ArticleJournal of virology2000
A metastable form of the large envelope protein of duck hepatitis B virus: low-pH release results in a transition to a hydrophobic, potentially fusogenic conformation.
Article in Journal of virology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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
11 citing papers in PubMed, 26 citations in OpenAlex.
- Sulfated liposome-based artificial cell membrane glycocalyx nanodecoys for coronavirus inactivation by membrane fusion.Bioactive materials · 2024Article
- Article
- Energy Requirements for Loss of Viral Infectivity.Food and environmental virology · 2020Article
- The first transmembrane domain of the hepatitis B virus large envelope protein is crucial for infectivity.Journal of virology · 2009Article
- HBV life cycle: entry and morphogenesis.Viruses · 2009Article
- Viral and cellular determinants involved in hepadnaviral entry.World journal of gastroenterology · 2007Review
- Stable association of herpes simplex virus with target membranes is triggered by low pH in the presence of the gD receptor, HVEM.Journal of virology · 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
- Hydrophobicity of reactive site loop of SCCA1 affects its binding to hepatitis B virus.World journal of gastroenterology · 2005Article
- Cytolytic toxin Cyt1A and its mechanism of membrane damage: data and hypotheses.Applied and environmental microbiology · 2003Review
- The S4 genome segment of baboon reovirus is bicistronic and encodes a novel fusion-associated small transmembrane protein.Journal of virology · 2002Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have examined the structure and fusion potential of the duck hepatitis B virus (DHBV) envelope proteins by treating subviral particles with deforming agents known to release envelope proteins of viruses from a metastable to a fusion-active state. Exposure of DHBV particles to low pH triggered a major structural change in the large envelope protein (L), resulting in exposure of trypsin sites within its S domain but without affecting the same region in the small surface protein (S) subunits. This conformational change was associated with increased hydrophobicity of the particle surface, most likely arising from surface exposure of the hydrophobic first transmembrane domain (TM1). In the hydrophobic conformation, DHBV particles were able to bind to liposomes and intact cells, while in their absence these particles aggregated, resulting in viral inactivation. These results suggests that some L molecules are in a spring-loaded metastable state which, when released, exposes a previously hidden hydrophobic domain, a transition potentially representing the fusion-active state of the envelope.
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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.