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Respiratory syncytial virus matrix protein assembles as a lattice with local and extended order that coordinates the position of the fusion glycoprotein

Bryan S. Sibert, Joseph Y. Kim, Jie E. Yang, Zunlong Ke, Christopher C. Stobart, Martin M. Moore, View ORCID ProfileElizabeth R. Wright
doi: https://doi.org/10.1101/2021.10.13.464285
Bryan S. Sibert
1Department of Biochemistry, University of Wisconsin, Madison, WI USA
2Cryo-Electron Microscopy Research Center, Department of Biochemistry, University of Wisconsin, Madison, WI USA
3Midwest Center for Cryo-Electron Tomography, Department of Biochemistry, University of Wisconsin, Madison, WI USA
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Joseph Y. Kim
1Department of Biochemistry, University of Wisconsin, Madison, WI USA
4Department of Chemistry, University of Wisconsin, Madison, WI USA
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Jie E. Yang
1Department of Biochemistry, University of Wisconsin, Madison, WI USA
2Cryo-Electron Microscopy Research Center, Department of Biochemistry, University of Wisconsin, Madison, WI USA
3Midwest Center for Cryo-Electron Tomography, Department of Biochemistry, University of Wisconsin, Madison, WI USA
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Zunlong Ke
5Department of Cell and Virus Structure, Max Planck Institute of Biochemistry, Martinsried, Germany
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Christopher C. Stobart
6Department of Biological Sciences, Butler University, Indianapolis, IN USA
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Martin M. Moore
7Meissa Vaccines, Inc., Redwood City, CA USA
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Elizabeth R. Wright
1Department of Biochemistry, University of Wisconsin, Madison, WI USA
2Cryo-Electron Microscopy Research Center, Department of Biochemistry, University of Wisconsin, Madison, WI USA
3Midwest Center for Cryo-Electron Tomography, Department of Biochemistry, University of Wisconsin, Madison, WI USA
8Morgridge Institute for Research, Madison, WI, USA
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  • ORCID record for Elizabeth R. Wright
  • For correspondence: erwright2@wisc.edu
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Abstract

Respiratory syncytial virus (RSV) is a significant cause of respiratory illness in young children and adults worldwide. There is currently no vaccine or targeted antiviral for RSV. RSV is an enveloped, filamentous, negative-strand RNA virus. Individual virions vary in both diameter and length, with an average diameter of ∼130 nm and ranging from ∼500 nm to over 10 μm in length. The RSV matrix (M) protein is peripherally associated with the interior of the viral membrane. Though the general arrangement of structural proteins within the virion is known, the molecular organization of M and other structural proteins was previously unknown. Here, using whole-cell cryo-electron tomography and sub-tomogram averaging, we show that M is arranged in a packed helical-like lattice of M-dimers ordered at an angle of ∼47° to the viral long axis. Sub-tomogram averages including F and M indicate that the position of F on the viral surface is correlated with the underlying M lattice. Finally, we report that RSV F is frequently observed as pairs, with the F trimers oriented in an anti-parallel conformation to support potential interaction between trimers. These results provide insight into RSV assembly and virion organization and may aid in the identification and development of RSV vaccines and anti-viral targets.

Competing Interest Statement

The authors have declared no competing interest.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. All rights reserved. No reuse allowed without permission.
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Posted October 15, 2021.
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Respiratory syncytial virus matrix protein assembles as a lattice with local and extended order that coordinates the position of the fusion glycoprotein
Bryan S. Sibert, Joseph Y. Kim, Jie E. Yang, Zunlong Ke, Christopher C. Stobart, Martin M. Moore, Elizabeth R. Wright
bioRxiv 2021.10.13.464285; doi: https://doi.org/10.1101/2021.10.13.464285
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Respiratory syncytial virus matrix protein assembles as a lattice with local and extended order that coordinates the position of the fusion glycoprotein
Bryan S. Sibert, Joseph Y. Kim, Jie E. Yang, Zunlong Ke, Christopher C. Stobart, Martin M. Moore, Elizabeth R. Wright
bioRxiv 2021.10.13.464285; doi: https://doi.org/10.1101/2021.10.13.464285

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