earticle

영어

Envelope antigen gene of Hepatitis B virus (HBV) consists of successive preS1, preS2, and S regions. Depending on alternative translation starting from each initiation codon of the corresponding regions, three envelop proteins, termed large (L), middle (M) and small (S) proteins, are synthesized. Dobeel Corp. developed improved HBV vaccine as the form of virus-like particle (VLP) comprising all three types of envelope proteins which were expressed from Chinese hamster ovary (CHO) cell. N-glycan profiles of total VLP as well as each L, M, and S protein were analyzed by using normal phase high performance liquid chromatography (NP-HPLC) after labeling of fluorescnece tag and matrix assisted laser desorption/ionization time-of-flight (MALDI-TOF) spectrometry. Sialylated bi-antennary glycans with core fucose (NeuAc1-2 Gal2Man3GlcNAc4Fuc1) were detected as major peaks while bi-antennary neutral glycans terminated with galatose and sialylated tri- and tetra-antennary glycans were also detected in significant amounts. Especially, higher amount of bi-antennary glycan structures were observed in S and M protein whereas the quantities of tri- and tetra-antennary structures were more abundant in L protein. O-glycan, predicted at preS2 region, was also analyzed after the release from unfolded VLP by hydrazinolysis method. Its glycan profile showed that mucin-type sialylated core 1 glycans (NeuAc1-2GalGalNAc) exist in major populations.