ArticleJournal of virology1998
Avian hepatitis B virus infection is initiated by the interaction of a distinct pre-S subdomain with the cellular receptor gp180.
Article in Journal of virology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 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.
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Who cites it
34 citing papers in PubMed, 70 citations in OpenAlex.
- Both middle and large envelope proteins can mediate neutralization of hepatitis B virus infectivity by anti-preS2 antibodies: escape by naturally occurring preS2 deletions.Journal of virology · 2024Article
- Animal Models for the Study of Hepatitis B Virus Pathobiology and Immunity: Past, Present, and Future.Frontiers in microbiology · 2021Review
- Hepatocytic expression of human sodium-taurocholate cotransporting polypeptide enables hepatitis B virus infection of macaques.Nature communications · 2017Article
- From DCPD to NTCP: the long journey towards identifying a functional hepatitis B virus receptor.Clinical and molecular hepatology · 2015Review
- The Molecular and Structural Basis of HBV-resistance to Nucleos(t)ide Analogs.Journal of clinical and translational hepatology · 2014Review
- NTCP and beyond: opening the door to unveil hepatitis B virus entry.International journal of molecular sciences · 2014Review
- Virus entry mediated by hepatitis B virus envelope proteins.World journal of gastroenterology · 2013Review
- Sodium taurocholate cotransporting polypeptide mediates woolly monkey hepatitis B virus infection of Tupaia hepatocytes.Journal of virology · 2013Article
- Hepatitis B virus-cell interactions and pathogenesis.Journal of cellular physiology · 2008Review
- Entry of duck hepatitis B virus into primary duck liver and kidney cells after discovery of a fusogenic region within the large surface protein.Journal of virology · 2007Article
- Viral and cellular determinants involved in hepadnaviral entry.World journal of gastroenterology · 2007Review
- Avian hepatitis B viruses: molecular and cellular biology, phylogenesis, and host tropism.World journal of gastroenterology · 2007Review
- Identification of a structural motif crucial for infectivity of hepatitis B viruses.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- A hydrophobic domain in the large envelope protein is essential for fusion of duck hepatitis B virus at the late endosome.Journal of virology · 2005Article
- Mapping of the hepatitis B virus pre-S1 domain involved in receptor recognition.Journal of virology · 2005Article
- NACA as a potential cellular target of hepatitis B virus preS1 protein.Digestive diseases and sciences · 2005Article
- St, a truncated envelope protein derived from the S protein of duck hepatitis B virus, acts as a chaperone for the folding of the large envelope protein.Journal of virology · 2005Article
- Identification and characterization of avihepadnaviruses isolated from exotic anseriformes maintained in captivity.Journal of virology · 2005Article
- Itinerary of hepatitis B viruses: delineation of restriction points critical for infectious entry.Journal of virology · 2004Article
- Evolution of cell recognition by viruses: a source of biological novelty with medical implications.Advances in virus research · 2003Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Functionally relevant hepadnavirus-cell surface interactions were investigated with the duck hepatitis B virus (DHBV) animal model by using an in vitro infection competition assay. Recombinant DHBV pre-S polypeptides, produced in Escherichia coli, were shown to inhibit DHBV infection in a dose-dependent manner, indicating that monomeric pre-S chains were capable of interfering with virus-receptor interaction. Particle-associated pre-S was, however, 30-fold more active, suggesting that cooperative interactions enhance particle binding. An 85-amino-acid pre-S sequence, spanning about half of the DHBV pre-S chain, was characterized by deletion analysis as essential for maximal inhibition. Pre-S polypeptides from heron hepatitis B virus (HHBV) competed DHBV infection equally well despite a 50% difference in amino acid sequence and a much-reduced infectivity of HHBV for duck hepatocytes. These observations are taken to indicate (i) that the functionality of the DHBV pre-S subdomain, which interacts with the cellular receptor, is determined predominantly by a defined three-dimensional structure rather than by primary sequence elements; (ii) that cellular uptake of hepadnaviruses is a multistep process involving more than a single cellular receptor component; and (iii) that gp180, a cellular receptor candidate unable to discriminate between DHBV and HHBV, is a common component of the cellular receptor complex for avian hepadnaviruses.
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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.