ArticleJournal of virology2011
Hepatitis B virus surface antigen assembly function persists when entire transmembrane domains 1 and 3 are replaced by a heterologous transmembrane sequence.
Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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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
8 citing papers in PubMed.
- Extracellular RNA in viral-host interactions: Thinking outside the cell.Wiley interdisciplinary reviews. RNA · 2019Review
- 3D visualisation of hepatitis B vaccine in the oral delivery vehicle SBA-15.Scientific reports · 2019Article
- Occult HBV infection in Chinese blood donors: role of N-glycosylation mutations and amino acid substitutions in S protein transmembrane domains.Emerging microbes & infections · 2019Article
- Prospects for prophylactic hepatitis C vaccines based on virus-like particles.Human vaccines & immunotherapeutics · 2013Review
- Role of transmembrane domains of hepatitis B virus small surface proteins in subviral-particle biogenesis.Journal of virology · 2013Article
- Host factors involved in hepatitis B virus maturation, assembly, and egress.Medical microbiology and immunology · 2012Review
- Live attenuated rubella viral vectors stably express HIV and SIV vaccine antigens while reaching high titers.Vaccine · 2012Article
- Toolbox for non-intrusive structural and functional analysis of recombinant VLP based vaccines: a case study with hepatitis B vaccine.PloS one · 2012Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Native hepatitis B surface antigen (HBsAg) spontaneously assembles into 22-nm subviral particles. The particles are lipoprotein micelles, in which HBsAg is believed to span the lipid layer four times. The first two transmembrane domains, TM1 and TM2, are required for particle assembly. We have probed the requirements for particle assembly by replacing the entire first or third TM domain of HBsAg with the transmembrane domain of HIV gp41. We found that either TM domain of HBsAg could be replaced, resulting in HBsAg-gp41 chimeras that formed particles efficiently. HBsAg formed particles even when both TM1 and TM3 were replaced with the gp41 domain. The results indicate remarkable flexibility in HBsAg particle formation and provide a novel way to express heterologous membrane proteins that are anchored to a lipid surface by their own membrane-spanning domain. The membrane-proximal exposed region (MPER) of gp41 is an important target of broadly reactive neutralizing antibodies against HIV-1, and HBsAg-MPER particles may provide a good platform for future vaccine development.
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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.