Pharmacomodulation of a ligand targeting the HBV capsid hydrophobic pocket.
Mathilde Briday, François Hallé, Lauriane Lecoq, Sylvie Radix, Juliette Martin, Roland Montserret, Marie Dujardin, Marie-Laure Fogeron, Michael Nassal, Beat H Meier and 2 more
Article in Chemical science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
2 · The registry
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
5 · Who and what money
Authors and funding
12 authors.
Mathilde BridayMolecular Microbiology and Structural Biochemistry (MMSB) UMR 5086 CNRS/Université de Lyon, Labex Ecofect 7 Passage du Vercors 69367 Lyon France lauriane.lecoq@ibcp.fr anja.bockmann@ibcp.fr.
François HalléUniversité de Lyon, Université Lyon 1, CNRS UMR 5246 Institut de Chimie et Biochimie Moléculaires et Supramoléculaires (ICBMS), Faculté de Pharmacie-ISPB 8 Avenue Rockefeller FR-69373 Lyon Cedex 08 France thierry.lomberget@univ-lyon1.fr.
Lauriane LecoqMolecular Microbiology and Structural Biochemistry (MMSB) UMR 5086 CNRS/Université de Lyon, Labex Ecofect 7 Passage du Vercors 69367 Lyon France lauriane.lecoq@ibcp.fr anja.bockmann@ibcp.fr.
Sylvie RadixUniversité de Lyon, Université Lyon 1, CNRS UMR 5246 Institut de Chimie et Biochimie Moléculaires et Supramoléculaires (ICBMS), Faculté de Pharmacie-ISPB 8 Avenue Rockefeller FR-69373 Lyon Cedex 08 France thierry.lomberget@univ-lyon1.fr.
Juliette MartinMolecular Microbiology and Structural Biochemistry (MMSB) UMR 5086 CNRS/Université de Lyon, Labex Ecofect 7 Passage du Vercors 69367 Lyon France lauriane.lecoq@ibcp.fr anja.bockmann@ibcp.fr.
Roland MontserretMolecular Microbiology and Structural Biochemistry (MMSB) UMR 5086 CNRS/Université de Lyon, Labex Ecofect 7 Passage du Vercors 69367 Lyon France lauriane.lecoq@ibcp.fr anja.bockmann@ibcp.fr.
Marie DujardinMolecular Microbiology and Structural Biochemistry (MMSB) UMR 5086 CNRS/Université de Lyon, Labex Ecofect 7 Passage du Vercors 69367 Lyon France lauriane.lecoq@ibcp.fr anja.bockmann@ibcp.fr.
Marie-Laure FogeronMolecular Microbiology and Structural Biochemistry (MMSB) UMR 5086 CNRS/Université de Lyon, Labex Ecofect 7 Passage du Vercors 69367 Lyon France lauriane.lecoq@ibcp.fr anja.bockmann@ibcp.fr.
Michael NassalDepartment of Medicine II/Molecular Biology, University Hospital Freiburg, Medical Center, University of Freiburg Freiburg 79106 Germany.ORCID https://orcid.org/0000-0003-2204-9158
Beat H MeierPhysical Chemistry, ETH Zürich 8093 Zürich Switzerland.
Thierry LombergetUniversité de Lyon, Université Lyon 1, CNRS UMR 5246 Institut de Chimie et Biochimie Moléculaires et Supramoléculaires (ICBMS), Faculté de Pharmacie-ISPB 8 Avenue Rockefeller FR-69373 Lyon Cedex 08 France thierry.lomberget@univ-lyon1.fr.ORCID https://orcid.org/0000-0002-4071-0002
Anja BöckmannMolecular Microbiology and Structural Biochemistry (MMSB) UMR 5086 CNRS/Université de Lyon, Labex Ecofect 7 Passage du Vercors 69367 Lyon France lauriane.lecoq@ibcp.fr anja.bockmann@ibcp.fr.ORCID https://orcid.org/0000-0001-8149-7941
Funding
No grant is acknowledged in the PubMed record.
6 · The paper itself
Abstract
Hepatitis B virus (HBV) is a small enveloped retrotranscribing DNA virus and an important human pathogen. Its capsid-forming core protein (Cp) features a hydrophobic pocket proposed to be central notably in capsid envelopment. Indeed, mutations in and around this pocket can profoundly modulate, and even abolish, secretion of enveloped virions. We have recently shown that Triton X-100, a detergent used during Cp purification, binds to the hydrophobic pocket with micromolar affinity. We here performed pharmacomodulation of pocket binders through systematic modifications of the three distinct chemical moieties composing the Triton X-100 molecule. Using NMR and ITC, we found that the flat aromatic moiety is essential for binding, while the number of atoms of the aliphatic chain modulates binding affinity. The hydrophilic tail, in contrast, is highly tolerant to changes in both length and type. Our data provide essential information for designing a new class of HBV antivirals targeting capsid-envelope interactions.
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.
Pharmacomodulation of a ligand targeting the HBV capsid hydrophobic pocket. · full record | OpenQuestion