Mechanisms of assembly and genome packaging in an RNA virus revealed by high-resolution cryo-EM

被引：0
作者：
Emma L. Hesketh
Yulia Meshcheriakova
Kyle C. Dent
Pooja Saxena
Rebecca F. Thompson
Joseph J. Cockburn
George P. Lomonossoff
Neil A. Ranson
机构：
[1] Astbury Centre for Structural Molecular Biology,Department of Biological Chemistry
[2] University of Leeds,undefined
[3] Mount Preston Street,undefined
[4] Leeds LS2 9JT,undefined
[5] UK,undefined
[6] John Innes Centre,undefined
[7] Norwich Research Park,undefined
[8] Colney,undefined
[9] Norwich NR4 7UH,undefined
[10] UK,undefined
[11] Present address: Life Science Division,undefined
[12] Diamond Light Source,undefined
[13] Harwell Science and Innovation Campus,undefined
[14] Fermi Avenue,undefined
[15] Didcot,undefined
[16] Oxfordshire OX11 0QX,undefined
[17] UK,undefined
[18] Present address: Department of Chemistry,undefined
[19] Indiana University,undefined
[20] 800 East Kirkwood Avenue,undefined
[21] Bloomington,undefined
[22] Indiana 47405-7102,undefined
[23] USA,undefined
来源：
Nature Communications | / 6卷
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摘要：
Cowpea mosaic virus is a plant-infecting member of the Picornavirales and is of major interest in the development of biotechnology applications. Despite the availability of >100 crystal structures of Picornavirales capsids, relatively little is known about the mechanisms of capsid assembly and genome encapsidation. Here we have determined cryo-electron microscopy reconstructions for the wild-type virus and an empty virus-like particle, to 3.4 Å and 3.0 Å resolution, respectively, and built de novo atomic models of their capsids. These new structures reveal the C-terminal region of the small coat protein subunit, which is essential for virus assembly and which was missing from previously determined crystal structures, as well as residues that bind to the viral genome. These observations allow us to develop a new model for genome encapsidation and capsid assembly.
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