High-yield vesicle-packaged recombinant protein production from E. coli

Eastwood et al. (2023)
Cell Reports Methods
This study describes the development and application of a Vesicle Nucleating peptide (VNp) for the production and release of recombinant protein filled vesicles from E. coli. This technology was invented and developed by the Mulvihill group, and allows high yield expression of a wide range of proteins (including those challenging to express), and simplified downstream processing (purification). This globally patented technology is freely available to use by non-profit organisations, and has been adopted by hundreds of labs throughout the world.

Simple recombinant monoclonal antibody production from E. coli

Baker et al. (2025)
Open Biology
This study demonstrates utilisation of the VNp-expression system to produce functional monoclonal antibodies (mAbs) from E. coli, negating the need to use expensive mammalian cell culture. The VNp has since been applied to a range of mAbs, and both simplifies and reduces cost of mAbs production for research and diagnostic applications. This provides evidence of the potential and capacity of the VNp system.

A High-Throughput Multiwell-Plate based Approach for the combined Expression, Export and Assay of Recombinant Proteins

Baker & Mulvihill (2025)
Current Protocols
This paper describes the application of the VNp technology to produce the first High Throughput Screen (HTS) multi-well plate compatible system that directly exports assay-ready protein into culture media in a single step. This protocol can be applied to a wide range of high-throughput research and development screening applications, ranging from streamlining protein production, identification of activity enhancing mutations, to ligand screening for basic research, biotechnological and drug discovery applications.

An enhanced recombinant amino-terminal acetylation system and novel in vivo high-throughput screen for molecules affecting α-synuclein oligomerisation

Eastwood et al. (2017)
FEBS Letters
The vast majority of eukaryote proteins are amino-terminally acetylated to facilitate folding, stability and functionality of proteins. This study describes the further development of a recombinant expression system allowing production of amino-terminally acetylated proteins from E. coli, something bacteria cannot normally do. This project builds upon an earlier 2010 study from the Mulvihill group (180 citations; plasmids sent to > 200 labs), that has been adopted by researchers across the world to produce diverse functional proteins for research.

Optimized Production and Analysis of Recombinant Protein-Filled Vesicles from E. coli

Streather et al. (2023)
JoVE
A detailed protocol for using the VNp system.

Targeted Amino-Terminal Acetylation of Recombinant Proteins in E. coli

Johnson et al. (2010)
PLoS One
The original Mulvihill group acetylation study.