Please use this identifier to cite or link to this item: https://doi.org/10.1128/JVI.01239-15
Title: Flexibility of NS5 methyltransferase-polymerase linker region is essential for dengue virus replication
Authors: Zhao Y.
Soh T.S.
Chan K.W.K. 
Fung S.S.Y. 
Swaminathan K. 
Lim S.P. 
Shi P.-Y. 
Huber T.
Lescar J. 
Luo D.
Vasudevan S.G. 
Keywords: methyltransferase
nonstructural protein 5
NS5 protein, dengue virus
recombinant protein
virus protein
virus RNA
amino acid substitution
Article
controlled study
Dengue virus
enzyme activity
nonhuman
plasticity
priority journal
protein conformation
protein domain
protein expression
site directed mutagenesis
structure activity relation
virus mutation
virus replication
amino acid sequence
animal
cell line
chemistry
Cricetulus
Dengue virus
gene expression
genetics
human
metabolism
molecular dynamics
molecular genetics
mutation
physiology
protein secondary structure
protein tertiary structure
sequence alignment
virus replication
X ray crystallography
Amino Acid Sequence
Animals
Cell Line
Cricetulus
Crystallography, X-Ray
Dengue Virus
Gene Expression
Humans
Molecular Dynamics Simulation
Molecular Sequence Data
Mutation
Protein Structure, Secondary
Protein Structure, Tertiary
Recombinant Proteins
RNA, Viral
Sequence Alignment
Viral Nonstructural Proteins
Virus Replication
Issue Date: 2015
Publisher: American Society for Microbiology
Citation: Zhao Y., Soh T.S., Chan K.W.K., Fung S.S.Y., Swaminathan K., Lim S.P., Shi P.-Y., Huber T., Lescar J., Luo D., Vasudevan S.G. (2015). Flexibility of NS5 methyltransferase-polymerase linker region is essential for dengue virus replication. Journal of Virology 89 (20) : 10717-10721. ScholarBank@NUS Repository. https://doi.org/10.1128/JVI.01239-15
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.
Source Title: Journal of Virology
URI: https://scholarbank.nus.edu.sg/handle/10635/175294
ISSN: 0022-538X
DOI: 10.1128/JVI.01239-15
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