Spacer domain in hepatitis B virus polymerase: Plugging a hole or performing a role?
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Hepatitis B virus (HBV) polymerase is divided into terminal protein, spacer, reverse transcriptase, and RNase domains. Spacer has previously been considered dispensable, merely acting as a tether between other domains or providing plasticity to accommodate deletions and mutations. We explore evidence for the role of spacer sequence, structure, and function in HBV evolution and lineage, consider its associations with escape from drugs, vaccines, and immune responses, and review its potential impacts on disease outcomes.
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Journal Journal of Virology
Volume 96
Issue number 9
Pages e00051-22
Available online
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Publisher website (DOI) 10.1128/jvi.00051-22
Europe PubMed Central 35412348
Pubmed 35412348
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