De, Swastik Kaus, Katherine Sinclair, Shada Case, Brandon C. Olson, Rich Binding of RbmC1 and RbmC2 to mammalian cells. <p>(A) Fluorescence microscopy of defibrinated rabbit whole blood incubated with the RbmC2-GFP<sub>UV</sub> fusion. Wild-type or a D853A point mutation (with significantly reduced glycan-binding activity) are shown. Images include GFP, brightfield, and merged channels for constructs at 2.5 μM and 0.5 μM concentrations. Each WT/mutant pair was placed on an identical brightness scale, but WT and D853A are on different brightness scales. The white scale bar (lower right on the merged image) represents 10 microns. (B) Same as in A, but with WT RbmC1 and the D539A point mutation (purple asterisk on <a href="http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1006841#ppat.1006841.g001" target="_blank">Fig 1C</a>).</p> cholerae secretes virulence factors;carboxy-terminal β- prism domain;cholerae β- prism selectivity;bind carbohydrate receptors;biofilm proteins Vibrio cholerae;strategy;biofilm matrix proteins;RbmC β- prism domains target;pentasaccharide core;VCC β- prism domain;RbmC β- prism domain;Vibrio cholerae cytolysin;toxin;cholerae biofilm matrix protein RbmC;β- prism domains;glycan;target host cells 2018-02-12
    https://plos.figshare.com/articles/figure/Binding_of_RbmC1_and_RbmC2_to_mammalian_cells_/5880772
10.1371/journal.ppat.1006841.g006