ArticleJournal of biological physics2018
A single point mutation in precursor protein VI doubles the mechanical strength of human adenovirus.
Article in Journal of biological physics, 2018. 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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Who cites it
10 citing papers in PubMed.
- Viruses under mechanical force: Implications and applications.Virus research · 2026Review
- From viral assembly to host interaction: AFM's contributions to virology.Journal of virology · 2025Review
- Adenovirus core protein V reinforces the capsid and enhances genome release from disrupted particles.Science advances · 2023Article
- Article
- Understanding Post Entry Sorting of Adenovirus Capsids; A Chance to Change Vaccine Vector Properties.Viruses · 2021Review
- Physics Comes to the Aid of Medicine-Clinically-Relevant Microorganisms through the Eyes of Atomic Force Microscope.Pathogens (Basel, Switzerland) · 2020Review
- Keeping It Together: Structures, Functions, and Applications of Viral Decoration Proteins.Viruses · 2020Review
- Physical virology: From virus self-assembly to particle mechanics.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2020Review
- Dynamic competition for hexon binding between core protein VII and lytic protein VI promotes adenovirus maturation and entry.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Viruses are extensively studied as vectors for vaccine applications and gene therapies. For these applications, understanding the material properties of viruses is crucial for creating optimal functionality. Using atomic force microscopy (AFM) nanoindentation, we studied the mechanical properties of human adenovirus type 5 with the fiber of type 35 (Ad5F35) and compared it to viral capsids with a single point mutation in the protein VI precursor protein (pVI-S28C). Surprisingly, the pVI-S28C mutant turned out to be twice as stiff as the Ad5F35 capsids. We suggest that this major increase in strength is the result of the DNA crosslinking activity of precursor protein VII, as this protein was detected in the pVI-S28C mutant capsids. The infectivity was similar for both capsids, indicating that mutation did not affect the ability of protein VI to lyse the endosomal membrane. This study highlights that it is possible to increase the mechanical stability of a capsid even with a single point mutation while not affecting the viral life cycle. Such insight can help enable the development of more stable vectors for therapeutic applications.
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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.