10.1371/journal.ppat.1006841.g003 Swastik De Swastik De Katherine Kaus Katherine Kaus Shada Sinclair Shada Sinclair Brandon C. Case Brandon C. Case Rich Olson Rich Olson Glycan binding affinities. Public Library of Science 2018 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 18:46:13 Figure https://plos.figshare.com/articles/figure/Glycan_binding_affinities_/5880757 <p>Binding affinities for various glycans were determined using ITC (blue) or intrinsic tryptophan fluorescence spectroscopy (red). Errors are reported as 95% confidence levels (for ITC data) or the standard error of the mean (for fluorescence data). Dashes represent experiments not carried out due to lack of feasibility. Carbohydrates are represented as described in <a href="http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1006841#ppat.1006841.g002" target="_blank">Fig 2A</a>. *Asialofetuin is a glycoprotein containing three primary glycosylation sites, which contain a mixture of bi- and tri-antennary glycans [<a href="http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1006841#ppat.1006841.ref035" target="_blank">35</a>]. Data were fit assuming three sites per glycoprotein, but due to the heterogeneity of glycosylation these numbers may represent an overestimation of the binding affinity. The asialofetuin schematic shows the predominant tri-antennary glycan.</p>