"""Nsp2 possesses multiple interaction surfaces for host proteins. (A) Interaction scores (average between MiST and Saint Scores) for human proteins (""""preys"""") deemed high-confidence interactions in at least one affinity purification (""""bait"""") mass spectrometry assay and detected to interact with both the wild-type Nsp2 in this study and in Gordon et al (2020a). Interaction scores range from zero to one, one being the most high-confidence. (B) Quantitative statistical analysis of data-dependent acquisition (DDA) mass spectrometry data using MSstats for interactions selected and depicted in A. Prey intensities were normalized by bait expression abundance. Log2 fold changes and BH-adjusted p-values were calculated by comparing each mutant to the wild-type from this study. Square black outlines depict adjusted p-values < 0.05. (C) Parallel reaction monitoring (PRM) analysis of select preys from B for mutants found to possess significantly-changed interactions (adjusted p-value < 0.05). (D) Nsp2 structure depicted as surface (light blue) with the mutations considered in this study depicted on the surface: E63K/E66K (dark blue), K330D/K337D (red), D23Y/R27C (yellow), T85I (orange), and G262V/G265V (grey). Lost interactions (adjusted p-value < 0.05) from data-dependent acquisition global proteomics analysis (DDA) from B depicted in blue and gained protein complexes depicted in red"""
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