ArticleNPJ vaccines2020
Structural characterization of a neutralizing mAb H16.001, a potent candidate for a common potency assay for various HPV16 VLPs.
Article in NPJ vaccines, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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
10 citing papers in PubMed, 12 citations in OpenAlex.
- Factors impacting protective immunity conferred by vaccination with adeno-associated virus-like particles displaying human papillomavirus L2 residues 17-36.Journal of virology · 2026Trial
- Susceptibility of naturally human papillomavirus type 16 major capsid protein L1 variants to vaccines and predictions of future evolutionary trends.Tumour virus research · 2026Article
- Comparison of plant- and mammalian cell-produced human papillomavirus pseudovirions.Journal of virological methods · 2025Article
- Human monoclonal antibodies to HPV16 show evidence for common developmental pathways and public epitopes.PLoS pathogens · 2025Article
- Dissolving Microneedle for Maintaining the Integrity of HPV Virus-Like Particles Enabling Durable Sterile Protection Across Various Mucosal Tissues.Advanced healthcare materials · 2025Article
- Establishing a universal IVRP method for quadrivalent HPV vaccines to replace in vivo potency tests.NPJ vaccines · 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
- Development of functionally relevant potency assays for monovalent and multivalent vaccines delivered by evolving technologies.NPJ vaccines · 2022Review
- Cryo EM Analysis Reveals Inherent Flexibility of Authentic Murine Papillomavirus Capsids.Viruses · 2021Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
Abstract
With more human papillomavirus (HPV) virus-like particle (VLP) vaccines to hit the market in future, a monoclonal antibody (mAb) with preferably comparable reactivity against vaccines from different expression systems and bioprocesses is urgently needed for the potency characterization. Among all mAbs against HPV16 collected, rabbit mAb H16.001 is potently neutralizing with the highest affinity, recognizes an immune-dominant epitope, and can comparably react with HPV16 vaccines from various sources. Cryo-electron microscopic (cryo-EM) structure demonstrated that 360 H16.001 Fabs could bind to HPV16 capsid in preferable binding manner without steric hindrance between neighboring Fabs, potentially supporting its identification for VLP structural integrity and utility in monitoring VLP structural probity. This structural analysis indicated that mAb H16.001 afforded unbiased potency characterization for various HPV16 vaccines and was potential for use in vaccine regulation practice. This study also showed a model process for selecting suitable mAbs for potency assays of other vaccines.
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