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>