In silico mutation analysis of non-structural protein-5 (NS5) dengue virus

International Symposium on Current Progress in Functional Materials

Puspitasari, R.D.^1 ; Tambunan, U.S.F.^1

Bioinformatics Research Group, Department of Chemistry, Faculty of Mathematics, Natural Sciences Universitas Indonesia, Kampus UI Depok, Depok

16424, Indonesia^1

关键词: DENV3;    Enzymatic activities;    glutamine;    Methyltransferases;    mutation;    Mutation frequency;    S adenosyl l methionines;    threonine;   

Others  :  https://iopscience.iop.org/article/10.1088/1757-899X/188/1/012043/pdf
DOI  :  10.1088/1757-899X/188/1/012043

来源: IOP

【 摘 要 】

Dengue fever is a world disease. It is endemic in more than 100 countries. Information about the effect of mutations in the virus is important in drug design and development. In this research, we studied the effect of mutation on NS5 dengue virus. NS5 is the large protein containing 67% amino acid similarity in DENV 1-4 and has multifunctional enzymatic activities. Dengue virus is an RNA virus that has very high mutation frequency with an average of 100 times higher than DNA mutations, and the accumulation of mutations will be possible to generate the new serotype. In this study, we report that mutation occurs in NS5 of DENV serotype 3, glutamine mutates into methionine at position 10 and threonine mutates into isoleucine at position 55. These residues are part of the domain named S-Adenosyl-L-Methionine-Dependent Methyltransferase (IPR029063).