Energy landscape reshaped by strain-specific mutations underlies epistasis in NS1 evolution of influenza A virus

• Published in: Nature communications Vol. 13; no. 1; pp. 5775 - 13
• Main Authors: Kim, Iktae, Dubrow, Alyssa, Zuniga, Bryan, Zhao, Baoyu, Sherer, Noah, Bastiray, Abhishek, Li, Pingwei, Cho, Jae-Hyun
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 01.10.2022; Nature Publishing Group; Nature Portfolio
• Subjects: 1-Phosphatidylinositol 3-kinase; 101/6; 631/181/735; 631/326/596/1578; 631/535/878/1263; 82/103; 82/6; 82/80; 82/83; Binding; Dynamic structural analysis; Energy; Epistasis; Evolution; Humanities and Social Sciences; Hydrophobicity; Influenza; Influenza A; Kinases; Molecular evolution; multidisciplinary; Mutation; NMR; Nuclear magnetic resonance; Proteins; Residues; Science; Science (multidisciplinary); Spin dynamics; Virulence factors; Viruses

Elucidating how individual mutations affect the protein energy landscape is crucial for understanding how proteins evolve. However, predicting mutational effects remains challenging because of epistasis—the nonadditive interactions between mutations. Here, we investigate the biophysical mechanism of...