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Virology. 2012 Jun 20;428(1):64-9. doi: 10.1016/j.virol.2012.03.017. Epub 2012 Apr 20.

The energetic contributions of scaffolding and coat proteins to the assembly of bacteriophage procapsids.

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  • 1Department of Molecular & Cellular Biochemistry, Indiana University, Bloomington, IN 47405, USA. azlotnic@indiana.edu

Abstract

In vitro assembly of bacteriophage P22 procapsids requires coat protein and sub-stoichiometric concentrations of the internal scaffolding protein. If there is no scaffolding protein, coat protein assembles aberrantly, but only at higher concentrations. Too much scaffolding protein results in partial procapsids. By treating the procapsid as a lattice that can bind and be stabilized by scaffolding protein we dissect procapsid assembly as a function of protein concentration and scaffolding/coat protein ratio. We observe that (i) the coat-coat association is weaker for procapsids than for aberrant polymer formation, (ii) scaffolding protein makes a small but sufficient contribution to stability to favor the procapsid form, and (iii) there are multiple classes of scaffolding protein binding sites. This approach should be applicable to other heterogeneous virus assembly reactions and will facilitate our ability to manipulate such in vitro reactions to probe assembly, and for development of nanoparticles.

Copyright © 2012 Elsevier Inc. All rights reserved.

PMID:
22520942
[PubMed - indexed for MEDLINE]
PMCID:
PMC3351694
Free PMC Article
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