coli. This over-expression did not affect E. coli growth but induced biofilm formation and changed its morphology, indicating functional conservancy.
This is the first compelling evidence depicting the role of a plant BolA-like protein in morphogenetic pathway ICG-001 solubility dmso and biofilm formation. The implications of the phenotypic consequences of this heterologous expression are discussed. “
“The effects of detergents (cholic acid, deoxycholic acid, Triton X-100, and Nonidet P-40) on the secretion of EspB from the locus for enterocyte effacement (LEE) gene-positive Escherichia coli strains were examined. Clinical isolates of eight EPEC strains and seven STEC strains were used to detect EspB after they had been cultivated in Luria–Bertani (LB) broth containing one of the detergents. When the bacteria were cultured in LB broth supplemented with one of the detergents, the amount of EspB produced was increased by 2–32-fold depending on the detergent
and the strain used. EspB was detected in all strains when they were cultured in LB broth containing all of the detergents. The results obtained in this study can be applied to immunological diagnostic methods for detecting EspB and also to the production of EspB for research purposes. Enteropathogenic Escherichia coli (EPEC) is a significant cause of infant diarrhea in developing countries and is often associated with high mortality check details rates. EPEC attach to the microvilli of enterocytes through their intimin protein, causing an attaching-effacing (A/E) lesion and cell disorders, inducing acute gastroenteritis. The genes responsible for the development of this lesion are clustered on a chromosome and form a pathogenicity island called the locus of enterocyte effacement (LEE) (McDaniel et al.,
1995). The LEE of the human Cytidine deaminase EPEC strain E2348/69 was the first to be cloned and sequenced (Elliott et al., 1998). LEE contains genes encoding type III secretion proteins EspA, EspB, and EspD, which are required for attachment and effacement; outer membrane protein intimin, which is required for intimate attachment of EPEC to host cells; and the translocated intimin receptor (Tir) for intimin (Jarvis et al., 1995; Abe et al., 1998). Shiga toxin-producing E. coli (STEC) also cause A/E lesions, but their main virulence factor is Shiga toxin. In research laboratories, EPEC and STEC are defined on the basis of their pathogenic properties, and recently, multiplex PCR has been used (Toma et al., 2003). However, the detection of pathogenic properties is expensive, laborious, and requires expensive apparatus; therefore, they are often defined on the basis of serogrouping, especially in the developing world.