The R&D team is engaged in the research and development of a multi-new bacterial project, which is applied to the animal experiment of Haemophilus influenza type b (Hib) and pneumonia vaccine, LTh(αK) conjugated to pneumoniae polysaccharide antigen (S. pneumoniae polysaccharide) It has also been confirmed that it can significantly promote the production of IgG antibodies against polysaccharide antigens. Most commercially available products use tetanus toxoid or diphtheria toxoid as the carrier protein for carbohydrate antigens (carrying protein), but tetanus toxoid or diphtheria toxoid is routinely vaccinated for children. If the two proteins are used for vaccine conjugation, it will cause children to suffer in a short period of time. Too much internal vaccination of these two antigens may cause immune interference and affect immune function. The adverse results in this regard have been confirmed and have been published in the literature.

Using genetic engineering methods to transform LT into non-toxic LT(αK) recombinant protein, without chemical detoxification, it can replace tetanus toxoid or diphtheria toxoid as carrier protein. (Currently, only CRM197 (diphtheria toxin) from Wyeth Pharmaceuticals is a genetically modified non-toxic recombinant protein on the market. Others require chemical detoxification before use. Tetanus and diphtheria toxoid are complex to produce and prepare, and LTh(αK) can be used. . coli is mass-produced, the purification process is simple, and the cost is competitive.

This plan has been confirmed by experiments that using LTh(αK) as a carrying protein is more effective than current products and does not interfere with tetanus toxoid or diphtheria toxoid as a routine vaccination plan for children. Therefore, this plan is conducive to product competitiveness.