Osmolyte-mediated encapsulation of proteins inside MS2 viral capsids.

ABSTRACT: The encapsulation of enzymes in nanometer-sized compartments has the potential to enhance and control enzymatic activity, both in vivo and in vitro. Despite this potential, there is little quantitative data on the effect of encapsulation in a well-defined compartment under varying conditions. To gain more insight into these effects, we have characterized two improved methods for the encapsulation of heterologous molecules inside bacteriophage MS2 viral capsids. First, attaching DNA oligomers to a molecule of interest and incubating it with MS2 coat protein dimers yielded reassembled capsids that packaged the tagged molecules. The addition of a protein-stabilizing osmolyte, trimethylamine-N-oxide, significantly increased the yields of reassembly. Second, we found that expressed proteins wit

SUBMITTER: Glasgow JE 

PROVIDER: S-EPMC3479312 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature