Stability and Shape of Hepatitis B Virus Capsids In Vacuo

Authors

  • Charlotte Uetrecht,

    1. Biomolecular Mass Spectrometry and Proteomics Group, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Sorbonnelaan 16, 3584 CA Utrecht (The Netherlands), Fax: (+31) 30-251-8219
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  • Cees Versluis,

    1. Biomolecular Mass Spectrometry and Proteomics Group, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Sorbonnelaan 16, 3584 CA Utrecht (The Netherlands), Fax: (+31) 30-251-8219
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  • Norman R. Watts,

    1. Protein Expression Laboratory, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892 (USA)
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  • Paul T. Wingfield,

    1. Protein Expression Laboratory, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892 (USA)
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  • Alasdair C. Steven,

    1. Laboratory of Structural Biology Research, National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892 (USA)
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  • Albert J. R. Heck Prof. Dr.

    1. Biomolecular Mass Spectrometry and Proteomics Group, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Sorbonnelaan 16, 3584 CA Utrecht (The Netherlands), Fax: (+31) 30-251-8219
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  • This research was supported by the Netherlands Proteomics Centre and the NIAMS Intramural Research Program of the NIH.

Abstract

original image

Viruses at a glance: Ion mobility mass spectrometry allows the identification and differentiation of states in a viral assembly not only by mass but also by conformation. This approach has been used to obtain a biophysical characterization of the hepatitis B virus capsids, and has shown that of its two distinct icosahedral geometries, the spherical capsid structure is preserved in vacuo (see picture).

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