ArticleVirology2015
Structural comparison of four different antibodies interacting with human papillomavirus 16 and mechanisms of neutralization.
Article in Virology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 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
35 citing papers in PubMed.
- The DE and FG loops of the HPV major capsid protein contribute to the epitopes of vaccine-induced cross-neutralising antibodies.Scientific reports · 2016Trial
- Cross-protection of the Bivalent Human Papillomavirus (HPV) Vaccine Against Variants of Genetically Related High-Risk HPV Infections.The Journal of infectious diseases · 2016Trial
- Cross-Neutralizing and Broadly Neutralizing Human Antibodies Against Nonenveloped Viruses.European journal of immunology · 2026Review
- Susceptibility of naturally human papillomavirus type 16 major capsid protein L1 variants to vaccines and predictions of future evolutionary trends.Tumour virus research · 2026Article
- Post-attachment neutralization of HPV16 by antibodies derived from Gardasil-vaccinated women.NPJ vaccines · 2025Article
- Human monoclonal antibodies to HPV16 show evidence for common developmental pathways and public epitopes.PLoS pathogens · 2025Article
- Critical Residues Involved in the Coassembly of L1 and L2 Capsid Proteins of Human Papillomavirus 16.Journal of virology · 2023Article
- B-cell epitope discovery: The first protein flexibility-based algorithm-Zika virus conserved epitope demonstration.PloS one · 2023Article
- Characterization of an Escherichia coli-derived triple-type chimeric vaccine against human papillomavirus types 39, 68 and 70.NPJ vaccines · 2022Article
- Contribution of Surface-Exposed Loops on the HPV16 Capsid to Antigenic Domains Recognized by Vaccine or Natural Infection Induced Neutralizing Antibodies.Microbiology spectrum · 2022Article
- Epitope mapping of antibodies in C-reactive protein assay kits by hydrogen-deuterium exchange mass spectrometry explains differential results across kits.Analytical and bioanalytical chemistry · 2022Article
- Human Papillomavirus (HPV) Entry Inhibitors.Advances in experimental medicine and biology · 2022Article
- Cryo EM Analysis Reveals Inherent Flexibility of Authentic Murine Papillomavirus Capsids.Viruses · 2021Article
- Structural basis for the shared neutralization mechanism of three classes of human papillomavirus type 58 antibodies with disparate modes of binding.Journal of virology · 2021Article
- High resolution cryo EM analysis of HPV16 identifies minor structural protein L2 and describes capsid flexibility.Scientific reports · 2021Article
- Comprehensive Assessment of the Antigenic Impact of Human Papillomavirus Lineage Variation on Recognition by Neutralizing Monoclonal Antibodies Raised against Lineage A Major Capsid Proteins of Vaccine-Related Genotypes.Journal of virology · 2020Article
- Article
- Phylogeny and In Silico Structure Analysis of Major Capsid Protein (L1) Human Papillomavirus 45 from Indonesian Isolates.Asian Pacific journal of cancer prevention : APJCP · 2020Article
- Rational design of a multi-valent human papillomavirus vaccine by capsomere-hybrid co-assembly of virus-like particles.Nature communications · 2020Article
- Neutralization Mechanism of a Monoclonal Antibody Targeting a Porcine Circovirus Type 2 Cap Protein Conformational Epitope.Journal of virology · 2020Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Cryo-electron microscopy (cryo-EM) was used to solve the structures of human papillomavirus type 16 (HPV16) complexed with fragments of antibody (Fab) from three different neutralizing monoclonals (mAbs): H16.1A, H16.14J, and H263.A2. The structure-function analysis revealed predominantly monovalent binding of each Fab with capsid interactions that involved multiple loops from symmetry related copies of the major capsid protein. The residues identified in each Fab-virus interface map to a conformational groove on the surface of the capsomer. In addition to the known involvement of the FG and HI loops, the DE loop was also found to constitute the core of each epitope. Surprisingly, the epitope mapping also identified minor contributions by EF and BC loops. Complementary immunological assays included mAb and Fab neutralization. The specific binding characteristics of mAbs correlated with different neutralizing behaviors in pre- and post-attachment neutralization assays.
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Registered trials
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