Our SpyTag/SpyCatcher protein superglue enables us to avoid many of the challenges of binding antigens to virus-like particles
Vaccines rely on the body’s immune system recognising foreign proteins called antigens and responding to them by creating antibodies to fight against infection.
One of the best ways to create an effective vaccine is to make a harmless virus-like particle (VLP) and bind target antigens to it. This then sends a strong signal to the immune system and evokes a strong antibody response.
However, binding antigens to the coat proteins of VLPs in a controlled and reliable way using conventional technology is highly complex. Directly fusing antigens to VLPs often damages the shape of the antigens or VLPs or both, rendering the vaccine ineffective. The alternative of chemically binding the antigens to the VLP is a complex and time-consuming process that does not allow scientists to control the quantity or orientation of antigens that attach to the VLP. This can also compromise the efficacy of the vaccine.
Our proprietary SpyTag/SpyCatcher protein superglue enables us to circumvent these issues. Our unique technology allows us to split a protein from the common bacterium, Streptococcus pyogenes, into two parts: the SpyTag peptide that can be bound to antigens and its partner protein SpyCatcher that binds to the VLP. The two pieces of the original SpyTag/SpyCatcher protein then bind back together in a spontaneous conjugation forming an unbreakable covalent bond.
The process is rapid, efficient, irreversible and extremely versatile. It allows for specific assembly of antigens on VLPs to generate an optimal immune response and can be applied to a wide range of infectious viral, bacterial and parasitical diseases and potentially to cancer and allergies. Both SpyTag and SpyCatcher can be made in any cell type.
Armed with this breakthrough technology we are able to generate a wide range of vaccines candidates.