Project description:A survey for nematode infection in German cockroaches captured in restaurants in various areas of Japan as well as the laboratory-bred colony was carried out. The nematodes were then identified morphologically and molecularly. Of the 320 German cockroaches collected at 79 restaurants in 26 prefectures in Japan, 66.6% (213/320) were found to be parasitized by a single species of pinworm in the hindgut. The mean number of pinworms per cockroach was less than 1.6. Of the three laboratory-bred lines of cockroaches examined, 2 lines (NIID and NK) were found to be infected with a single species of nematode. The prevalence was 93.0% (40/43) and 84.8% (39/46), respectively. The other laboratory line (WAT) was found to be free of the nematode infection. The nematode detected in this study was identified as Blatticola blattae. This is the first report of B. blattae infection in German cockroaches in Japan. Our study showed that B. blattae is distributed all over Japan together with its host Blattella germanica. An experimental infection with B. blattae in nematode-free cockroach by contaminating the rearing environment with infected-cockroach feces showed that once the environment of the cockroach is contaminated with B. blattae eggs, the pinworm infection could spread easily.
Project description:Here, we adapted and improved our FASTBAC-Seq method originally designed in Helicobacter pylori to investigate T1TAs in the model organism Escherichia coli. Our approach combines a life and death selection with deep-sequencing to assess the killing capability of a toxin and obtain an overview of single-nucleotide substitutions suppressing the toxin expression or activity in absence of its antitoxin. As a proof of concept, we revisited the regulation of the plasmidic hok/Sok T1TA system.
Project description:Here we announce the complete genome sequence of the coenzyme B(12)-producing enteric bacterium Shimwellia blattae (formerly Escherichia blattae). The genome consists of a single chromosome (4,158,636 bp). The genome size is smaller than that of most other enteric bacteria. Genome comparison revealed significant differences from the Escherichia coli genome.
Project description:The purpose of the present study was to elucidate in more details the molecular mechanisms of neutrophil-mediated inflammation. We therefore investigated the time-dependent stimulatory potential of LPS from Escherichia coli on cytokine response in neutrophil-like HL-60 cells. <br><br>To get a general overview on the total mRNA changes in DMSO-differentiated HL-60 cells, we performed whole-transcript analysis of LPS-stimulated dHL-60 cells after 2h and 6h of LPS treatment. The samples were collected from three independent experiments from three different passages in cell culture. Non-stimulated dHL-60 cells served as control. We identified the differentially expressed cytokine genes implicated in the human inflammatory response and prominent for their role in neutrophil-mediated inflammatory processes.
Project description:The structure of Escherichia blattae non-specific acid phosphatase (EB-NSAP) has been determined at 1.9 A resolution with a bound sulfate marking the phosphate-binding site. The enzyme is a 150 kDa homohexamer. EB-NSAP shares a conserved sequence motif not only with several lipid phosphatases and the mammalian glucose-6-phosphatases, but also with the vanadium-containing chloroperoxidase (CPO) of Curvularia inaequalis. Comparison of the crystal structures of EB-NSAP and CPO reveals striking similarity in the active site structures. In addition, the topology of the EB-NSAP core shows considerable similarity to the fold of the active site containing part of the monomeric 67 kDa CPO, despite the lack of further sequence identity. These two enzymes are apparently related by divergent evolution. We have also determined the crystal structure of EB-NSAP complexed with the transition-state analog molybdate. Structural comparison of the native enzyme and the enzyme-molybdate complex reveals that the side-chain of His150, a putative catalytic residue, moves toward the molybdate so that it forms a hydrogen bond with the metal oxyanion when the molybdenum forms a covalent bond with NE2 of His189.
