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

R. D. Puspitasari, Usman Sumo Friend

Research output: Contribution to journalConference articlepeer-review

1 Citation (Scopus)

Abstract

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).

Original languageEnglish
Article number012043
JournalIOP Conference Series: Materials Science and Engineering
Volume188
Issue number1
DOIs
Publication statusPublished - 2 May 2017
EventInternational Symposium on Current Progress in Functional Materials 2016, ISCPFM 2016 - Bali, Indonesia
Duration: 26 Jul 201627 Jul 2016

Keywords

  • DENV3
  • glutamine
  • mutation
  • NS5
  • threonine

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