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The role of surface basic amino acids of dengue virus NS 3 helicase in viral RNA replication and enzyme activities
Author(s) -
Chiang PaoYin,
Wu HueyNan
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12232
Subject(s) - helicase , replicon , rna helicase a , viral replication , rna , dengue virus , mutagenesis , biology , mutant , ns3 , rna dependent rna polymerase , chemistry , virology , microbiology and biotechnology , biochemistry , virus , dna , plasmid , hepatitis c virus , gene
Structure‐based mutagenesis analysis on selected conserved surface basic residues of DENV NS 3 helicase was performed using a selectable replicon and recombinant protein. We found a requirement for basic side chains of NS 3 residues #225, #268, and #538 to activate viral RNA replication and ensure RNA ‐stimulated ATP ase activity, and a critical role for R560 and R599 residues in maintaining NS 3 helicase structure, linked to its biological function and catalytic activity. Three screened NS3 second‐site mutations for R225A and R268A/E mutations elevated the functional RNA binding of NS 3 helicase and compensated the replication defect of the original NS 3 mutant replicons.