The de novo expression of Escherichia coli K1, K5, and K12 capsules was analyzed with immunoelectron microscopy in temperature upshift experiments, with upshift from 18 degrees C (capsule restrictive) to 37 degrees C (capsule permissive). Newly produced capsular polysaccharides appeared at the cell surface atop membrane adhesion sites (Bayer's junctions). After plasmolysis of the bacteria at an early expression stage, the capsular polysaccharides were labeled at discrete sites in the periplasm by the immunogold technique. After temperature upshift in the presence of carbonyl cyanide m-chlorophenylhydrazone (CCCP) or chloramphenicol, the polysaccharides were labeled in the cytoplasm.
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http://dx.doi.org/10.1128/jb.172.6.3469-3472.1990 | DOI Listing |
J Water Health
January 2025
Department of Biology and Ecology, Faculty of Science, University of Kragujevac, Kragujevac 34000, Serbia.
Extended spectrum -lactamase (ESBL)-producing Enterobacteriaceae, including and , pose a serious risk to human health because of antibiotic resistance. Wastewater serves as a reservoir for these bacteria, contributing to the evolution and transmission of antibiotic-resistant strains. The research aims to identify ESBL bacterium in wastewater samples from District Kohat.
View Article and Find Full Text PDFFront Cell Infect Microbiol
January 2025
College of Public Health, North China University of Science and Technology, Tangshan, China.
Enterohemorrhagic (EHEC) is a contagious foodborne pathogen that specifically colonizes the human large intestine, which is regulated by different environmental stimuli within the gut. Transcriptional regulation of EHEC virulence and infection has been extensively studied, while the posttranscriptional regulation of these processes by small RNAs (sRNAs) remains not fully understood. Here we present a virulence-regulating pathway in EHEC O157:H7, in which the sRNA EvrS binds to and destabilizes the mRNA of Z2269, a novel transcriptional regulator.
View Article and Find Full Text PDFFront Antibiot
January 2025
Institute of Bioanalytical Chemistry, Faculty of Chemistry and Mineralogy, Center for Biotechnology and Biomedicine, Leipzig University, Leipzig, Germany.
Because of the global spread of multi- and pan-resistant bacteria, there is a need to identify, research, and develop new strategies to combat these pathogens. In a previous proof-of-concept study, we presented an innovative strategy by genetically modifying lytic T7 bacteriophages. We integrated DNA fragments encoding for derivatives of the antimicrobial peptide (AMP) apidaecin into the phage genome to induce the production and release of apidaecin within the T7 infection cycle, thereby also targeting phage-resistant bacteria.
View Article and Find Full Text PDFJ Hazard Mater
January 2025
State Key Laboratory of NBC Protection for Civilian, Beijing 102205, China. Electronic address:
This study is the first to use synthetic biological omics technology to analyze the molecular mechanism underlying deep degradation of TNT, to construct an artificial transformation system to create engineered Escherichia coli bacteria, and to use Bacillus subtilis as an expression host to explore the mechanism driving the reshaping of the deep degradation platform on microecology. Nitroreductase family protein, 2-oxoacid:acceptor oxidoreductase, NADPH-cytochrome P450 reductase, monooxygenase, ring-cleaving dioxygenase, and RraA family protein significantly participated in the reduction-hydroxylation-ring opening cleavage of TNT, achieving deep transformation of TNT to produce pyruvic acid and other products that entered the cellular metabolic cycle. The key toxic metabolic pathways of TNT, 2,4-diamino-6-nitrotoluene, 2,4,6-triaminotoluene, and 2,4,6-trihydroxytoluene are pantothenate and CoA biosynthesis.
View Article and Find Full Text PDFJ Chromatogr B Analyt Technol Biomed Life Sci
January 2025
Northwest University Chang An Hospital, Faculty of Life Sciences and Medicine, Northwest University, Xi'an, Shaanxi 710069, China; Department of Clinical Pharmaceutics, Chang An District Hospital, Xi'an, Shaanxi 710118, China. Electronic address:
Immobilizing the target protein on a solid surface with controlled orientation, high specificity, and maintained activity is a proven strategy to enhance the stability of the protein. In this study, we employed an ultra-high affinity protein pair consisting of a mutant of colicin E7 Dnase and its corresponding inhibitor, immunity protein 7(Im7), to develop an immobilized α-adrenoceptor (α-AR) column. Briefly, we expressed α-AR fused with CL7 as a tag at its C-terminus in Escherichia coli cells.
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