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PMID: 11207548 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Inhibition of Shigella flexneri-induced transepithelial migration of polymorphonuclear leucocytes by cadaverine.

Cellular microbiology ·Vol. 1 ·No. 2 ·1999-09-00 ·Pages 143-55

McCormick BA, Fernandez MI, Siber AM, Maurelli AT

Abstract

Dysentery caused by Shigella species is characterized by infiltration of polymorphonuclear leucocytes (PMNs) into the colonic mucosa. Shigella spp. evolved into pathogens by the acquisition of virulence genes and by the deletion of 'antivirulence' genes detrimental to its pathogenic lifestyle. An example is cadA (encoding lysine decarboxylase), which is uniformly absent in Shigella spp., whereas it is present in nearly all isolates of the closely related non-pathogen Escherichia coli. Here, using monolayers of T84 cells to model the human intestinal epithelium, we determined that the introduction of cadA into S. flexneri and the expression of lysine decarboxylase attenuated the bacteria's ability to induce PMN influx across model intestinal epithelium. Such inhibition was caused by cadaverine generated from the decarboxylation of lysine. Cadaverine treatment of model intestinal epithelia specifically inhibited S. flexneri induction of PMN transepithelial migration, while having no effect on the ability of Salmonella or enteropathogenic E. coli (EPEC) to induce PMN migration. These observations not only provide insight into mechanisms of S. flexneri pathogen evolution and pathogenesis, but also suggest a potential for the use of cadaverine in the treatment of dysentery.

MeSH Terms
Actins/metabolism Cadaverine/metabolism,pharmacology Carboxy-Lyases/genetics,metabolism Cell Culture Techniques Cell Line Cell Movement/drug effects,physiology Cell Polarity Cell Size Dose-Response Relationship, Drug Dysentery Enzyme-Linked Immunosorbent Assay Escherichia coli O157/metabolism Humans Interleukin-8/metabolism Intestinal Mucosa/cytology,drug effects,microbiology Lysine/metabolism Membrane Proteins/metabolism Microscopy, Fluorescence N-Formylmethionine Leucyl-Phenylalanine/metabolism Neutrophils/drug effects,physiology Phosphoproteins/metabolism Salmonella typhimurium/metabolism Shigella flexneri/metabolism,pathogenicity Signal Transduction Zonula Occludens-1 Protein
Chemicals
Actins Interleukin-8 Membrane Proteins Phosphoproteins TJP1 protein, human Zonula Occludens-1 Protein N-Formylmethionine Leucyl-Phenylalanine Carboxy-Lyases lysine decarboxylase Lysine Cadaverine
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
McCormick B A
Department of Pediatric Gastroenterology and Nutrition, Massachusetts General Hospital-East, Charlestown 02129, USA. mccormic@helix.mgh.harvard.edu
Fernandez M I
Siber A M
Maurelli A T
Article Info
Journal
Cellular microbiology
Abbr.
Cell Microbiol
ISSN
1462-5814
Published
1999-09-00
Pages
143-55
Language
English
Region
England
NLM ID
100883691
Subset
IM
Grants
NIAID NIH HHS · AI-24656 · United States
NIDDK NIH HHS · DK-50989 · United States
NICHD NIH HHS · HD31852 · United States
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