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Bacterial Bonding Technique Devised to Simplify Vaccines

Streptococcus pyogenes bacteria

Streptococcus pyogenes bacteria (Centers for Disease Control and Prevention)

20 January 2016. Researchers at Oxford University developed and tested engineered proteins from bacteria that in lab tests make vaccine design simpler and more reliable. The team from the lab of biochemistry professor Mark Howarth published its proof-of-concept results in the 19 January issue of Scientific Reports.

Howarth — with immunologists from Oxford’s Jenner Institute that studies vaccines and University of Bern in Switzerland — are seeking new techniques for creating vaccines that simplify the process and increase their likelihood of success. Current methods often depend on virus-like particles, proteins and other components from viruses that do not cause disease, but still induce an immune response.

Virus-like particles, however, have a mixed record of success, with configurations of these particles in many cases not able to produce immunity. The authors point to malaria, HIV, and some cancer immunotherapies as examples where vaccines face false starts, delays, and high costs.

Karl Brune, a doctoral candidate in Howarth’s lab and first author, devised a technique that aims to make the assembly of vaccines simpler and more reliable. Brune’s solution uses proteins from Streptococcus pyogenes bacteria, engineered to act as bonding agents between virus-like particles, and are not considered pathogenic.

The two engineered proteins are called SpyCatcher and SpyTag. SpyCatcher acts as a protein base connecting with SpyTag peptides forming a spontaneous and stable organic bond. In assembling vaccines, virus-like particles are biologically encoded with SpyCatcher proteins. Antigens, proteins that induce production of antibodies in the immune system, are then attached to SpyTag peptides, which in turn bond solidly to SpyCatcher with virus-like particles.

The Oxford team tested the SpyCatcher-SpyTag technology in lab cultures and mice, creating prototype vaccines using CIDR and Pfs25 antigens associated with malaria. In each case, the vaccines created with the SpyCatcher-SpyTag technology induced a strong immune response. The researchers also found the SpyCatcher-SpyTag proteins could also fuse with peptides derived from epidermal growth factor receptor mutations associated with glioblastoma, a form of brain cancer, which suggests the technology’s potential in cancer immunotherapy.

The team plans to test SpyCatcher-SpyTag technology with more types of diseases and under more live rather than lab conditions. In addition, Oxford University’s technology transfer office applied for a European patent on the underlying peptide-bonding technology, listing Mark Howarth as the inventor.

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