The effects of PA-I lectin isolated from the human pathogen Pseudomonas aeruginosa upon cellular metabolism in vivo have been studied using the rat gut as a model system. Orally ingested PA-I lectin stimulated metabolic activity and induced polyamine accumulation and growth in the small intestine, caecum and colon. The nature and extent of the changes induced by PA-I lectin were similar to those caused by dietary kidney bean lectin and were likely to lead to impaired epithelial cell function and integrity. This finding contributes to our understanding of the possible roles of these lectins in Pseudomonas aeruginosa infection.
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http://dx.doi.org/10.1111/j.1574-695X.1995.tb00116.x | DOI Listing |
FEMS Microbiol Lett
July 2014
Departamento de Biología Molecular y Biotecnología, Instituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México, México, México.
Pseudomonas aeruginosa is a free-living bacterium and an important opportunistic pathogen. The genes coding for virulence-associated traits are regulated at the level of transcription by the quorum-sensing response. In this response, the regulator LasR coupled with the autoinducer 3-oxo-dodecanoyl homoserine lactone (3O-C12-HSL) activates transcription of genes for several virulence factors.
View Article and Find Full Text PDFAnn Surg
February 2012
Center of Surgical Infection Research and Therapeutics, Department of Surgery, Pritzker School of Medicine, University of Chicago, Chicago, IL 60637, USA.
Objective: This study was designed to examine the effect of morphine administration on the intestinal mucus barrier and determine its direct effect on the virulence and lethality of Pseudomonas aeruginosa, one of the most frequent pathogens to colonize the gut of critically ill patients.
Background Data: Surgical injury is associated with significant exposure of host tissues to morphine from both endogenous release and its use as a potent analgesic agent. Morphine use in surgical patients exposed to extreme physiologic stress is well established to result in increased infection risk.
Surgery
August 2008
Department of Surgery, Pritzker School of Medicine, University of Chicago, Chicago, IL, USA.
Background: We explored the possibility that the opportunistic pathogen, Pseudomonas aeruginosa senses low phosphate (Pi) as a signal of host injury and shifts to a lethal phenotype.
Methods: Virulence expression in P aeruginosa was examined in vitro under low phosphate conditions by assessing expression of the PA-I lectin, a barrier dysregulating protein, pyocyanin, and biofilm production, and PstS, a phosphate scavenging protein. Virulence expression in vivo was assessed using operatively injured mice (30% hepatectomy) intestinally inoculated with P aeruginosa.
Am J Physiol Gastrointest Liver Physiol
January 2007
Department of Surgery, University of Chicago, Chicago, Illinois, USA.
Human intestinal epithelial cell monolayers (Caco-2) subjected to hypoxia and reoxygenation release soluble factors into the apical medium that activate the virulence of the opportunistic pathogen Pseudomonas aeruginosa to express the potent barrier-dysregulating protein PA-I lectin/adhesin. In this study, we defined the role of hypoxia-inducible factor (HIF)-1alpha in this response. We tested the ability of medium from Caco-2 cells with forced expression of HIF-1alpha to increase PA-I expression in P.
View Article and Find Full Text PDFAnal Biochem
January 2006
Faculty of Pharmaceutical Sciences, Kinki University, Kowakae 3-4-1, Higashiosaka-shi, Osaka 577-8502, Japan.
Animal colostrum and milk contain complex mixtures of oligosaccharides, which have species-specific profiles. Milk oligosaccharides have various types of structure related to the core structures of glycolipids and N- and O-glycans of glycoproteins and provide a good library to examine the binding of oligosaccharides to various lectins. Recently, we reported a capillary affinity electrophoresis (CAE) method for analyzing the interactions between lectins and complex mixtures of N-linked oligosaccharides prepared from serum glycoproteins.
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