A Structural analysis of M protein in coronavirus assembly and morphology

Benjamin W. Neuman; Gabriella Kiss; Andreas H. Kunding; David Bhella; M. Fazil Baksh; Stephen Connelly; Ben Droese; Joseph P. Klaus; Shinji Makino; Stanley G. Sawicji; Stuart G. Siddell; Dimitrios Stamou; Ian A. Wilson; Peter Kuhn; Michael J. Buchmeier

doi:10.1016/j.jsb.2010.11.021

A Structural analysis of M protein in coronavirus assembly and morphology

Benjamin W. Neuman, Gabriella Kiss, Andreas H. Kunding, David Bhella, M. Fazil Baksh, Stephen Connelly, Ben Droese, Joseph P. Klaus, Shinji Makino, Stanley G. Sawicji, Stuart G. Siddell, Dimitrios Stamou, Ian A. Wilson, Peter Kuhn, Michael J. Buchmeier

Department of Neuroscience

259 Citations (Scopus)

Abstract

The M protein of coronavirus plays a central role in virus assembly, turning cellular membranes into workshops where virus and host factors come together to make new virus particles. We investigated how M structure and organization is related to virus shape and size using cryo-electron microscopy, tomography and statistical analysis. We present evidence that suggests M can adopt two conformations and that membrane curvature is regulated by one M conformer. Elongated M protein is associated with rigidity, clusters of spikes and a relatively narrow range of membrane curvature. In contrast, compact M protein is associated with flexibility and low spike density. Analysis of several types of virus-like particles and virions revealed that S protein, N protein and genomic RNA each help to regulate virion size and variation, presumably through interactions with M. These findings provide insight into how M protein functions to promote virus assembly.

Original language	English
Journal	Journal of Structural Biology
Volume	174
Issue number	1
Pages (from-to)	11-22
Number of pages	12
ISSN	1047-8477
DOIs	https://doi.org/10.1016/j.jsb.2010.11.021
Publication status	Published - 1 Apr 2011

Access to Document

10.1016/j.jsb.2010.11.021

http://www.sciencedirect.com/science/article/pii/S1047847710003588

Cite this

W. Neuman, B., Kiss, G., H. Kunding, A., Bhella, D., Baksh, M. F., Connelly, S., Droese, B., P. Klaus, J., Makino, S., G. Sawicji, S., G. Siddell, S., Stamou, D., A. Wilson, I., Kuhn, P., & J. Buchmeier, M. (2011). A Structural analysis of M protein in coronavirus assembly and morphology. Journal of Structural Biology, 174(1), 11-22. https://doi.org/10.1016/j.jsb.2010.11.021

W. Neuman, B, Kiss, G, H. Kunding, A, Bhella, D, Baksh, MF, Connelly, S, Droese, B, P. Klaus, J, Makino, S, G. Sawicji, S, G. Siddell, S, Stamou, D, A. Wilson, I, Kuhn, P & J. Buchmeier, M 2011, 'A Structural analysis of M protein in coronavirus assembly and morphology', Journal of Structural Biology, vol. 174, no. 1, pp. 11-22. https://doi.org/10.1016/j.jsb.2010.11.021

@article{effc65d4208e49bd8556be3708e24913,

title = "A Structural analysis of M protein in coronavirus assembly and morphology",

abstract = "The M protein of coronavirus plays a central role in virus assembly, turning cellular membranes into workshops where virus and host factors come together to make new virus particles. We investigated how M structure and organization is related to virus shape and size using cryo-electron microscopy, tomography and statistical analysis. We present evidence that suggests M can adopt two conformations and that membrane curvature is regulated by one M conformer. Elongated M protein is associated with rigidity, clusters of spikes and a relatively narrow range of membrane curvature. In contrast, compact M protein is associated with flexibility and low spike density. Analysis of several types of virus-like particles and virions revealed that S protein, N protein and genomic RNA each help to regulate virion size and variation, presumably through interactions with M. These findings provide insight into how M protein functions to promote virus assembly.",

author = "{W. Neuman}, Benjamin and Gabriella Kiss and {H. Kunding}, Andreas and David Bhella and Baksh, {M. Fazil} and Stephen Connelly and Ben Droese and {P. Klaus}, Joseph and Shinji Makino and {G. Sawicji}, Stanley and {G. Siddell}, Stuart and Dimitrios Stamou and {A. Wilson}, Ian and Peter Kuhn and {J. Buchmeier}, Michael",

year = "2011",

month = apr,

day = "1",

doi = "10.1016/j.jsb.2010.11.021",

language = "English",

volume = "174",

pages = "11--22",

journal = "Journal of Structural Biology",

issn = "1047-8477",

publisher = "Academic Press",

number = "1",

}

TY - JOUR

T1 - A Structural analysis of M protein in coronavirus assembly and morphology

AU - W. Neuman, Benjamin

AU - Kiss, Gabriella

AU - H. Kunding, Andreas

AU - Bhella, David

AU - Baksh, M. Fazil

AU - Connelly, Stephen

AU - Droese, Ben

AU - P. Klaus, Joseph

AU - Makino, Shinji

AU - G. Sawicji, Stanley

AU - G. Siddell, Stuart

AU - Stamou, Dimitrios

AU - A. Wilson, Ian

AU - Kuhn, Peter

AU - J. Buchmeier, Michael

PY - 2011/4/1

Y1 - 2011/4/1

N2 - The M protein of coronavirus plays a central role in virus assembly, turning cellular membranes into workshops where virus and host factors come together to make new virus particles. We investigated how M structure and organization is related to virus shape and size using cryo-electron microscopy, tomography and statistical analysis. We present evidence that suggests M can adopt two conformations and that membrane curvature is regulated by one M conformer. Elongated M protein is associated with rigidity, clusters of spikes and a relatively narrow range of membrane curvature. In contrast, compact M protein is associated with flexibility and low spike density. Analysis of several types of virus-like particles and virions revealed that S protein, N protein and genomic RNA each help to regulate virion size and variation, presumably through interactions with M. These findings provide insight into how M protein functions to promote virus assembly.

AB - The M protein of coronavirus plays a central role in virus assembly, turning cellular membranes into workshops where virus and host factors come together to make new virus particles. We investigated how M structure and organization is related to virus shape and size using cryo-electron microscopy, tomography and statistical analysis. We present evidence that suggests M can adopt two conformations and that membrane curvature is regulated by one M conformer. Elongated M protein is associated with rigidity, clusters of spikes and a relatively narrow range of membrane curvature. In contrast, compact M protein is associated with flexibility and low spike density. Analysis of several types of virus-like particles and virions revealed that S protein, N protein and genomic RNA each help to regulate virion size and variation, presumably through interactions with M. These findings provide insight into how M protein functions to promote virus assembly.

U2 - 10.1016/j.jsb.2010.11.021

DO - 10.1016/j.jsb.2010.11.021

M3 - Journal article

C2 - 21130884

SN - 1047-8477

VL - 174

SP - 11

EP - 22

JO - Journal of Structural Biology

JF - Journal of Structural Biology

IS - 1

ER -

A Structural analysis of M protein in coronavirus assembly and morphology

Abstract

Access to Document

Fingerprint

Cite this