ArticleProceedings of the National Academy of Sciences of the United States of America2021
High-resolution asymmetric structure of a Fab-virus complex reveals overlap with the receptor binding site.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 23 citations in OpenAlex.
- Distinct evolutionary patterns of endemic and emerging parvoviruses and the origin of a new pandemic virus.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Atomic-resolution structure of a chimeric Powassan tick-borne flavivirus.Science advances · 2025Article
- Structural characterization of antibody-responses following Zolgensma treatment for AAV capsid engineering to expand patient cohorts.Nature communications · 2025Article
- Structures and functions of the limited natural polyclonal antibody response to parvovirus infection.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural studies of Parvoviridae capsid assembly and evolution: implications for novel AAV vector design.Frontiers in artificial intelligence · 2025Review
- Cryo-EM reconstruction of helical polymers: Beyond the simple cases.Quarterly reviews of biophysics · 2024Review
- Isolation, cloning and analysis of parvovirus-specific canine antibodies from peripheral blood B cells.Developmental and comparative immunology · 2023Article
- Cryo EM structures map a post vaccination polyclonal antibody response to canine parvovirus.Communications biology · 2023Article
- The Structures and Functions of Parvovirus Capsids and Missing Pieces: the Viral DNA and Its Packaging, Asymmetrical Features, Nonprotein Components, and Receptor or Antibody Binding and Interactions.Journal of virology · 2023Review
- Viral Capsid, Antibody, and Receptor Interactions: Experimental Analysis of the Antibody Escape Evolution of Canine Parvovirus.Journal of virology · 2023Article
- Canine Parvovirus in Turkey: First Whole-Genome Sequences, Strain Distribution, and Prevalence.Viruses · 2023Article
- Detection of Selected Canine Viruses in Nigerian Free-Ranging Dogs Traded for Meat Consumption.Animals : an open access journal from MDPI · 2023Article
- A cryo-ET survey of microtubules and intracellular compartments in mammalian axons.The Journal of cell biology · 2022Article
- Molecular characterization ofFrontiers in veterinary science · 2022Article
- 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 3 institutions in 1 country.
Funding
Abstract
Canine parvovirus is an important pathogen causing severe diseases in dogs, including acute hemorrhagic enteritis, myocarditis, and cerebellar disease. Overlap on the surface of parvovirus capsids between the antigenic epitope and the receptor binding site has contributed to cross-species transmission, giving rise to closely related variants. It has been shown that Mab 14 strongly binds and neutralizes canine but not feline parvovirus, suggesting this antigenic site also controls species-specific receptor binding. To visualize the conformational epitope at high resolution, we solved the cryogenic electron microscopy (cryo-EM) structure of the Fab-virus complex. We also created custom software, Icosahedral Subparticle Extraction and Correlated Classification, to solve a Fab-virus complex with only a few Fab bound per capsid and visualize local structures of the Fab-bound and -unbound antigenic sites extracted from the same complex map. Our results identified the antigenic epitope that had significant overlap with the receptor binding site, and the structures revealed that binding of Fab induced conformational changes to the virus. We were also able to assign the order and position of attached Fabs to allow assessment of complementarity between the Fabs bound to different positions. This approach therefore provides a method for using cryo-EM to investigate complementarity of antibody binding.
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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.