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Structure and oligomerization state of the C‐terminal region of the Middle East respiratory syndrome coronavirus nucleoprotein

Identifieur interne : 000979 ( Pmc/Curation ); précédent : 000978; suivant : 000980

Structure and oligomerization state of the C‐terminal region of the Middle East respiratory syndrome coronavirus nucleoprotein

Auteurs : Thi Hong Van Nguyen ; Julie Lichière ; Bruno Canard ; Nicolas Papageorgiou ; Sarah Attoumani ; François Ferron ; Bruno Coutard

Source :

RBID : PMC:7159728

Abstract

Middle East respiratory syndrome coronavirus (MERS‐CoV) is a human pathogen responsible for a severe respiratory illness that emerged in 2012. Structural information about the proteins that constitute the viral particle is scarce. In order to contribute to a better understanding of the nucleoprotein (N) in charge of RNA genome encapsidation, the structure of the C‐terminal domain of N from MERS‐CoV obtained using single‐crystal X‐ray diffraction is reported here at 1.97 Å resolution. The molecule is present as a dimer in the crystal structure and this oligomerization state is confirmed in solution, as measured by additional methods including small‐angle X‐ray scattering measurements. Comparisons with the structures of the C‐terminal domains of N from other coronaviruses reveals a high degree of structural conservation despite low sequence conservation, and differences in electrostatic potential at the surface of the protein.


Url:
DOI: 10.1107/S2059798318014948
PubMed: 30644840
PubMed Central: 7159728

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PMC:7159728

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<p>Middle East respiratory syndrome coronavirus (MERS‐CoV) is a human pathogen responsible for a severe respiratory illness that emerged in 2012. Structural information about the proteins that constitute the viral particle is scarce. In order to contribute to a better understanding of the nucleoprotein (N) in charge of RNA genome encapsidation, the structure of the C‐terminal domain of N from MERS‐CoV obtained using single‐crystal X‐ray diffraction is reported here at 1.97 Å resolution. The molecule is present as a dimer in the crystal structure and this oligomerization state is confirmed in solution, as measured by additional methods including small‐angle X‐ray scattering measurements. Comparisons with the structures of the C‐terminal domains of N from other coronaviruses reveals a high degree of structural conservation despite low sequence conservation, and differences in electrostatic potential at the surface of the protein.</p>
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Aix-Marseille Université, AFMB UMR 7257, 13288Marseilles, France</aff>
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CNRS, AFMB UMR 7257, 13288Marseilles, France</aff>
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François Ferron, e-mail:
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<copyright-statement content-type="article-copyright">© International Union of Crystallography, 2019</copyright-statement>
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<license-p>This article is being made freely available through PubMed Central as part of the COVID-19 public health emergency response. It can be used for unrestricted research re-use and analysis in any form or by any means with acknowledgement of the original source, for the duration of the public health emergency.</license-p>
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<p>Middle East respiratory syndrome coronavirus (MERS‐CoV) is a human pathogen responsible for a severe respiratory illness that emerged in 2012. Structural information about the proteins that constitute the viral particle is scarce. In order to contribute to a better understanding of the nucleoprotein (N) in charge of RNA genome encapsidation, the structure of the C‐terminal domain of N from MERS‐CoV obtained using single‐crystal X‐ray diffraction is reported here at 1.97 Å resolution. The molecule is present as a dimer in the crystal structure and this oligomerization state is confirmed in solution, as measured by additional methods including small‐angle X‐ray scattering measurements. Comparisons with the structures of the C‐terminal domains of N from other coronaviruses reveals a high degree of structural conservation despite low sequence conservation, and differences in electrostatic potential at the surface of the protein.</p>
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<p>The X‐ray structure and SAXS analysis of the C‐terminal domain of the nucleocapsid from Middle East respiratory syndrome coronavirus, an emerging virus, are reported.
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