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Mutational profiling of the variability of individual amino acid positions in the hepatitis B virus matrix domain.

Virology 458-459, 183-189 (2014)
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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 Artikelnummer: , Supplement: ,
Verlag Elsevier
Verlagsort San Diego
Begutachtungsstatus Peer reviewed