Status: Bibliographieeintrag
Standort: ---
Exemplare:
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| Online-Ressource |
Verfasst von: | Ni, Yi [VerfasserIn]  |
| Sonnabend, Jessika [VerfasserIn]  |
| Seitz, Stefan [VerfasserIn]  |
| Urban, Stephan [VerfasserIn]  |
Titel: | The pre-S2 domain of the hepatitis B virus is dispensable for infectivity but serves a spacer function for L-protein-connected virus assembly |
Verf.angabe: | Yi Ni, Jessika Sonnabend, Stefan Seitz, and Stephan Urban |
E-Jahr: | 2010 |
Jahr: | 3 February 2010 |
Umfang: | 10 S. |
Fussnoten: | Gesehen am 15.05.2023 |
Titel Quelle: | Enthalten in: Journal of virology |
Ort Quelle: | Baltimore, Md. : Soc., 1967 |
Jahr Quelle: | 2010 |
Band/Heft Quelle: | 84(2010), 8, Seite 3879-3888 |
ISSN Quelle: | 1098-5514 |
Abstract: | 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. |
DOI: | doi:10.1128/JVI.02528-09 |
URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext: https://doi.org/10.1128/JVI.02528-09 |
| Volltext: https://journals.asm.org/doi/10.1128/JVI.02528-09 |
| DOI: https://doi.org/10.1128/JVI.02528-09 |
Datenträger: | Online-Ressource |
Sprache: | eng |
K10plus-PPN: | 1845369033 |
Verknüpfungen: | → Zeitschrift |
¬The¬ pre-S2 domain of the hepatitis B virus is dispensable for infectivity but serves a spacer function for L-protein-connected virus assembly / Ni, Yi [VerfasserIn]; 3 February 2010 (Online-Ressource)
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