ArticleNature chemical biology2013
The hepatitis B virus preS1 domain hijacks host trafficking proteins by motif mimicry.
Article in Nature chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 30 citations in OpenAlex.
- Multistep receptor binding of the hepatitis B virus preS1 domain.Nature communications · 2026Article
- Determining buffer conditions for downstream processing of VLP-based recombinant hepatitis B surface antigen using multimodal resins in bind-elute and flow-through purification modes.Scientific reports · 2023Article
- Release of hepatitis B virions is positively regulated by glucose-regulated protein 78 through direct interaction with preS1.Journal of medical virology · 2023Article
- Insights into the client protein release mechanism of the ATP-independent chaperone Spy.Nature communications · 2022Article
- Investigating the disordered regions (MoRFs, SLiMs and LCRs) and functions of mimicry proteins/peptides in silico.PloS one · 2022Article
- The Role of Exosome and the ESCRT Pathway on Enveloped Virus Infection.International journal of molecular sciences · 2021Review
- Article
- Phosphorylation and Alternative Translation on Wheat Germ Cell-Free Protein Synthesis of the DHBV Large Envelope Protein.Frontiers in molecular biosciences · 2019Article
- Recognition by host nuclear transport proteins drives disorder-to-order transition in Hendra virus V.Scientific reports · 2018Article
- Host Cell Rab GTPases in Hepatitis B Virus Infection.Frontiers in cell and developmental biology · 2018Review
- Bivalent Motif-Ear Interactions Mediate the Association of the Accessory Protein Tepsin with the AP-4 Adaptor Complex.The Journal of biological chemistry · 2015Article
- Classification of intrinsically disordered regions and proteins.Chemical reviews · 2014Review
- Large-scale production and structural and biophysical characterizations of the human hepatitis B virus polymerase.Journal of virology · 2014Article
- Digested disorder: Quarterly intrinsic disorder digest (July-August-September, 2013).Intrinsically disordered proteins · 2014Review
- Involvement of ESCRT-II in hepatitis B virus morphogenesis.PloS one · 2014Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 3 countries.
Funding
Abstract
Hepatitis B virus (HBV) is an infectious, potentially lethal human pathogen. However, there are no effective therapies for chronic HBV infections. Antiviral development is hampered by the lack of high-resolution structures for essential HBV protein-protein interactions. The interaction between preS1, an HBV surface-protein domain, and its human binding partner, γ2-adaptin, subverts the membrane-trafficking apparatus to mediate virion export. This interaction is a putative drug target. We report here atomic-resolution descriptions of the binding thermodynamics and structural biology of the interaction between preS1 and the EAR domain of γ2-adaptin. NMR, protein engineering, X-ray crystallography and MS showed that preS1 contains multiple γ2-EAR-binding motifs that mimic the membrane-trafficking motifs (and binding modes) of host proteins. These motifs localize together to a relatively rigid, functionally important region of preS1, an intrinsically disordered protein. The preS1-γ2-EAR interaction was relatively weak and efficiently outcompeted by a synthetic peptide. Our data provide the structural road map for developing peptidomimetic antivirals targeting the γ2-EAR-preS1 interaction.
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Registered trials
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.