Abstract
The outermost surface of bacterial pathogens consists primarily of complex carbohydrate structures—polysaccharides, glycolipids, and glycoproteins. To raise a long-lasting and effective immune response against carbohydrate antigens, they generally require covalent attachment to an immunogenic carrier protein—a so-called glycoconjugate vaccine. One hurdle to the development of glycoconjugate vaccines is that carbohydrate antigens remain inaccessible to recombinant production. Thus, the carbohydrate antigen is typically purified from the pathogen and then chemically conjugated to an immunogenic protein. Recent developments in the field of bacterial glycoengineering have opened the opportunity for total recombinant production of glycoconjugate vaccines. In this method, we describe the production of proteinaceous, virus-like particles (VLPs) bearing the conserved N-glycan of Actinobacillus pleuropneumoniae, the causative agent of porcine pleuropneumoniae.
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Acknowledgments
We are grateful to Professor Markus Aebi for his guidance in study design and comments on the manuscript, Dr. Miriam Lucas and ScopeM for assistance with transmission electron microscopy, and Dr. Serge Chesnov and the FGCZ for mass spectrometric analysis. This research was funded through a Bridge Discovery grant and by an ETH Zurich Career Seed Grant (SEED-33 16-1) awarded to T.G.K.
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Oi, K.K., Kloter, T.A., Keys, T.G. (2021). Biosynthesis of Glycoconjugate Virus-like Particles (VLPs). In: Pfeifer, B.A., Hill, A. (eds) Vaccine Delivery Technology. Methods in Molecular Biology, vol 2183. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-0795-4_11
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DOI: https://doi.org/10.1007/978-1-0716-0795-4_11
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