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Homogeneous Glycoconjugate Produced by Combined Unnatural Amino Acid Incorporation and Click-Chemistry for Vaccine Purposes
Published on: December 19, 2020
Glyceraldehyde-3-phosphate dehydrogenase, an immunogenic Streptococcus equi ssp. zooepidemicus adhesion protein and
Qiang Fu1, Zigong Wei, Xiaohong Liu
1State Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-sen University, Guangzhou 510006, PR China.
Abstract:
Streptococcus equi ssp. zooepidemicus (Streptococcus zooepidemicus, SEZ) is an important pathogen associated with opportunistic infections of a wide range of species, including pigs and humans. The absence of a suitable vaccine makes it difficult to control SEZ infection. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has been previously identified as an immunogenic protein using immunoproteomic techniques. In the present study, we confirmed that the sequence of GAPDH was highly conserved with other Streptococcus spp. The purified recombinant GAPDH could elicit a significant humoral antibody response in mice and confer significant protection against challenge with a lethal dose of SEZ. GAPDH could adhere to the Hep-2 cells, confirmed by flow cytometry, and inhibit adherence of SEZ to Hep-2 cells in an adherence inhibition assay. In addition, real-time PCR demonstrated that GAPDH was induced in vivo following infection of mice with SEZ. These suggest that GAPDH could play an important role in the pathogenesis of SEZ infection and could be a target for vaccination against SEZ.
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