| Literature DB >> 26269182 |
Yongqian Zhao1, Tingjin Sherryl Soh2, Kitti Wing Ki Chan3, Sarah Suet Yin Fung3, Kunchithapadam Swaminathan4, Siew Pheng Lim5, Pei-Yong Shi5, Thomas Huber6, Julien Lescar7, Dahai Luo8, Subhash G Vasudevan9.
Abstract
We examined the function of the conserved Val/Ile residue within the dengue virus NS5 interdomain linker (residues 263 to 272) by site-directed mutagenesis. Gly substitution or Gly/Pro insertion after the conserved residue increased the linker flexibility and created slightly attenuated viruses. In contrast, Pro substitution abolished virus replication by imposing rigidity in the linker and restricting NS5's conformational plasticity. Our biochemical and reverse genetics experiments demonstrate that NS5 utilizes conformational regulation to achieve optimum viral replication.Entities:
Mesh:
Substances:
Year: 2015 PMID: 26269182 PMCID: PMC4580200 DOI: 10.1128/JVI.01239-15
Source DB: PubMed Journal: J Virol ISSN: 0022-538X Impact factor: 5.103