Human Rhinovirus B14

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The Experts below are selected from a list of 3 Experts worldwide ranked by ideXlab platform

Yangchao Dong - One of the best experts on this subject based on the ideXlab platform.

  • antibody induced uncoating of Human Rhinovirus B14
    Proceedings of the National Academy of Sciences of the United States of America, 2017
    Co-Authors: Yangchao Dong, Yue Liu, Wen Jiang, Thomas J Smith, Zhikai Xu, Michael G Rossmann
    Abstract:

    Rhinoviruses (RVs) are the major causes of common colds in Humans. They have a nonenveloped, icosahedral capsid surrounding a positive-strand RNA genome. Here we report that the antigen-binding (Fab) fragment of a neutralizing antibody (C5) can trigger genome release from RV-B14 to form emptied particles and neutralize virus infection. Using cryo-electron microscopy, structures of the C5 Fab in complex with the full and emptied particles have been determined at 2.3 A and 3.0 A resolution, respectively. Each of the 60 Fab molecules binds primarily to a region on viral protein 3 (VP3). Binding of the C5 Fabs to RV-B14 results in significant conformational changes around holes in the capsid through which the viral RNA might exit. These results are so far the highest resolution view of an antibody–virus complex and elucidate a mechanism whereby antibodies neutralize RVs and related viruses by inducing virus uncoating.

Michael G Rossmann - One of the best experts on this subject based on the ideXlab platform.

  • antibody induced uncoating of Human Rhinovirus B14
    Proceedings of the National Academy of Sciences of the United States of America, 2017
    Co-Authors: Yangchao Dong, Yue Liu, Wen Jiang, Thomas J Smith, Zhikai Xu, Michael G Rossmann
    Abstract:

    Rhinoviruses (RVs) are the major causes of common colds in Humans. They have a nonenveloped, icosahedral capsid surrounding a positive-strand RNA genome. Here we report that the antigen-binding (Fab) fragment of a neutralizing antibody (C5) can trigger genome release from RV-B14 to form emptied particles and neutralize virus infection. Using cryo-electron microscopy, structures of the C5 Fab in complex with the full and emptied particles have been determined at 2.3 A and 3.0 A resolution, respectively. Each of the 60 Fab molecules binds primarily to a region on viral protein 3 (VP3). Binding of the C5 Fabs to RV-B14 results in significant conformational changes around holes in the capsid through which the viral RNA might exit. These results are so far the highest resolution view of an antibody–virus complex and elucidate a mechanism whereby antibodies neutralize RVs and related viruses by inducing virus uncoating.

Yue Liu - One of the best experts on this subject based on the ideXlab platform.

  • antibody induced uncoating of Human Rhinovirus B14
    Proceedings of the National Academy of Sciences of the United States of America, 2017
    Co-Authors: Yangchao Dong, Yue Liu, Wen Jiang, Thomas J Smith, Zhikai Xu, Michael G Rossmann
    Abstract:

    Rhinoviruses (RVs) are the major causes of common colds in Humans. They have a nonenveloped, icosahedral capsid surrounding a positive-strand RNA genome. Here we report that the antigen-binding (Fab) fragment of a neutralizing antibody (C5) can trigger genome release from RV-B14 to form emptied particles and neutralize virus infection. Using cryo-electron microscopy, structures of the C5 Fab in complex with the full and emptied particles have been determined at 2.3 A and 3.0 A resolution, respectively. Each of the 60 Fab molecules binds primarily to a region on viral protein 3 (VP3). Binding of the C5 Fabs to RV-B14 results in significant conformational changes around holes in the capsid through which the viral RNA might exit. These results are so far the highest resolution view of an antibody–virus complex and elucidate a mechanism whereby antibodies neutralize RVs and related viruses by inducing virus uncoating.

Wen Jiang - One of the best experts on this subject based on the ideXlab platform.

  • antibody induced uncoating of Human Rhinovirus B14
    Proceedings of the National Academy of Sciences of the United States of America, 2017
    Co-Authors: Yangchao Dong, Yue Liu, Wen Jiang, Thomas J Smith, Zhikai Xu, Michael G Rossmann
    Abstract:

    Rhinoviruses (RVs) are the major causes of common colds in Humans. They have a nonenveloped, icosahedral capsid surrounding a positive-strand RNA genome. Here we report that the antigen-binding (Fab) fragment of a neutralizing antibody (C5) can trigger genome release from RV-B14 to form emptied particles and neutralize virus infection. Using cryo-electron microscopy, structures of the C5 Fab in complex with the full and emptied particles have been determined at 2.3 A and 3.0 A resolution, respectively. Each of the 60 Fab molecules binds primarily to a region on viral protein 3 (VP3). Binding of the C5 Fabs to RV-B14 results in significant conformational changes around holes in the capsid through which the viral RNA might exit. These results are so far the highest resolution view of an antibody–virus complex and elucidate a mechanism whereby antibodies neutralize RVs and related viruses by inducing virus uncoating.

Thomas J Smith - One of the best experts on this subject based on the ideXlab platform.

  • antibody induced uncoating of Human Rhinovirus B14
    Proceedings of the National Academy of Sciences of the United States of America, 2017
    Co-Authors: Yangchao Dong, Yue Liu, Wen Jiang, Thomas J Smith, Zhikai Xu, Michael G Rossmann
    Abstract:

    Rhinoviruses (RVs) are the major causes of common colds in Humans. They have a nonenveloped, icosahedral capsid surrounding a positive-strand RNA genome. Here we report that the antigen-binding (Fab) fragment of a neutralizing antibody (C5) can trigger genome release from RV-B14 to form emptied particles and neutralize virus infection. Using cryo-electron microscopy, structures of the C5 Fab in complex with the full and emptied particles have been determined at 2.3 A and 3.0 A resolution, respectively. Each of the 60 Fab molecules binds primarily to a region on viral protein 3 (VP3). Binding of the C5 Fabs to RV-B14 results in significant conformational changes around holes in the capsid through which the viral RNA might exit. These results are so far the highest resolution view of an antibody–virus complex and elucidate a mechanism whereby antibodies neutralize RVs and related viruses by inducing virus uncoating.