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

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 evidenc...

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Detalles Bibliográficos
Autores principales: Pley, Caitlin, Lourenço, José, McNaughton, Anna L., Matthews, Philippa C.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Microbiology 2022
Materias:
Gem
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9093120/
https://www.ncbi.nlm.nih.gov/pubmed/35412348
http://dx.doi.org/10.1128/jvi.00051-22
Descripción
Sumario: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.