ArticleJournal of physics. Condensed matter : an Institute of Physics journal2018
Varieties of charge distributions in coat proteins of ssRNA+ viruses.
Article in Journal of physics. Condensed matter : an Institute of Physics journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- Structural Changes Likely Cause Chemical Differences between Empty and Full AAV Capsids.Biomedicines · 2024Article
- Electrostatic Theory of the Acidity of the Solution in the Lumina of Viruses and Virus-Like Particles.The journal of physical chemistry. B · 2023Article
- Packing and trimer-to-dimer protein reconstruction in icosahedral viral shells with a single type of symmetrical structural unit.Nanoscale advances · 2022Article
- Relative humidity in droplet and airborne transmission of disease.Journal of biological physics · 2021Review
- pH-induced morphological changes of proteinaceous viral shells.Scientific reports · 2019Article
- Electrostatics-Driven Inflation of Elastic Icosahedral Shells as a Model for Swelling of Viruses.Biophysical journal · 2018Article
- Compactness of viral genomes: effect of disperse and localized random mutations.Journal of physics. Condensed matter : an Institute of Physics journal · 2018Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
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Abstract
A major part of the interactions involved in the assembly and stability of icosahedral, positive-sense single-stranded RNA (ssRNA+) viruses is electrostatic in nature, as can be inferred from the strong pH- and salt-dependence of their assembly phase diagrams. Electrostatic interactions do not act only between the capsid coat proteins (CPs), but just as often provide a significant contribution to the interactions of the CPs with the genomic RNA, mediated to a large extent by positively charged, flexible N-terminal tails of the CPs. In this work, we provide two clear and complementary definitions of an N-terminal tail of a protein, and use them to extract the tail sequences of a large number of CPs of ssRNA+ viruses. We examine the pH-dependent interplay of charge on both tails and CPs alike, and show that-in contrast to the charge on the CPs-the net positive charge on the N-tails persists even to very basic pH values. In addition, we note a limit to the length of the wild-type genomes of those viruses which utilize positively charged tails, when compared to viruses without charged tails and similar capsid size. At the same time, we observe no clear connection between the charge on the N-tails and the genome lengths of the viruses included in our study.
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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.