Fig. 3: Structure of domain I and transepithelial transport of PLTs.
From: Discovery of mono-ADP ribosylating toxins with high structural homology to Pseudomonas exotoxin A
a PE (PDB 1IKQ; grey), b Collimonas (Cfx; blue), c Chromobacterium (Hmx; green), d Janthinobacterium (Jlx; red), and e Shewanella (Spx; yellow) exotoxins in upper panels. The lower panels show the electrostatic surface potential of domain I from each toxin, calculated using the APBS tool in PyMOL (scale from -5, red to +5, blue), with proteins in the same orientation as the upper panels. f, g Fusion proteins composed of domain I regions of each PLT genetically conjoined to human growth hormone (hGH) were examined for their capacity for apical to basal transport across human (f) small intestinal (SMI-100) or (g) airway (AIR-100) cell monolayers. Domain I PLT-hGH fusions were applied to apical surfaces at 20 µg/mL with total transport determined after 2 h by ELISA for hGH with standard curves prepared using each chimera. n = 3; mean ± SEM. A one-way ANOVA test was used and showed there was a significant variance between the data sets, with *p < 0.05 compared to the control group in a Bonferroni post-test. The p-values for (f) are overall ANOVA p = 0.0118. Chx p = 0.0301. Sfx p = 0.0234, and (g) overall ANOVA p = 0.0052. PE p = 0.0217. Abx p = 0.0457. Sfx p = 0.0118.
