Premium
Hydrophobic residues of terminal protein domain of hepatitis B virus polymerase contribute to distinct steps in viral genome replication
Author(s) -
Shin Youn-Chul,
Ko Chunkyu,
Ryu Wang-Shick
Publication year - 2011
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 - 10.1016/j.febslet.2011.11.003
Subject(s) - polymerase , biology , viral structural protein , viral replication , hepatitis b virus , virology , hepatitis b virus pre beta , genome , rna dependent rna polymerase , hepatitis b virus dna polymerase , genetics , dna , viral entry , virus , gene
Hepatitis B virus (HBV) replicates its DNA genome via reverse transcription. Precise roles of the terminal protein domain of HBV polymerase remain unknown. To gain insight, we created alanine substitution mutations at hydrophobic residues (i.e., tyrosine, tryptophan, and isoleucine), and then examined the extent by which these mutants carry out viral genome replication. Evidence indicated that three hydrophobic residues of the terminal protein domain (i.e., W74, Y147, and Y173) contribute to distinct steps of viral genome replication: the former two residues are important for viral DNA synthesis, while the latter is important for viral RNA encapsidation.