Mechanisms of Crystalloid versus Colloid Osmosis across the Peritoneal Membrane.

Osmosis drives transcapillary ultrafiltration and water removal in patients treated with peritoneal dialysis. Crystalloid osmosis, typically induced by glucose, relies on dialysate tonicity and occurs through endothelial aquaporin-1 water channels and interendothelial clefts. In contrast, the mechanisms mediating water flow driven by colloidal agents, such as icodextrin, and combinations of osmotic agents have not been evaluated.

Addition of a nitric oxide inhibitor to a more biocompatible peritoneal dialysis solution in a rat model of chronic renal failure.

Biocompatible dialysis solutions have been developed to preserve peritoneal membrane morphology and function. Compared with a conventional solution, a combination of glycerol, amino acids, and dextrose in a bicarbonate/lactate buffer (GLAD) led to less peritoneal fibrosis and fewer vessels in a chronic peritoneal exposure model in the rat. However, no concomitant reduction in small-solute transport was observed.

The effects of a dialysis solution with a combination of glycerol/amino acids/dextrose on the peritoneal membrane in chronic renal failure.

Background: Long-term peritoneal dialysis (PD) with conventional glucose based, lactate-buffered PD fluids may lead to morphological and functional alterations of the peritoneal membrane. It was hypothesized that long-term exposure to a different buffer and a mixture of osmotic agents would cause less peritoneal abnormality.

Objectives: To investigate the effects of long-term exposure to a bicarbonate/lactate-buffered dialysis solution with a mixture of osmotic agents: glycerol 1.

High prevalence iron receptor genes of avian pathogenic Escherichia coli.

Avian pathogenic Escherichia coli are known to cause significant losses in the poultry industry worldwide. Although prophylactic measures based on vaccination are advisable, until now no full heterologous protection against colibacillosis has been achieved. Since iron is an essential nutrient to these bacteria, the aim of this study was to investigate the prevalence of 12 outer-membrane iron receptor genes in 239 pathogenic strains isolated from clinical cases of colibacillosis in chickens.

Immunization with the biologically active lectin domain of PapGII induces strong adhesion-inhibiting antibody responses but not protection against avian pathogenic Escherichia coli.

The aim of this study was to investigate whether immunization with the sugar binding domain of PapGII (PapGII196) was able to protect chickens against avian pathogenic Escherichia coli. PapGII196 was expressed, purified by Ni-NTA column chromatography and shown to retain its biological activity, as demonstrated by binding to its receptor, globoside. PapGII196 was tested as a vaccine in specific pathogen free broilers and also by vaccinating breeders and assessing protection in their offspring, and using aerosol exposure or air sac inoculation for challenge.

Immunization with the binding domain of FimH, the adhesin of type 1 fimbriae, does not protect chickens against avian pathogenic Escherichia coli.

The aim of this study was to investigate whether vaccination with the sugar-binding domain of FimH (FimH156) was able to protect chickens against avian pathogenic Escherichia coli (APEC). FimH156 was expressed and purified using Ni-NTA affinity chromatography. Binding of FimH156 to mannosylated bovine serum albumin demonstrated that the protein retained its biological activity.

Predominance of the papGII allele with high sequence homology to that of human isolates among avian pathogenic Escherichia coli (APEC).

Avian pathogenic Escherichia coli (APEC) are often found in poultry and are responsible for a set of diseases, commonly referred to as avian colibacillosis. One of the important virulence factors is adhesion to different epithelial surfaces, which is mediated by pili. P pili are thought to play a role by means of their PapG adhesin, which occurs in three molecular variants: PapGI, PapGII and PapGIII.

Sequence analysis demonstrates the conservation of fimH and variability of fimA throughout avian pathogenic Escherichia coli (APEC).

In this study we sequenced and analysed the fimH and fimA genes of 24 avian pathogenic Escherichia coli (APEC) isolates, in order to investigate their possible conserved nature. Additional parameters (serotype, presence of aerobactin receptor, expression of F1 pili and virulence for chickens) were investigated to look for correlations with the obtained sequences. The sequence analysis demonstrated that FimH is highly conserved among all investigated APEC strains (>99% homology), whereas the major subunit FimA is less conserved, presenting 6 variable regions distributed along the protein.