ArticleJournal of virology1998
Carboxypeptidase D (gp180), a Golgi-resident protein, functions in the attachment and entry of avian hepatitis B viruses.
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 43 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.
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Who cites it
43 citing papers in PubMed.
- 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
- In Vivo Model Systems for Hepatitis B Virus Research.ACS infectious diseases · 2019Review
- Hepatocellular Carcinoma: Causes, Mechanism of Progression and Biomarkers.Current chemical genomics and translational medicine · 2018Review
- Review
- From DCPD to NTCP: the long journey towards identifying a functional hepatitis B virus receptor.Clinical and molecular hepatology · 2015Review
- Article
- 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
- Initiation of duck hepatitis B virus infection requires cleavage by a furin-like protease.Journal of virology · 2010Article
- Hepatitis B: the virus and disease.Hepatology (Baltimore, Md.) · 2009Article
- Drug targets in hepatitis B virus infection.Infectious disorders drug targets · 2009Review
- 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
- Avian hepatitis B viruses: molecular and cellular biology, phylogenesis, and host tropism.World journal of gastroenterology · 2007Review
- Viral and cellular determinants involved in hepadnaviral entry.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
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Carboxypeptidase D (gp180), one of many candidate receptors proposed for hepatitis B viruses (HBVs), was examined and found to be the actual cellular receptor for avian HBVs. This conclusion was based on the following observations: (i) gp180 was the only host protein that bound with high affinity to the pre-S ectodomain of the large duck hepatitis B virus (DHBV) envelope protein, which is known to be essential for virus infection; (ii) a pre-S subdomain which determines physical binding to gp180 was found to coincide with a domain functionally defined in infection competition experiments as a receptor binding domain; (iii) soluble gp180, lacking the membrane anchor, efficiently inhibited DHBV infection; (iv) efficient interspecies gp180-pre-S interaction was limited to the natural hosts of avian hepadnaviruses; and (v) expression of gp180 in a heterologous hepatoma cell line mediated cellular attachment and subsequent internalization of fluorescently labeled viral particles into vesicular structures. However, gp180 expression did not render transfected heterologous cells permissive for productive infection, suggesting that a species-specific coreceptor is required for fusion to complete viral entry. In contrast to the case for known virus receptors, gp180 was not detected on the hepatocyte cell surface but was found to be concentrated in the Golgi apparatus, from where it functions by cycling to and from the plasma membrane.
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