key to generating a protective immune response. Foot-and-mouth disease virus (FMDV) capsids comprise identical Pentameric Protein subunits held together by tenuous noncovalent interactions and are often unstable. Chemically inactivated or recombinant empty capsids, which could form the basis of future vaccines, are even less stable than live virus. Here we devised a computational method to assess the relative stability of Protein-Protein interfaces and used it to design improved candidate vaccines for two poorly stable, but globally important, serotypes of FMDV: O and SAT2. We used a restrained molecular dynamics strategy to rank mutations predicted to strengthen the pentamer interfaces and applied the results to produce stabilized capsids. Structural analyses and stability assays confirmed the predictions, and vaccinated animals generated improved neutralizing-antibody responses to stabilized particles compared to parental viruses and wild-type capsids. Foot-and-mouth disease virus (FMDV) capsids are often unstable, thus limiting their use as vaccines. A computational method was used to strengthen Protein-Protein interfaces and engineer stabilized FMDV capsids, which generated improved antibody responses in vaccinated calves and guinea pigs.

  • Structure-based energetics of Protein interfaces guides foot-and-mouth disease virus vaccine design.
    Nature structural & molecular biology, 2015
    Co-Authors: Abhay Kotecha, Julian Seago, Katherine Anne Scott, Alison Burman, Silvia Loureiro, Jingshan Ren, Claudine Porta, Helen M. Ginn, Terry Jackson, Eva Pérez-martín
    Abstract:

    Virus capsids are primed for disassembly, yet capsid integrity is key to generating a protective immune response. Foot-and-mouth disease virus (FMDV) capsids comprise identical Pentameric Protein subunits held together by tenuous noncovalent interactions and are often unstable. Chemically inactivated or recombinant empty capsids, which could form the basis of future vaccines, are even less stable than live virus. Here we devised a computational method to assess the relative stability of Protein-Protein interfaces and used it to design improved candidate vaccines for two poorly stable, but globally important, serotypes of FMDV: O and SAT2. We used a restrained molecular dynamics strategy to rank mutations predicted to strengthen the pentamer interfaces and applied the results to produce stabilized capsids. Structural analyses and stability assays confirmed the predictions, and vaccinated animals generated improved neutralizing-antibody responses to stabilized particles compared to parental viruses and wild-type capsids.

Jingshan Ren - One of the best experts on this subject based on the ideXlab platform.

  • Structure-based energetics of Protein interfaces guides foot-and-mouth disease virus vaccine design
    Nature Structural & Molecular Biology, 2015
    Co-Authors: Abhay Kotecha, Julian Seago, Alison Burman, Silvia Loureiro, Jingshan Ren, Claudine Porta, Helen M. Ginn, Terry Jackson, Katherine Scott, Eva Pérez-martín
    Abstract:

    Virus capsids are primed for disassembly, yet capsid integrity is key to generating a protective immune response. Foot-and-mouth disease virus (FMDV) capsids comprise identical Pentameric Protein subunits held together by tenuous noncovalent interactions and are often unstable. Chemically inactivated or recombinant empty capsids, which could form the basis of future vaccines, are even less stable than live virus. Here we devised a computational method to assess the relative stability of Protein-Protein interfaces and used it to design improved candidate vaccines for two poorly stable, but globally important, serotypes of FMDV: O and SAT2. We used a restrained molecular dynamics strategy to rank mutations predicted to strengthen the pentamer interfaces and applied the results to produce stabilized capsids. Structural analyses and stability assays confirmed the predictions, and vaccinated animals generated improved neutralizing-antibody responses to stabilized particles compared to parental viruses and wild-type capsids. Foot-and-mouth disease virus (FMDV) capsids are often unstable, thus limiting their use as vaccines. A computational method was used to strengthen Protein-Protein interfaces and engineer stabilized FMDV capsids, which generated improved antibody responses in vaccinated calves and guinea pigs.

  • Structure-based energetics of Protein interfaces guides foot-and-mouth disease virus vaccine design.
    Nature structural & molecular biology, 2015
    Co-Authors: Abhay Kotecha, Julian Seago, Katherine Anne Scott, Alison Burman, Silvia Loureiro, Jingshan Ren, Claudine Porta, Helen M. Ginn, Terry Jackson, Eva Pérez-martín
    Abstract:

    Virus capsids are primed for disassembly, yet capsid integrity is key to generating a protective immune response. Foot-and-mouth disease virus (FMDV) capsids comprise identical Pentameric Protein subunits held together by tenuous noncovalent interactions and are often unstable. Chemically inactivated or recombinant empty capsids, which could form the basis of future vaccines, are even less stable than live virus. Here we devised a computational method to assess the relative stability of Protein-Protein interfaces and used it to design improved candidate vaccines for two poorly stable, but globally important, serotypes of FMDV: O and SAT2. We used a restrained molecular dynamics strategy to rank mutations predicted to strengthen the pentamer interfaces and applied the results to produce stabilized capsids. Structural analyses and stability assays confirmed the predictions, and vaccinated animals generated improved neutralizing-antibody responses to stabilized particles compared to parental viruses and wild-type capsids.

Terry Jackson - One of the best experts on this subject based on the ideXlab platform.

  • Structure-based energetics of Protein interfaces guides foot-and-mouth disease virus vaccine design
    Nature Structural & Molecular Biology, 2015
    Co-Authors: Abhay Kotecha, Julian Seago, Alison Burman, Silvia Loureiro, Jingshan Ren, Claudine Porta, Helen M. Ginn, Terry Jackson, Katherine Scott, Eva Pérez-martín
    Abstract:

    Virus capsids are primed for disassembly, yet capsid integrity is key to generating a protective immune response. Foot-and-mouth disease virus (FMDV) capsids comprise identical Pentameric Protein subunits held together by tenuous noncovalent interactions and are often unstable. Chemically inactivated or recombinant empty capsids, which could form the basis of future vaccines, are even less stable than live virus. Here we devised a computational method to assess the relative stability of Protein-Protein interfaces and used it to design improved candidate vaccines for two poorly stable, but globally important, serotypes of FMDV: O and SAT2. We used a restrained molecular dynamics strategy to rank mutations predicted to strengthen the pentamer interfaces and applied the results to produce stabilized capsids. Structural analyses and stability assays confirmed the predictions, and vaccinated animals generated improved neutralizing-antibody responses to stabilized particles compared to parental viruses and wild-type capsids. Foot-and-mouth disease virus (FMDV) capsids are often unstable, thus limiting their use as vaccines. A computational method was used to strengthen Protein-Protein interfaces and engineer stabilized FMDV capsids, which generated improved antibody responses in vaccinated calves and guinea pigs.

  • Structure-based energetics of Protein interfaces guides foot-and-mouth disease virus vaccine design.
    Nature structural & molecular biology, 2015
    Co-Authors: Abhay Kotecha, Julian Seago, Katherine Anne Scott, Alison Burman, Silvia Loureiro, Jingshan Ren, Claudine Porta, Helen M. Ginn, Terry Jackson, Eva Pérez-martín
    Abstract:

    Virus capsids are primed for disassembly, yet capsid integrity is key to generating a protective immune response. Foot-and-mouth disease virus (FMDV) capsids comprise identical Pentameric Protein subunits held together by tenuous noncovalent interactions and are often unstable. Chemically inactivated or recombinant empty capsids, which could form the basis of future vaccines, are even less stable than live virus. Here we devised a computational method to assess the relative stability of Protein-Protein interfaces and used it to design improved candidate vaccines for two poorly stable, but globally important, serotypes of FMDV: O and SAT2. We used a restrained molecular dynamics strategy to rank mutations predicted to strengthen the pentamer interfaces and applied the results to produce stabilized capsids. Structural analyses and stability assays confirmed the predictions, and vaccinated animals generated improved neutralizing-antibody responses to stabilized particles compared to parental viruses and wild-type capsids.

Helen M. Ginn - One of the best experts on this subject based on the ideXlab platform.

  • Structure-based energetics of Protein interfaces guides foot-and-mouth disease virus vaccine design
    Nature Structural & Molecular Biology, 2015
    Co-Authors: Abhay Kotecha, Julian Seago, Alison Burman, Silvia Loureiro, Jingshan Ren, Claudine Porta, Helen M. Ginn, Terry Jackson, Katherine Scott, Eva Pérez-martín
    Abstract:

    Virus capsids are primed for disassembly, yet capsid integrity is key to generating a protective immune response. Foot-and-mouth disease virus (FMDV) capsids comprise identical Pentameric Protein subunits held together by tenuous noncovalent interactions and are often unstable. Chemically inactivated or recombinant empty capsids, which could form the basis of future vaccines, are even less stable than live virus. Here we devised a computational method to assess the relative stability of Protein-Protein interfaces and used it to design improved candidate vaccines for two poorly stable, but globally important, serotypes of FMDV: O and SAT2. We used a restrained molecular dynamics strategy to rank mutations predicted to strengthen the pentamer interfaces and applied the results to produce stabilized capsids. Structural analyses and stability assays confirmed the predictions, and vaccinated animals generated improved neutralizing-antibody responses to stabilized particles compared to parental viruses and wild-type capsids. Foot-and-mouth disease virus (FMDV) capsids are often unstable, thus limiting their use as vaccines. A computational method was used to strengthen Protein-Protein interfaces and engineer stabilized FMDV capsids, which generated improved antibody responses in vaccinated calves and guinea pigs.

  • Structure-based energetics of Protein interfaces guides foot-and-mouth disease virus vaccine design.
    Nature structural & molecular biology, 2015
    Co-Authors: Abhay Kotecha, Julian Seago, Katherine Anne Scott, Alison Burman, Silvia Loureiro, Jingshan Ren, Claudine Porta, Helen M. Ginn, Terry Jackson, Eva Pérez-martín
    Abstract:

    Virus capsids are primed for disassembly, yet capsid integrity is key to generating a protective immune response. Foot-and-mouth disease virus (FMDV) capsids comprise identical Pentameric Protein subunits held together by tenuous noncovalent interactions and are often unstable. Chemically inactivated or recombinant empty capsids, which could form the basis of future vaccines, are even less stable than live virus. Here we devised a computational method to assess the relative stability of Protein-Protein interfaces and used it to design improved candidate vaccines for two poorly stable, but globally important, serotypes of FMDV: O and SAT2. We used a restrained molecular dynamics strategy to rank mutations predicted to strengthen the pentamer interfaces and applied the results to produce stabilized capsids. Structural analyses and stability assays confirmed the predictions, and vaccinated animals generated improved neutralizing-antibody responses to stabilized particles compared to parental viruses and wild-type capsids.