Functional and evolutionary insight from the crystal structure of rubella virus protein E1

Rebecca M. DuBois, Marie-Christine Vaney, M. Alejandra Tortorici, Rana Al Kurdi, Giovanna Barba-Spaeth, Thomas Krey and Félix A. Rey ()
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Rebecca M. DuBois: Institut Pasteur, Unité de Virologie Structurale and CNRS URA 3015, F-75724 Paris Cedex 15, France
Marie-Christine Vaney: Institut Pasteur, Unité de Virologie Structurale and CNRS URA 3015, F-75724 Paris Cedex 15, France
M. Alejandra Tortorici: Institut Pasteur, Unité de Virologie Structurale and CNRS URA 3015, F-75724 Paris Cedex 15, France
Rana Al Kurdi: Institut Pasteur, Unité de Virologie Structurale and CNRS URA 3015, F-75724 Paris Cedex 15, France
Giovanna Barba-Spaeth: Institut Pasteur, Unité de Virologie Structurale and CNRS URA 3015, F-75724 Paris Cedex 15, France
Thomas Krey: Institut Pasteur, Unité de Virologie Structurale and CNRS URA 3015, F-75724 Paris Cedex 15, France
Félix A. Rey: Institut Pasteur, Unité de Virologie Structurale and CNRS URA 3015, F-75724 Paris Cedex 15, France

Nature, 2013, vol. 493, issue 7433, 552-556

Abstract: The crystal structure of rubella virus E1 glycoprotein in its post-fusion form reveals a class II fusion protein with distinct features so far unseen in any other crystallized fusion protein; the location of an antibody-neutralization epitope also suggests that rubella-specific antibodies may function through prevention of E1 glycoprotein trimer formation during cell entry.

Date: 2013
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DOI: 10.1038/nature11741

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