Malaysian researchers have developed a new method for purifying virus-like particles (VLPs), which could remove the need for chromatography columns during manufacture. The team, from the School of Biosciences at Taylor’s University, has developed a method using free metal ions to separate VLPs from unwanted proteins produced in bacteria.

According to Lee Khai Wooi, PhD, a senior lecturer at Taylor’s, the technique could be useful to manufacturers working on vaccines and drug delivery. “This isn’t a high-end technology, but it simplifies the process very much,” he says.

VLPs mimic infection by real viruses, but don’t have a pathogenic viral genome, making them useful for generating an immune response in a vaccine and easily manipulated as nano-vehicles for delivering drugs into cells. Produced in a bioreactor inside cells, such as E. coli, VLPs often need to be separated from junk cellular proteins during the manufacturing process typically using expensive and time-consuming techniques, such as chromatography columns.

Simplifying the process

Lee and his team decided to simplify this process using the polyhistidine tags (His-tags) already used for the purification of recombinant proteins.

Instead of binding the tagged VLPs to nickel-immobilized chromatography columns and removing them afterward, the team experimented with allowing free metal ions to interact with the His-tags. They found that the metal ions bound the tags together, causing the VLPs to form large clumps that could be removed with simple size separation.

“With this method, you don’t need a chromatography column,” explains Lee. “You can do simple size separation using a centrifuge.”

Most industry manufacturers already use centrifuges, he adds, making the technique easy to implement. The team is now planning to investigate the purification of different types of VLPs and to trial their technique in large-scale production of VLPs for vaccines and nanomedicines.

They hope to publish early results from their industrial trials later this year.

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