Protecting enzymatic function through directed packaging into bacterial outer membrane vesicles

Nathan J. Alves, Kendrick B. Turner, Igor L. Medintz, Scott A. Walper

Research output: Contribution to journalArticle

31 Scopus citations

Abstract

Bacteria possess innate machinery to transport extracellular cargo between cells as well as package virulence factors to infect host cells by secreting outer membrane vesicles (OMVs) that contain small molecules, proteins, and genetic material. These robust proteoliposomes have evolved naturally to be resistant to degradation and provide a supportive environment to extend the activity of encapsulated cargo. In this study, we sought to exploit bacterial OMV formation to package and maintain the activity of an enzyme, phosphotriesterase (PTE), under challenging storage conditions encountered for real world applications. Here we show that OMV packaged PTE maintains activity over free PTE when subjected to elevated temperatures (>100-fold more activity after 14 days at 37 °C), iterative freeze-thaw cycles (3.4-fold post four-cycles), and lyophilization (43-fold). We also demonstrate how lyophilized OMV packaged PTE can be utilized as a cell free reagent for long term environmental remediation of pesticide/chemical warfare contaminated areas.

Original languageEnglish (US)
Article number24866
JournalScientific reports
Volume6
DOIs
StatePublished - Apr 27 2016
Externally publishedYes

ASJC Scopus subject areas

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