ArticleJournal of virology2004
Structural requirements of astrovirus virus-like particles assembled in insect cells.
Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed, 40 citations in OpenAlex.
- Distinct intracellular and extracellular maturation of goose astrovirus 2 capsid protein and the potential of virus-like particles as a novel subunit vaccine.Frontiers in veterinary science · 2026Article
- Identification of a novel linear B-cell epitope recognized by a monoclonal antibody against the capsid protein of goose astrovirus genotypes 2.BMC veterinary research · 2025Article
- The neonatal Fc receptor is a cellular receptor for human astrovirus.Nature microbiology · 2024Article
- Human astrovirus capsid protein releases a membrane lytic peptide upon trypsin maturation.Journal of virology · 2023Article
- A Review of Emerging Goose Astrovirus Causing Gout.BioMed research international · 2022Review
- Structural Insights into the Human Astrovirus Capsid.Viruses · 2021Review
- Baculoviruses in Gene Therapy and Personalized Medicine.Biologics : targets & therapy · 2021Review
- Review
- The Astrovirus Capsid: A Review.Viruses · 2017Review
- Crystal Structure of the Human Astrovirus Capsid Protein.Journal of virology · 2016Article
- Structural, Mechanistic, and Antigenic Characterization of the Human Astrovirus Capsid.Journal of virology · 2015Article
- Human astroviruses.Clinical microbiology reviews · 2014Review
- Use of baculovirus expression system for generation of virus-like particles: successes and challenges.Protein expression and purification · 2013Review
- Crystal structure of the avian astrovirus capsid spike.Journal of virology · 2013Article
- Construction and characterization of virus-like particles: a review.Molecular biotechnology · 2013Review
- Article
- Virus-like particles: the new frontier of vaccines for animal viral infections.Veterinary immunology and immunopathology · 2012Review
- Astrovirus increases epithelial barrier permeability independently of viral replication.Journal of virology · 2007Article
- Association of the astrovirus structural protein VP90 with membranes plays a role in virus morphogenesis.Journal of virology · 2007Article
- Identification of structural domains involved in astrovirus capsid biology.Viral immunology · 2005Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Expression of the complete ORF2 of human astrovirus serotype 1 (HAstV-1) in the baculovirus system led to the formation of virus-like particles (VLPs) of around 38 nm. The same kind of VLPs were also obtained either with the expression of a truncated form of ORF2 lacking the first 70 amino acids (aa), or with the same truncated form in which those 70 aa were replaced by the green fluorescent protein. All three kinds of VLPs were equally recognized by an anti-HAstV-1 polyclonal antibody and by two monoclonal antibodies (MAbs; 8E7 and 5B7), indicating a nonessential role of those amino acids neither in the capsid assembly nor in the antigen structure. A second type of structure consisting of 16-nm ring-like units was observed in all of the cases, mostly after disassembling the 38-nm VLPs through the addition of EDTA. The removal of the EDTA and the addition of Mg(2+) ions promoted the reassembly of the 38-nm VLPs. The nature of these 16-nm ring-like structures, capsomers or T = 1 VLPs, still remains unclear. Biochemical analysis revealed no differences between the 38-nm VLPs and the 16-nm structures, whereas antigenically, they shared the 8E7 MAb epitope but differed in the 5B7 MAb epitope, with the latter structures being more readily recognized.
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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.