ArticleACS omega2026
Computational Insights into the Structural Dynamics of the E Protein's DIII Domain in Brazilian Yellow Fever Virus: Implications of Amino Acid Variations on Protein Plasticity and Potential Impact on Vaccine Efficacy.
Article in ACS omega, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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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.
The trial behind it
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Who cites it
1 citing paper in PubMed.
- Molecular Evolution of the Chikungunya VirusViruses · 2026Article
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
During 2016-2019, Brazil witnessed one of the largest yellow fever virus (YFV) outbreaks. Experimental studies suggested that the epitope recognized by vaccine-specific mAb 411 is strongly associated with the EDIII domain of the E protein. This prompted us to analyze the global protein sequences of the YFV-EDIII domain to explore the conserved mutations that modulate the domain structure. Through comprehensive computational analysis combining sequence alignment, stability prediction, and molecular dynamics simulations, we characterized structural and functional consequences of mutations exclusive to Brazilian strains. Multiple sequence alignments of 223 publicly available YFV protein sequences revealed four prevalent mutations in the EDIII domain: V318A, K331R, I335 M, and I344 V, occurring in more than 65% of the analyzed sequences. Notably, V318A and I335 M mutations were found exclusively in Brazilian strains, while K331R and I344 V showed broader geographic distributions but higher prevalence in South American isolates. Thermodynamic stability predictions using multiple computational approaches revealed that individual mutations, particularly V318A, consistently demonstrated destabilizing effects, with predicted ΔΔ
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