A HA2-Fusion tag limits the endosomal release of its protein cargo despite causing endosomal lysis.

ABSTRACT:

Background

Protein transduction domains (PTDs) can be fused to a protein to render it cell-permeable. The delivery efficiencies of PTDs are, however, often poor because PTD-protein conjugates cannot escape from endosomes. A potential solution to this problem consists in adding HA2 analogs to the PTD-protein construct as these peptides can cause endosomal lysis upon acidification of the endosomal lumen. To date, however, the utility of HA2-based PTDs has not been clearly established.

Methods

We investigate the biophysical and cellular properties of the glutamate-rich HA2 analog E5 fused to the model protein TAT-mCherry.

Results

E5-TAT-mCherry causes the release of fluorescent dextrans trapped with the protein inside endosomes. Yet, E5-TAT-mCherry itself is not released

SUBMITTER: Lee YJ 

PROVIDER: S-EPMC3128663 | biostudies-literature | 2011 Aug

REPOSITORIES: biostudies-literature