Home
Deutsch
Advanced Search
Browse by ...
Publication overview
Contact persons
Help
DOI
PMC
 |
|
Open Access Green as soon as Postprint is submitted to ZB.
Mutational profiling of the variability of individual amino acid positions in the hepatitis B virus matrix domain.
Virology 458-459, 183-189 (2014)
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.
Altmetric
Additional Metrics?
Edit extra informations
Login
Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Envelopment ; Hepatitis B Virus ; Large Surface Protein ; Matrix Domain; Large Envelope Protein; Pre-s Domain; Transmembrane Topology; Virion Formation; Surface; Morphogenesis; Capsids; Replication; Sequence
ISSN (print) / ISBN
0042-6822
e-ISSN
0042-6822
Journal
Virology
Quellenangaben
Volume: 458-459,
Issue: 1,
Pages: 183-189
Publisher
Elsevier
Publishing Place
San Diego
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Virology (VIRO)