Abstract:
:The hepatitis B virus (HBV) is formed by budding. A stretch of 22 amino acids (aa) (matrix domain, MD, R103 - S124) in the large envelope protein L is crucial for virion formation and probably establishes contact to the nucleocapsid. Here, we assess the impact of sequence variations at numerous individual aa positions within the MD on virion formation. We generated panels of L mutants covering all 19 possible aa for 11 positions and tested the capacity of these mutants to rescue virus production by an L-defective HBV genome. At four positions (L112, R113, P117, W122), any replacement of the wild type (WT) aa reduced virus assembly to undetectable levels. Virus production was strongly diminished by substitutions at five other positions (R103, T106, S115, H116, A119). Only two tested positions (D114, Q118) tolerated several substitutions. The restricted positions may represent promising targets for the development of novel antiviral strategies.
journal_name
Virologyjournal_title
Virologyauthors
Schittl B,Bruss Vdoi
10.1016/j.virol.2014.04.030subject
Has Abstractpub_date
2014-06-01 00:00:00pages
183-9eissn
0042-6822issn
1096-0341pii
S0042-6822(14)00153-6journal_volume
458-459pub_type
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