TY - JOUR

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

A1 - Neuman,Benjamin W.

A1 - Kiss,Gabriella

A1 - Kunding,Andreas Hjarne

A1 - Bhella,David

A1 - Baksh,M. Fazil

A1 - Connelly,Stephen

A1 - Droese,Ben

A1 - Klaus,Joseph P.

A1 - Makino,Shinji

A1 - Sawicki,Stanley G.

A1 - Siddell,Stuart G.

A1 - Stamou,Dimitrios G.

A1 - Wilson,Ian A.

A1 - Kuhn,Peter

A1 - Buchmeier,Michael J.

AU - Neuman,Benjamin W.

AU - Kiss,Gabriella

AU - Kunding,Andreas Hjarne

AU - Bhella,David

AU - Baksh,M. Fazil

AU - Connelly,Stephen

AU - Droese,Ben

AU - Klaus,Joseph P.

AU - Makino,Shinji

AU - Sawicki,Stanley G.

AU - Siddell,Stuart G.

AU - Stamou,Dimitrios G.

AU - Wilson,Ian A.

AU - Kuhn,Peter

AU - Buchmeier,Michael J.

PB - Academic Press

PY - 2011

Y1 - 2011

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.<br /> Keyword: Cryo-electron microscopy,Viral matrix protein,Coronavirus,Pleomorphic virus structure,Cryo-electron tomography

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.<br /> Keyword: Cryo-electron microscopy,Viral matrix protein,Coronavirus,Pleomorphic virus structure,Cryo-electron tomography

U2 - 10.1016/j.jsb.2010.11.021

DO - 10.1016/j.jsb.2010.11.021

JO - Journal of Structural Biology

JF - Journal of Structural Biology

SN - 1047-8477

VL - 174

SP - 11

EP - 22

ER -