Spacer Domain in Hepatitis B Virus Polymerase: Plugging a Hole or Performing a Role?

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Abstract

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.
Original languageEnglish
JournalJournal of Virology
Volume96
Issue number9
DOIs
Publication statusPublished - 12 Apr 2022

Bibliographical note

Funding Information:
P.C.M. is funded by a Wellcome intermediate fellowship, reference no. 110110/Z/15/ Z. A.L.M. has received NIHR Research Capability Funding (RCF) from the University of Oxford. This research was funded in whole, or in part, by the Wellcome Trust. For the purpose of Open Access, the author has applied a CC BY public copyright license to any Author Accepted Manuscript version arising from this submission.

Publisher Copyright:
Copyright © 2022 Pley et al.

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