Analysis Affinity of mAb III/V with PNGase F-Deglycosylated Pfs48F1 by KinExA (CAT#: STEM-MB-0041-CJ)

Introduction

N-linked glycosylation is a post-translational modification which is critical for correct folding, stability and biological activity of many proteins including recombinant subunit vaccines and therapeutic proteins produced in heterologous expression systems. Some eukaryotic (as well as bacterial) proteins may not contain N-glycans in the native host, but their proteins may contain multiple potential glycosylation sites that are aberrantly glycosylated when these proteins are expressed in heterologous eukaryotic expression systems, potentially leading to imp+I91aired functional activity. A bacterial PNGase F (Peptide: N-glycosidase F) in combination with a target protein of interest. PNGase F is a 34.8-kDa enzyme secreted by a Gram-negative bacterium Flavobacterium meningosepticum. It cleaves a bond between the innermost GlcNAc and asparagine residues of high-mannose, hybrid and complex oligosaccharides in N-linked glycop.The study showed that the malaria vaccine candidate Pfs48F1 produced by in vivo deglycation plants was significantly stronger than the glycation form of Pfs48F1 produced by plants, using monoclonal antibodies I, III, and V cultured against various epitopes (I, III, and V) native to Plasmodium falciparum.