ArticleScientific reports2017
An inter-residue network model to identify mutational-constrained regions on the Ebola coat glycoprotein.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 5 citations in OpenAlex.
- Configurationally Locked Ridaifen-B Analogs as Potent Ebola Virus Entry Inhibitors.Journal of medicinal chemistry · 2026Article
- Learned features of antibody-antigen binding affinity.Frontiers in molecular biosciences · 2023Article
- Article
- Prediction of the binding interface between monoclonal antibody m102.4 and Nipah attachment glycoprotein using structure-guided alanine scanning and computational docking.Scientific reports · 2020Article
- Article
- Molecular basis for dengue virus broad cross-neutralization by humanized monoclonal antibody 513.Scientific reports · 2018Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Recently, progress has been made in the development of vaccines and monoclonal antibody cocktails that target the Ebola coat glycoprotein (GP). Based on the mutation rates for Ebola virus given its natural sequence evolution, these treatment strategies are likely to impose additional selection pressure to drive acquisition of mutations in GP that escape neutralization. Given the high degree of sequence conservation among GP of Ebola viruses, it would be challenging to determine the propensity of acquiring mutations in response to vaccine or treatment with one or a cocktail of monoclonal antibodies. In this study, we analyzed the mutability of each residue using an approach that captures the structural constraints on mutability based on the extent of its inter-residue interaction network within the three-dimensional structure of the trimeric GP. This analysis showed two distinct clusters of highly networked residues along the GP
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