Engineered mutations change the structure and stability of a virus-like particle.

Abstract:

:The single-coat protein (CP) of bacteriophage Qβ self-assembles into T = 3 icosahedral virus-like particles (VLPs), of interest for a wide range of applications. These VLPs are very stable, but identification of the specific molecular determinants of this stability is lacking. To investigate these determinants along with manipulations that confer more capabilities to our VLP material, we manipulated the CP primary structure to test the importance of various putative stabilizing interactions. Optimization of a procedure to incorporate fused CP subunits allowed for good control over the average number of covalent dimers in each VLP. We confirmed that the disulfide linkages are the most important stabilizing elements for the capsid and that acidic conditions significantly enhance the resistance of VLPs to thermal degradation. Interdimer interactions were found to be less important for VLP assembly than intradimer interactions. Finally, a single point mutation in the CP resulted in a population of smaller VLPs in three distinct structural forms.

journal_name

Biomacromolecules

journal_title

Biomacromolecules

authors

Fiedler JD,Higginson C,Hovlid ML,Kislukhin AA,Castillejos A,Manzenrieder F,Campbell MG,Voss NR,Potter CS,Carragher B,Finn MG

doi

10.1021/bm300590x

subject

Has Abstract

pub_date

2012-08-13 00:00:00

pages

2339-48

issue

8

eissn

1525-7797

issn

1526-4602

journal_volume

13

pub_type

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