ArticleJournal of virology2007
Identification and characterization of peptides that interact with hepatitis B virus via the putative receptor binding site.
Article in Journal of virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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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.
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.
Who cites it
21 citing papers in PubMed, 42 citations in OpenAlex.
- Phage Display as a Promising Platform for Peptide Drug Discovery.Pharmaceuticals (Basel, Switzerland) · 2026Review
- Peptides developed against receptor binding sites of the E glycoprotein neutralize tick-borne encephalitis virus.Scientific reports · 2025Article
- Review
- Hepatitis B Virus Targets Lipid Transport Pathways to Infect Hepatocytes.Cellular and molecular gastroenterology and hepatology · 2023Article
- Antimicrobial peptides: natural or synthetic defense peptides against HBV and HCV infections.Virusdisease · 2022Review
- Development of peptides targeting receptor binding site of the envelope glycoprotein to contain the West Nile virus infection.Scientific reports · 2021Article
- Discovery of Antivirals Using Phage Display.Viruses · 2021Review
- Macrophage Phenotypes and Hepatitis B Virus Infection.Journal of clinical and translational hepatology · 2020Review
- Peptides to combat viral infectious diseases.Peptides · 2020Review
- Efficient Inhibition of Hepatitis B Virus Infection by a preS1-binding Peptide.Scientific reports · 2016Article
- Deciphering the mystery of hepatitis B virus receptors: A historical perspective.Virusdisease · 2015Review
- Applications of human hepatitis B virus preS domain in bio- and nanotechnology.World journal of gastroenterology · 2015Review
- Structural basis for the neutralization of hepatitis E virus by a cross-genotype antibody.Cell research · 2015Article
- Phage display creates innovative applications to combat hepatitis B virus.World journal of gastroenterology · 2014Review
- Novel recombinant hepatitis B virus vectors efficiently deliver protein and RNA encoding genes into primary hepatocytes.Journal of virology · 2013Article
- How the key finds its door - identification of HBV receptor.Virologica Sinica · 2013Article
- Phage display of combinatorial peptide libraries: application to antiviral research.Molecules (Basel, Switzerland) · 2011Review
- Development of novel therapeutics for chronic hepatitis B.Virologica Sinica · 2010Review
- Hepatitis B virus (HBV) surface antigen interacts with and promotes cyclophilin a secretion: possible link to pathogenesis of HBV infection.Journal of virology · 2010Article
- SLiMFinder: a probabilistic method for identifying over-represented, convergently evolved, short linear motifs in proteins.PloS one · 2007Article
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A direct involvement of the PreS domain of the hepatitis B virus (HBV) large envelope protein, and in particular amino acid residues 21 to 47, in virus attachment to hepatocytes has been suggested by many previous studies. Several PreS-interacting proteins have been identified. However, they share few common sequence motifs, and a bona fide cellular receptor for HBV remains elusive. In this study, we aimed to identify PreS-interacting motifs and to search for novel HBV-interacting proteins and the long-sought receptor. PreS fusion proteins were used as baits to screen a phage display library of random peptides. A group of PreS-binding peptides were obtained. These peptides could bind to amino acids 21 to 47 of PreS1 and shared a linear motif (W1T2X3W4W5) sufficient for binding specifically to PreS and viral particles. Several human proteins with such a motif were identified through BLAST search. Analysis of their biochemical and structural properties suggested that lipoprotein lipase (LPL), a key enzyme in lipoprotein metabolism, might interact with PreS and HBV particles. The interaction of HBV with LPL was demonstrated by in vitro binding, virus capture, and cell attachment assays. These findings suggest that LPL may play a role in the initiation of HBV infection. Identification of peptides and protein ligands corresponding to LPL that bind to the HBV envelope will offer new therapeutic strategies against HBV infection.
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What OpenQuestion holds
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.