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Verfasst von:Ni, Yi [VerfasserIn]   i
 Sonnabend, Jessika [VerfasserIn]   i
 Seitz, Stefan [VerfasserIn]   i
 Urban, Stephan [VerfasserIn]   i
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

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