ArticleJournal of virology2005
A hydrophobic domain in the large envelope protein is essential for fusion of duck hepatitis B virus at the late endosome.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 30 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
- Review
- Article
- Intracellular Trafficking of HBV Particles.Cells · 2020Review
- Hepatitis B Virus Entry into Cells.Cells · 2020Review
- Initiation of duck hepatitis B virus infection requires cleavage by a furin-like protease.Journal of virology · 2010Article
- Hepatitis B virus requires intact caveolin-1 function for productive infection in HepaRG cells.Journal of virology · 2010Article
- 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
- Duck hepatitis B virus requires cholesterol for endosomal escape during virus entry.Journal of virology · 2008Article
- The translocation motif of hepatitis B virus envelope proteins is dispensable for infectivity.Journal of virology · 2007Article
- Infectivity determinants of the hepatitis B virus pre-S domain are confined to the N-terminal 75 amino acid residues.Journal of virology · 2007Article
- 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
- Two potentially important elements of the hepatitis B virus large envelope protein are dispensable for the infectivity of hepatitis delta virus.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
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The duck hepatitis B virus (DHBV) envelope is comprised of two transmembrane (TM) proteins, the large (L) and the small (S), that assemble into virions and subviral particles. Secondary-structure predictions indicate that L and S have three alpha-helical, membrane-spanning domains, with TM1 predicted to act as the fusion peptide following endocytosis of DHBV into the hepatocyte. We used bafilomycin A1 during infection of primary duck hepatocytes to show that DHBV must be trafficked from the early to the late endosome for fusion to occur. Alanine substitution mutations in TM1 of L and S, which lowered TM1 hydrophobicity, were used to examine the role of TM1 in infectivity. The high hydrophobicity of the TM1 domain of L, but not of S, was shown to be essential for virus infection at a step downstream of receptor binding and virus internalization. Using wild-type and mutant synthetic peptides, we demonstrate that the hydrophobicity of this domain is required for the aggregation and the lipid mixing of phospholipid vesicles, supporting the role of TM1 as the fusion peptide. While lipid mixing occurred at pH 7, the kinetics of insertion of the fusion peptide was increased at pH 5, consistent with the location of DHBV in the late-endosome compartment and previous studies of the nonessential role of low pH for infectivity. Exchange of the TM1 of DHBV with that of hepatitis B virus yielded functional, infectious DHBV particles, suggesting that TM1 of all of the hepadnaviruses act similarly in the fusion mechanism.
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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.