ArticlemBio2017
Crystal Structures of Two Immune Complexes Identify Determinants for Viral Infectivity and Type-Specific Neutralization of Human Papillomavirus.
Article in mBio, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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.
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Who cites it
17 citing papers in PubMed.
- Immunogenicity of anVaccines · 2026Article
- The h4 coil surface region of human papillomavirus type 58 L1 virus-like particle serves as a potential location for presenting the RG1 epitope peptide.Human vaccines & immunotherapeutics · 2025Article
- Investigating the impact of oxygen concentration on the assembly of human papillomavirus virus like particles.Scientific reports · 2025Article
- Human monoclonal antibodies to HPV16 show evidence for common developmental pathways and public epitopes.PLoS pathogens · 2025Article
- Identification of a cross-neutralizing antibody that targets the receptor binding site of H1N1 and H5N1 influenza viruses.Nature communications · 2022Article
- 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
- Virus-like particles: preparation, immunogenicity and their roles as nanovaccines and drug nanocarriers.Journal of nanobiotechnology · 2021Review
- SARS-CoV-2 spike produced in insect cells elicits high neutralization titres in non-human primates.Emerging microbes & infections · 2020Article
- 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
- Expression of different L1 isoforms ofeLife · 2020Article
- Rational design of a multi-valent human papillomavirus vaccine by capsomere-hybrid co-assembly of virus-like particles.Nature communications · 2020Article
- Recent Progress on the Versatility of Virus-Like Particles.Vaccines · 2020Review
- Identification of Antibodies with Non-overlapping Neutralization Sites that Target Coxsackievirus A16.Cell host & microbe · 2020Article
- Epidemiology and Burden of Human Papillomavirus and Related Diseases, Molecular Pathogenesis, and Vaccine Evaluation.Frontiers in public health · 2020Review
- Structural characterization of a neutralizing mAb H16.001, a potent candidate for a common potency assay for various HPV16 VLPs.NPJ vaccines · 2020Article
- Neutralization sites of human papillomavirus-6 relate to virus attachment and entry phase in viral infection.Emerging microbes & infections · 2019Article
- Rational design of a triple-type human papillomavirus vaccine by compromising viral-type specificity.Nature communications · 2018Article
Corrections and comments
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Authors and funding
17 authors.
Funding
Abstract
Persistent, high-risk human papillomavirus (HPV) infection is the primary cause of cervical cancer. Neutralizing antibodies elicited by L1-only virus-like particles (VLPs) can block HPV infection; however, the lack of high-resolution structures has limited our understanding of the mode of virus infection and the requirement for type specificity at the molecular level. Here, we describe two antibodies, A12A3 and 28F10, that specifically bind to and neutralize HPV58 and HPV59, respectively, through two distinct binding stoichiometries. We show that the epitopes of A12A3 are clustered in the DE loops of two adjacent HPV58 L1 monomers, whereas 28F10 recognizes the HPV59 FG loop of a single monomer. Via structure-based mutagenesis and analysis of antibody binding, we further identified the residues HPV58 D154, S168, and N170 and HPV59 M267, Q270, E273, Y276, K278, and R283, which play critical roles in virus infection. By substituting these strategic epitope residues into other HPV genotypes, we could then redirect the type-specific binding of the antibodies to these genotypes, thus highlighting the importance of these specific residues, HPV58 R161, S168, and N308 and HPV59 Q270, E273, and D281. Overall, our findings provide molecular insights into potential structural determinants of HPV required for infectivity and type specificity.
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