The pre-S2 domain of the hepatitis B virus is dispensable for infectivity but serves a spacer function for L-protein-connected virus assembly
The envelope of the human hepatitis B virus (HBV) contains three membrane proteins (L, M, and S). They accomplish different functions in HBV infectivity and nucleocapsid envelopment. Infectivity determinants have been assigned to the N-terminal part of the pre-S1 domain of the L protein and the anti...
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| Hauptverfasser: | , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
3 February 2010
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| In: |
Journal of virology
Year: 2010, Jahrgang: 84, Heft: 8, Pages: 3879-3888 |
| ISSN: | 1098-5514 |
| DOI: | 10.1128/JVI.02528-09 |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1128/JVI.02528-09 Verlag, lizenzpflichtig, Volltext: https://journals.asm.org/doi/10.1128/JVI.02528-09 
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| Verfasserangaben: | Yi Ni, Jessika Sonnabend, Stefan Seitz, and Stephan Urban |
| Zusammenfassung: | The envelope of the human hepatitis B virus (HBV) contains three membrane proteins (L, M, and S). They accomplish different functions in HBV infectivity and nucleocapsid envelopment. Infectivity determinants have been assigned to the N-terminal part of the pre-S1 domain of the L protein and the antigenic loop of the S domain in the L and/or S protein. Nucleocapsid envelopment requires a C-terminal sequence within pre-S1, including the five N-terminal amino acids of pre-S2 as part of the L protein. However, the role of the M protein and the pre-S2 domain of the L protein are not entirely understood. We addressed this question and analyzed assembly competence and infectivity of viruses that lack the M protein and, at the same time, carry alterations in the pre-S2 domain of L. These include deletions, in part frameshift mutations and a randomization of virtually the entire pre-S2 sequence. We found that the M protein is dispensable for HBV in vitro infectivity. Viruses that lack the M protein and contain a mostly randomized pre-S2 sequence assemble properly and are infectious in HepaRG cells and primary human hepatocytes. While deletions of 20 amino acids in the pre-S2 domain of L protein allowed the production of infectious virions, more extended deletions interfered with assembly. This indicates that the pre-S2 domain of the L protein serves an important role for virus assembly, presumably as a spacer that supports conformational changes of L protein but does not participate as part of the M protein or as a subdomain of the L protein in virus entry. |
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| Beschreibung: | Gesehen am 15.05.2023 |
| Beschreibung: | Online Resource |
| ISSN: | 1098-5514 |
| DOI: | 10.1128/JVI.02528-09 |