Synergistic effects of mutations and nanoparticle templating in the self-assembly of cowpea chlorotic mottle virus capsids.
A study of the in vitro nanoparticle-templated assembly of a mutant of cowpea chlorotic mottle virus lacking most of the N-terminal domain (residues 4-37), NDelta34, is presented. Mutant empty proteins assemble into empty capsids with a much broader distribution of sizes than the wild-type virus. This increased flexibility in the assembly outcomes is known to be detrimental for the assembly process in the presence of molecular polyanions. However, when rigid polyanionic cores are used, such as nanoparticles, the assembly process is restored and virus-like particles form. Moreover, the breadth of the nanoparticle-templated capsid size distribution becomes comparable with the wild-type virus size distribution.
Aniagyei
Stella E
SE
Department of Chemistry, Indiana University, Bloomington, Indiana 47405, USA.
Kennedy
Chelsea J
CJ
Stein
Barry
B
Willits
Deborah A
DA
Douglas
Trevor
T
Young
Mark J
MJ
De
Mrinmoy
M
Rotello
Vincent M
VM
Srisathiyanarayanan
D
D
Kao
C Cheng
CC
Dragnea
Bogdan
B
D017795:Bromovirus / Q000737:chemistry* / Q000648:ultrastructure*; D002213:Capsid / Q000737:chemistry* / Q000648:ultrastructure*; D003460:Crystallization / Q000379:methods*; D046911:Macromolecular Substances / Q000737:chemistry; D008422:Materials Testing; D008968:Molecular Conformation; D009154:Mutation; D053758:Nanoparticles / Q000737:chemistry* / Q000648:ultrastructure*; D036103:Nanotechnology / Q000379:methods; D010316:Particle Size; D013499:Surface Properties
D046911:Macromolecular Substances