Journal
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
Volume 37, Issue 18, Pages 4767-4778Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/07391102.2018.1559100
Keywords
Bioinformatics; botulinum toxin type A; B-cell epitopes prediction; immunogenicity; in silico mutagenesis
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Funding
- Faculty of Biotechnology of Universitas Surabaya
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Botulinum toxin serotype A is a prominent therapeutic enzyme, for both clinical and cosmetic uses. Since this protein is produced by bacteria, it exhibits an allergenic effect when subjected to human therapy. Protein mutagenesis is one method to improve the characteristics of protein. However, in silico study is needed to give suggestion of which amino acid should be mutated. Hence, a lot of money and time can be saved. This study initially screened which residue of the Botulinum toxin serotype A is B-cell epitopes both linearly and conformationally. By overlapping the B-cell epitopes with the excluded conserve sequence, seven residues were allowed to be mutated. There were two proposed muteins showing a reduction in the antigenicity probability: Delta E147, E510F, T1062F, Delta E1080, N1089M and Delta Q1090; and Delta E147, E510F, T1062F, E1080W, N1089M and Delta Q1090. Molecular dynamics simulation of the 3D proposed muteins indicated an increase of flexibility in both muteins compared to that in the native protein. Both muteins have lower antigenicity. In addition, they are similar in structure, stability and functionality compared to the native protein.
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