ArticleVirology2010
The neutralizing antibody response to the vaccinia virus A28 protein is specifically enhanced by its association with the H2 protein.
Article in Virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 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
14 citing papers in PubMed, 18 citations in OpenAlex.
- An experimentally validated structure-based computational framework for humanisation of anti-orthopoxvirus antibodies.EBioMedicine · 2026Article
- Structural basis of mpox virus A30/H2 subcomplex formation.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Poxvirus structural biology for application to vaccine design.Trends in immunology · 2025Review
- Monoclonal Antibodies in Light of Mpox Outbreak: Current Research, Therapeutic Targets, and Animal Models.Antibodies (Basel, Switzerland) · 2025Review
- Neutralization Determinants on Poxviruses.Viruses · 2023Review
- Structural and functional analysis of vaccinia viral fusion complex component protein A28 through NMR and molecular dynamic simulations.PLoS pathogens · 2023Article
- Functional epitopes and neutralizing antibodies of vaccinia virus.Frontiers in microbiology · 2023Review
- A comparative review of viral entry and attachment during large and giant dsDNA virus infections.Archives of virology · 2017Review
- Membrane fusion during poxvirus entry.Seminars in cell & developmental biology · 2016Review
- T cell antigen discovery using soluble vaccinia proteome reveals recognition of antigens with both virion and nonvirion association.Journal of immunology (Baltimore, Md. : 1950) · 2014Article
- Humoral immunity to smallpox vaccines and monkeypox virus challenge: proteomic assessment and clinical correlations.Journal of virology · 2013Article
- Poxvirus cell entry: how many proteins does it take?Viruses · 2012Review
- The strategic use of novel smallpox vaccines in the post-eradication world.Expert review of vaccines · 2011Review
- Smallpox vaccines: targets of protective immunity.Immunological reviews · 2011Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The vaccinia virus (VACV) entry-fusion complex (EFC) is composed of at least nine membrane proteins. Immunization of mice with individual EFC genes induced corresponding protein-binding antibody but failed to protect against VACV intranasal challenge and only DNA encoding A28 elicited low neutralizing antibody. Because the A28 and H2 proteins interact, we determined the effect of immunizing with both genes simultaneously. This procedure greatly enhanced the amount of antibody that bound intact virions, neutralized infectivity, and provided partial protection against respiratory challenge. Neither injection of A28 and H2 plasmids at different sites or mixing A28 and H2 sera enhanced neutralizing antibody. The neutralizing antibody could be completely removed by binding to the A28 protein alone and the epitope was located in the C-terminal segment. These data suggest that the interaction of H2 with A28 stabilizes the immunogenic form of A28, mimicking an exposed region of the entry-fusion complex on infectious virions.
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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.