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Journal: bioRxiv
Article Title: High-throughput discovery of peptide activators of a bacterial sensor kinase
doi: 10.1101/2021.06.01.446581
Figure Lengend Snippet: ( a ) SLAY-TCS workflow. ( b ) Sort gate strategy for sort-seq, with sorting bins represented by alternating light and dark grey bars (see Supplementary Table 2 for bin edge fluorescence values). Histogram represents the results from a single biological replicate ( n = 1). ( c ) Calculated fluorescence distributions of no peptide, negative (defensin HNP-1), and positive (LL-37) control strains included in the library. Vertical lines indicate estimated mean fluorescence values for each control. ( d ) Sort-seq fold activation relative to no peptide control strains for all human AMP activators with > 2-fold activation. ( e ) Net charge and hydrophobicity, as measured by grand average of hydropathicity (GRAVY), for all human AMPs included in the screen. Human AMPs belonging to the same cluster ( Supplementary Table 1 ) are represented by a single data point with error bars indicating the median and 25 th to 75 th percentile ranges for that cluster. ( f ) Performance of the cathelicidin sparse robust linear model on peptide variants of human AMP activators of PhoPQ (cathelicidin, CCL20, hBD3, CCL19, NPY, GNLY, TCP) and on peptides variants of non-activating human AMPs (Other). Coefficient of determination ( r 2 ) and Pearson correlation coefficient ( r ) values were calculated for log 10 -transformed fold change and predicted fold change values.
Article Snippet: Macrophage cell lysates were collected at 4 h post-infection and subjected to
Techniques: Fluorescence, Control, Activation Assay, Transformation Assay