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Binding of a pocket factor to Hepatitis B virus capsids changes the rotamer conformation of Phenylalanine 97
Zitieren Sie bitte immer diese URN: urn:nbn:de:bvb:20-opus-248565
- (1) Background: During maturation of the Hepatitis B virus, a viral polymerase inside the capsid transcribes a pre-genomic RNA into a partly double stranded DNA-genome. This is followed by envelopment with surface proteins inserted into a membrane. Envelopment is hypothetically regulated by a structural signal that reports the maturation state of the genome. NMR data suggest that such a signal can be mimicked by the binding of the detergent Triton X 100 to hydrophobic pockets in the capsid spikes. (2) Methods: We have used electron(1) Background: During maturation of the Hepatitis B virus, a viral polymerase inside the capsid transcribes a pre-genomic RNA into a partly double stranded DNA-genome. This is followed by envelopment with surface proteins inserted into a membrane. Envelopment is hypothetically regulated by a structural signal that reports the maturation state of the genome. NMR data suggest that such a signal can be mimicked by the binding of the detergent Triton X 100 to hydrophobic pockets in the capsid spikes. (2) Methods: We have used electron cryo-microscopy and image processing to elucidate the structural changes that are concomitant with the binding of Triton X 100. (3) Results: Our maps show that Triton X 100 binds with its hydrophobic head group inside the pocket. The hydrophilic tail delineates the outside of the spike and is coordinated via Lys-96. The binding of Triton X 100 changes the rotamer conformation of Phe-97 in helix 4, which enables a π-stacking interaction with Trp-62 in helix 3. Similar changes occur in mutants with low secretion phenotypes (P5T and L60V) and in a mutant with a pre-mature secretion phenotype (F97L). (4) Conclusion: Binding of Triton X 100 is unlikely to mimic structural maturation because mutants with different secretion phenotypes show similar structural responses.…
Autor(en): | Cihan Makbul, Christian Kraft, Matthias Grießmann, Tim Rasmussen, Kilian Katzenberger, Melina Lappe, Paul Pfarr, Cato Stoffer, Mara Stöhr, Anna-Maria Wandinger, Bettina Böttcher |
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URN: | urn:nbn:de:bvb:20-opus-248565 |
Dokumentart: | Artikel / Aufsatz in einer Zeitschrift |
Institute der Universität: | Fakultät für Biologie / Theodor-Boveri-Institut für Biowissenschaften |
Fakultät für Biologie / Rudolf-Virchow-Zentrum | |
Sprache der Veröffentlichung: | Englisch |
Titel des übergeordneten Werkes / der Zeitschrift (Englisch): | Viruses |
ISSN: | 1999-4915 |
Erscheinungsjahr: | 2021 |
Band / Jahrgang: | 13 |
Heft / Ausgabe: | 11 |
Aufsatznummer: | 2115 |
Originalveröffentlichung / Quelle: | Viruses (2021) 13:11, 2115. https://doi.org/10.3390/v13112115 |
DOI: | https://doi.org/10.3390/v13112115 |
Allgemeine fachliche Zuordnung (DDC-Klassifikation): | 5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie |
6 Technik, Medizin, angewandte Wissenschaften / 61 Medizin und Gesundheit / 610 Medizin und Gesundheit | |
Freie Schlagwort(e): | Hepatitis B Virus; Triton X 100; electron cryo-microscopy; envelopment; isothermal titration calorimetry; maturation signal; pocket factor; single strand blocking |
Datum der Freischaltung: | 24.11.2022 |
Datum der Erstveröffentlichung: | 20.10.2021 |
Lizenz (Deutsch): | CC BY: Creative-Commons-Lizenz: Namensnennung 4.0 International |