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Alkali‐Treated LPS of Yersinia enterocolitica does not Induce Expression of E‐Selectin, ICAM‐1 or VCAM‐1 on Endothelial Cells but may Mediate Antibody‐ and Complement‐Dependent Cell Injury
Author(s) -
REPO H.,
RENKONEN R.,
HELANDER I. M.,
LEIRISALOREPO M.
Publication year - 1994
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1994.tb03367.x
Subject(s) - yersinia enterocolitica , yersinia , lipopolysaccharide , microbiology and biotechnology , yersinia infections , cell adhesion molecule , inflammation , chemistry , immunology , enterobacteriaceae , biology , escherichia coli , bacteria , biochemistry , genetics , gene
Lipopolysaccharide (LPS) prepared from a rough mutant of Salmonella typhimurium and deacylated enzymatically (dLPS) does not promote neutrophil adherence to human umbilical vein endothelial cells (HUVECs). This paper reports that similarly, a smooth form of LPS prepared from Yersinia enlerocolitica O:3, a serotype known to trigger reactive arthritis in humans, and treated with alkali (yersinia LPS‐OH) failed to augment neutrophil adherence to HUVECs. Studies of the mechanism underlying the poor augmentation revealed that neither enzymatically deacylated LPS from Escherichia coli J5 (J5 dLPS) nor yersinia LPS‐OH stimulated expression of endothelial cell adhesion molecules E‐selectin, VCAM‐1 and ICAM‐1, whereas both Intact J5 LPS and yersinia LPS were stimulatory. Impaired up‐regulation could not be explained by decreased binding of yersinia LPS‐OH to HUVECs. Furthermore, 51 Cr‐labelled HUVECs treated with different concentrations of yersinia LPS‐OH released 51 Cr in the presence of anti‐yersinia anti‐0 antibody and complement. J5 dLPS and yersinia LPS‐OH inhibited up‐regulation of the adhesion molecules induced by J5 LPS and yersinia LPS but not that induced by tumour necrosis factor alpha. Taken together, the results suggest that although yersinia LPS‐OH can depress development of acute inflammation by inhibiting up‐regulation of etidothelial‐cell adhesion molecules, sufiicient LPS‐OH is bound to induce cell injury and thereby inflammation in the prescence of specific antibody and complement. The findings may have pathogenetic implications in yersinia‐triggered reactive arthritis characterized by dissemination of yersinia LPS throughout the body.