The investigation of the GlcNAc glycosylation effect on molecular structure and solubility property in type 2 Dengue virus envelop protein

• Main Authors: Hsien-Chang Chen, 陳憲璋
• Other Authors: none
• Format: Others
• Language: zh-TW
• Published: 2004
• Online Access: http://ndltd.ncl.edu.tw/handle/91182026431453884901

碩士 === 國立中央大學 === 化學研究所 === 92 === 英 文 摘 要 Dengue virus, a member of the flavivirus family, which has four different serotypes in the most important arthropod-borne human pathogen. Classic dengue fever (DF) is an acute self-limited febrile illness. It is estimated that up to 100 million cases occur annually. In addition, a severe form of disease, dengue hemorrhagic fever（DHF）, has emerged causing approach 500,000 cases worldwide each year. The death rate of DHF is about 10-50％, is a terrible infectious disease. Dengue virus contains envelope protein that infects cell by membrane fusion. Envelope protein is a glycoprotein. For type 2 Dengue virus, the envelope protein has two glycosylation sites：Asn-67 and Asn-153. The glycan of Asn-67 is monosaccharide, N-Acetyl-glucosamine, that is unique among other glycoproteins. Therefore, we were focusing on the studies of specific role of this monosaccharide in the envelope protein. In the thesis, we synthesized a number of peptide that covers Asn-67 with glycosylation and without glycosylation. We characterized the protein secondary structure by means of chemical shift index analyses using liquid-state NMR, and to detect the solubility before and after glycosylation. We found that glycosylation serves two functions in the peptide we studied. First, the glycosylation is able to stabilize the peptide secondary structure in a preference of forming β-strain. Secondly, solubility of the peptide is significantly enhanced after glycosylation. This study might help to better understand the biological role of glycosylation in the envelope protein of type 2 Dengue virus.