ArticleJournal of virology2013
Integrin and defensin modulate the mechanical properties of adenovirus.
Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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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.
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Who cites it
47 citing papers in PubMed, 81 citations in OpenAlex.
- Protocol for AFM Nanoindentation of Viruses and Protein Cages.Methods in molecular biology (Clifton, N.J.) · 2027Article
- Viruses under mechanical force: Implications and applications.Virus research · 2026Review
- Review
- Alpha-defensin binding expands human adenovirus tropism.PLoS pathogens · 2024Article
- Mechanical fatigue testing in silico: Dynamic evolution of material properties of nanoscale biological particles.Acta biomaterialia · 2023Article
- Article
- Label-free microscopy for virus infections.Microscopy (Oxford, England) · 2023Article
- Adenovirus core protein V reinforces the capsid and enhances genome release from disrupted particles.Science advances · 2023Article
- Roles of Antimicrobial Peptides in Gynecological Cancers.International journal of molecular sciences · 2022Review
- Extracorporeal membrane oxygenation for paediatric refractory hypoxic respiratory failure caused by adenovirus in Shanghai: a case series.BMC pediatrics · 2022Observational
- Natural antimicrobial peptides as a source of new antiviral agents.The Journal of general virology · 2021Review
- Understanding Post Entry Sorting of Adenovirus Capsids; A Chance to Change Vaccine Vector Properties.Viruses · 2021Review
- Fluctuating nonlinear spring theory: Strength, deformability, and toughness of biological nanoparticles from theoretical reconstruction of force-deformation spectra.Acta biomaterialia · 2021Article
- Physics of viral dynamics.Nature reviews. Physics · 2021Review
- Defensin-driven viral evolution.PLoS pathogens · 2020Article
- Physical virology: From virus self-assembly to particle mechanics.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2020Review
- Antiviral Activities of Human Host Defense Peptides.Current medicinal chemistry · 2020Review
- Adenovirus major core protein condenses DNA in clusters and bundles, modulating genome release and capsid internal pressure.Nucleic acids research · 2019Article
- Adenovirus flow in host cell networks.Open biology · 2019Review
- α-Defensin HD5 StabilizesPathogens & immunity · 2019Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The propensity for capsid disassembly and uncoating of human adenovirus is modulated by interactions with host cell molecules like integrins and alpha defensins. Here, we use atomic force microscopy (AFM) nanoindentation to elucidate, at the single-particle level, the mechanism by which binding of these host molecules affects virus particle elasticity. Our results demonstrate the direct link between integrin or defensin binding and the mechanical properties of the virus. We show that the structure and geometry of adenovirus result in an anisotropic elastic response that relates to icosahedral symmetry. This elastic response changes upon binding host molecules. Whereas integrin binding softens the vertex regions, binding of a human alpha defensin has exactly the opposite effect. Our results reveal that the ability of these host molecules to influence adenovirus disassembly correlates with a direct effect on the elastic strength of the penton region. Host factors that influence adenovirus infectivity thus modulate the elastic properties of the capsid. Our findings reveal a direct link between virus-host interactions and capsid mechanics.
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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.