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TitleBinding of a Pocket Factor to Hepatitis B Virus Capsids Changes the Rotamer Conformation of Phenylalanine 97.
Journal, issue, pagesViruses, Vol. 13, Issue 11, Year 2021
Publish dateOct 20, 2021
AuthorsCihan Makbul / Christian Kraft / Matthias Grießmann / Tim Rasmussen / Kilian Katzenberger / Melina Lappe / Paul Pfarr / Cato Stoffer / Mara Stöhr / Anna-Maria Wandinger / Bettina Böttcher /
PubMed Abstract(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 ...(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.
External linksViruses / PubMed:34834922 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 3.2 Å
Structure data

EMDB-13726, PDB-7pz9:
HBc-F97L premature secretion phenotype
Method: EM (single particle) / Resolution: 2.8 Å

EMDB-13728, PDB-7pzi:
HBc-F97L (premature secretion phenotype) in complex with Triton X-100
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-13731, PDB-7pzk:
HBc-WT in complex with Triton X-100
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-13732, PDB-7pzl:
HBc-F97L premature secretion phenotype
Method: EM (single particle) / Resolution: 2.8 Å

EMDB-13733, PDB-7pzm:
HBc-P5T in complex with X-100
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-13734, PDB-7pzn:
wt HBc capsid like particles in complex with inhibitory peptide SLLGRM and Triton X-100
Method: EM (single particle) / Resolution: 3.2 Å

Chemicals

ChemComp-TRT:
FRAGMENT OF TRITON X-100 / detergent*YM

Source
  • Hepatitis B virus ayw/France/Tiollais/1979
  • hepatitis b virus genotype d subtype ayw (isolate france/tiollais/1979)
  • escherichia coli (E. coli)
KeywordsVIRUS LIKE PARTICLE / Icosahedral capsid like particle with T=4 / VIRAL PROTEIN / Pocket binding factor mimic Triton X-100 / premature secretion phenotype / hepatitis B virus / HBc-WT in complex with Triton X-100 / HBc-L60V (low secretion phenotype) in complex with Triton X-100 / HBc-P5T (low secretion phenotype) in complex with Triton X-100 / wt HBc capsid / Triton X-100 / inhibitory peptide SLLGRM / Cryo-EM

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