| 학회 |
한국화학공학회 |
| 학술대회 |
2003년 가을 (10/24 ~ 10/25, 한양대학교) |
| 권호 |
9권 2호, p.2153 |
| 발표분야 |
생물화공 |
| 제목 |
The influence of glycosylation on secretion, stability, and immunogenicity of recombinant HBV pre-S antigen synthesized in Saccharomyces cerevisiae |
| 초록 |
Three types of recombinant pre-S antigens (i.e., pre-S1S2) of hepatitis B virus (HBV) were synthesized in Saccharomyces cerevisiae and secreted into medium : wild type (pre-S1S2) and two mutant antigens, pre-S1°S2 (Asn15Gln) and pre-S1°S2° (Asn15Gln, Asn123Gln). The recombinant pre-S1S2 and pre-S1°S2 were secreted in the hyper-mannosylated form, while the recombinant pre-S1°S2° was produced without N-glycosylation. It has been demonstrated that the two particular N-linked glycans at Asn15 and Asn123 interfered with the B-cell response to the HBV-derived pre-S1S2, resulting in low titers of pre-S1S2-neutralizing antibodies. This problem was overcome by eliminating both of the N-glycosylation signals. But, the recombinant pre-S1°S2° showed two major problems: (1) inefficient Kex2 cleavage in the secretory pathway and (2) the proteolytic degradation by yeast proteases. The efficiency of Kex2 cleavage increased dramatically by removing N-glycosylation signal in the synthetic prosequence, but the proteolysis of pre-S1°S2° was somewhat inevitable. |
| 저자 |
박진승1, 이지원1, 문제영2, 김기용2, 문홍모2
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| 소속 |
1고려대, 2두비엘 |
| 키워드 |
HBV pre-S; Secretion; N-glycosylation; Immunogenicity; Proteolysis |
| E-Mail |
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| 원문파일 |
초록 보기 |
