PubMed · 7424864
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Y Ichiba, N Namba, H Misumi. 1980. Uridine diphosphate galactose 4-epimerase deficiency.. https://doi.org/10.1001/archpedi.1980.02130220071025
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Escherichia coli O157 strains have emerged as important human enteric pathogens. Strains that express the O-antigen 157 are commonly associated with severe clinical manifestations, including bloody diarrhea, hemorrhagic colitis, and hemolytic uremic syndrome. E. coli O157 strains may be transmitted in a variety of ways, including food, water and person-to-person or animal-to-person contact. Fecal contamination is one source of environmental contamination and is responsible for the presence of these pathogens in the environment. We used a specific and sensitive PCR assay based on the rfbE gene to detect low levels of these pathogens in wastewater. The set of primers used was designed to amplify an intragenic segment of the rfbE gene. The amplification assay detected 200 CFU of E. coli O157 in pure water. The prevalence of E. coli O157 in the effluents of 44 wastewater treatment plants was determined (7%).
We investigated the relationship between expression of the O side chain of outer membrane lipopolysaccharide (LPS) and infection by a Shiga toxin 2 (Stx2)-converting phage in normal and benign strains of Escherichia coli. Of 19 wild-type E. coli strains isolated from the feces of healthy subjects, those with low-molecular-weight LPS showed markedly higher susceptibility to lytic and lysogenic infection by Stx2 phages than those with high-molecular-weight LPS. All lysogens produced infectious phage particles and Stx2. The Stx-negative E. coli O157:H7 strain ATCC43888 with an intact O side chain was found to be resistant to lysis by an Stx2 phage and lysogenic infection by a recombinant Stx2 phage, whereas a rfbE mutant deficient in the expression of the O side chain was readily infected by the phage and yielded stable lysogens. The evidence suggests that an O side chain deficiency leads to the creation of new pathotypes of Shiga toxin-producing E. coli (STEC) within the intestinal microflora.
A recombinant Escherichia coli strain was developed to produce guanosine 5'-diphosphate (GDP)-L-fucose, donor of L-fucose, which is an essential substrate for the synthesis of fucosyloligosaccharides. GDP-D: -mannose-4, 6-dehydratase (GMD) and GDP-4-keto-6-deoxymannose 3, 5-epimerase 4-reductase (WcaG), the two crucial enzymes for the de novo GDP-L-fucose biosynthesis, were overexpressed in recombinant E. coli by constructing inducible overexpression vectors. Optimum expression conditions for GMD and WcaG in recombinant E. coli BL21(DE3) were 25 degrees C and 0.1 mM isopropyl-beta-D-thioglucopyranoside. Maximum GDP-L-fucose concentration of 38.9 +/- 0.6 mg l(-1) was obtained in a glucose-limited fed-batch cultivation, and it was enhanced further by co-expression of NADPH-regenerating glucose-6-phosphate dehydrogenase encoded by the zwf gene to achieve 55.2 +/- 0.5 mg l(-1) GDP-L-fucose under the same cultivation condition.