ArticleNature protocols2017
Combining confocal and atomic force microscopy to quantify single-virus binding to mammalian cell surfaces.
Article in Nature protocols, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 71 citations in OpenAlex.
- Proximity labelling of internalizing influenza A viruses reveals a role for neogenin in virus uptake.PLoS pathogens · 2025Article
- Atomic force microscopy at the forefront: unveiling foodborne viruses with biophysical tools.Npj viruses · 2025Review
- Nanomechanical characterization of soft nanomaterial using atomic force microscopy.Materials today. Bio · 2025Review
- Analytical methods in studying cell force sensing: principles, current technologies and perspectives.Regenerative biomaterials · 2025Review
- Site-specific sulfations regulate the physicochemical properties of papillomavirus-heparan sulfate interactions for entry.Science advances · 2024Article
- NRP1 is a receptor for mammalian orthoreovirus engaged by distinct capsid subunits.Cell host & microbe · 2024Article
- Single-Molecule Investigation of the Binding Interface Stability of SARS-CoV-2 Variants with ACE2.ACS nanoscience Au · 2024Article
- Biophysical investigation of interactions between SARS-CoV-2 spike protein and neuropilin-1.Protein science : a publication of the Protein Society · 2023Article
- Label-free microscopy for virus infections.Microscopy (Oxford, England) · 2023Article
- Deciphering molecular mechanisms stabilizing the reovirus-binding complex.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Paired immunoglobulin-like receptor B is an entry receptor for mammalian orthoreovirus.Nature communications · 2023Article
- Multivalent 9-O-Acetylated-sialic acid glycoclusters as potent inhibitors for SARS-CoV-2 infection.Nature communications · 2022Article
- A Deadly Embrace: Hemagglutination Mediated by SARS-CoV-2 Spike Protein at Its 22 N-Glycosylation Sites, Red Blood Cell Surface Sialoglycoproteins, and Antibody.International journal of molecular sciences · 2022Review
- Cell-Cell Mating Interactions: Overview and Potential of Single-Cell Force Spectroscopy.International journal of molecular sciences · 2022Review
- Atomic Force Microscopy for Structural and Biophysical Investigations on Nuclear Pore Complexes.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Quantifying molecular- to cellular-level forces in living cells.Journal of physics D: Applied physics · 2021Article
- Molecular insights into receptor binding energetics and neutralization of SARS-CoV-2 variants.Nature communications · 2021Article
- Article
- Single-molecule calorimeter and free energy landscape.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Imaging methods in mechanosensing: a historical perspective and visions for the future.Molecular biology of the cell · 2021Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Over the past five years, atomic force microscopy (AFM)-based approaches have evolved into a powerful multiparametric tool set capable of imaging the surfaces of biological samples ranging from single receptors to membranes and tissues. One of these approaches, force-distance curve-based AFM (FD-based AFM), uses a probing tip functionalized with a ligand to image living cells at high-resolution and simultaneously localize and characterize specific ligand-receptor binding events. Analyzing data from FD-based AFM experiments using appropriate probabilistic models allows quantification of the kinetic and thermodynamic parameters that describe the free-energy landscape of the ligand-receptor bond. We have recently developed an FD-based AFM approach to quantify the binding events of single enveloped viruses to surface receptors of living animal cells while simultaneously observing them by fluorescence microscopy. This approach has provided insights into the early stages of the interaction between a virus and a cell. Applied to a model virus, we probed the specific interaction with cells expressing viral cognate receptors and measured the affinity of the interaction. Furthermore, we observed that the virus rapidly established specific multivalent interactions and found that each bond formed in sequence strengthened the attachment of the virus to the cell. Here we describe detailed procedures for probing the specific interactions of viruses with living cells; these procedures cover tip preparation, cell sample preparation, step-by-step FD-based AFM imaging and data analysis. Experienced microscopists should be able to master the entire set of protocols in 1 month.
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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.