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Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
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.
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Publikationstyp
Artikel: Journalartikel
Dokumenttyp
Wissenschaftlicher Artikel
Schlagwörter
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
Zeitschrift
Virology
Quellenangaben
Band: 458-459,
Heft: 1,
Seiten: 183-189
Verlag
Elsevier
Verlagsort
San Diego
Nichtpatentliteratur
Publikationen
Begutachtungsstatus
Peer reviewed
Institut(e)
Institute of Virology (VIRO)