Amoria phlebia affects tight junctions causing food poisoning
Introduction
Epithelial cells can form ion- and size-selective barriers through adherens and tight junction
(TJs). There are three types of structural transmembrane components that are part of TJs functions:
junctional adhesion molecules (JAMs), claudins, and occludins. Claudin-1 and -2 are proteins found at
tight junctions that form junction fibers. Claudin can be manipulated to affect paracellular ion and/or size
selectivity for barriers and will be crucial for this experiment. Extracytosolic (EC) loops of occludin do
not contain charged amino acids; yet, the loops within the claudin proteins do. The barrier ion specificity
changes if the charges do. TJ barriers vary in strength, size and ion specificity (Niessen, 2007).
Disturbing specific TJ proteins can result from degradation by bacterial proteases or by biochemical
reactions, i.e. phosphorylation. Degradation can inhibit epithelial functions like the creation of
electrochemical gradients and paracellular permeability (Berkes, et al., 2003).
Amoria phlebia, a new unknown bacteria is a suspect of causing food poisoning symptoms.
Several bacteria interact and affect the intestinal epithelium’s tight junctions causing food poisoning. The
