Rapid disruption of epithelial barrier function by Salmonella typhimurium is associated with structural modification of intercellular junctions.
Short-term infection of MDCK II monolayers with Salmonella typhimurium SL1344 caused a progressive decrease in transepithelial electrical resistance concomitant with decreased cation permselectivity and increased paracellular inulin flux. Cytochemical staining of F-actin, E-cadherin, and ZO-1 revealed the concentration of each junctional protein in invaded cells as a result of contraction at their apical poles and resultant distortion of adjacent uninvaded cells.
Jepson
M A
MA
Department of Physiological Sciences, Medical School, University of Newcastle upon Tyne, United Kingdom.
Collares-Buzato
C B
CB
Clark
M A
MA
Hirst
B H
BH
Simmons
N L
NL
D000199:Actins / Q000302:isolation & purification; D000818:Animals; D015820:Cadherins / Q000302:isolation & purification; D002463:Cell Membrane Permeability; D016764:Cell Polarity; D002478:Cells, Cultured; D004285:Dogs; D017097:Electric Impedance; D004848:Epithelium / Q000382:microbiology; D005455:Fluorescent Antibody Technique; D007365:Intercellular Junctions / Q000648:ultrastructure*; D007668:Kidney / Q000166:cytology; D008564:Membrane Potentials; D008565:Membrane Proteins / Q000302:isolation & purification; D010750:Phosphoproteins / Q000302:isolation & purification; D012486:Salmonella typhimurium / Q000254:growth & development*; D062826:Zonula Occludens-1 Protein
D000199:Actins; D015820:Cadherins; D008565:Membrane Proteins; D010750:Phosphoproteins; D062826:Zonula Occludens-1 Protein