In Campylobacter jejuni, an htrB homologous gene is located in the lipo-oligosaccharide synthesis gene cluster. This study examined the effects of htrB expression on the responsiveness of Salmonella typhimurium and C. jejuni to harsh environments. Complementation experiments showed that the C. jejuni htrB gene could restore the normal morphology of the Salmonella htrB mutant, and its ability to grow without inhibition under heat, acid and osmotic stresses, but not bile stress. This indicated that the htrB genes in C. jejuni and S. typhimurium exhibit similar pleiotropic effects. Moreover, quantitative real-time RT-PCR showed that expression of the C. jejuni htrB gene was upregulated under acid, heat, oxidative and osmotic stresses, but did not change under bile stress. This indicated that the C. jejuni htrB gene plays a role in regulating cell responses to various environmental changes. Furthermore, deletion mutation of the htrB gene in C. jejuni was lethal, indicating that the htrB gene is essential for C. jejuni survival. Therefore, these results showed that expression of the htrB gene is essential for the response of S. typhimurium and C. jejuni to environmental stresses.
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http://dx.doi.org/10.1099/mic.0.29230-0 | DOI Listing |
Microbiology (Reading)
July 2023
Department of Molecular Microbiology, John Innes Centre, Norwich, Norwich Research Park, NR4 7UH, UK.
CutRS was the first two-component system to be identified in species and is highly conserved in this genus. It was reported >25 years ago that deletion of increases the production of the antibiotic actinorhodin in . However, despite this early work, the function of CutRS has remained enigmatic until now.
View Article and Find Full Text PDFBMC Microbiol
April 2023
Department of Veterinary Medicine, University of Cambridge, Madingley Road, Cambridge, UK.
Campylobacter species are the major cause of bacterial gastroenteritis. As there is no effective vaccine, combined with the rapid increase in antimicrobial resistant strains, there is a need to identify new targets for intervention. Essential genes are those that are necessary for growth and/or survival, making these attractive targets.
View Article and Find Full Text PDFVet Res Commun
December 2022
Department of Animal Health, University of Cordoba, Animal Health Building, Campus Universitario de Rabanales, 14014, Córdoba, Spain.
The aim of this study was to determine the prevalence of the htrA, htrB and ppk1 genes -all of which are related to environmental persistence- in C. jejuni and C. coli isolates obtained from abattoir samples at the arrival of broilers (initial stage) and in meat products after processing (final stage).
View Article and Find Full Text PDFMicrobiol Spectr
October 2022
Key Laboratory of Molecular Biophysics of the Ministry of Education, Hubei Key Laboratory of Bioinformatics and Molecular-Imaging, Department of Bioinformatics and Systems Biology, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, Hubei, China.
The genus Campylobacter contains pathogens that cause bacterial gastroenteritis in humans and animals. Despite large-scale sequencing efforts to raise clinical awareness of Campylobacter, little is known about the diversity and functions of virulence factors. Here, we constructed the pan-genome of Campylobacter using 39 representative genomes, elucidating their genetic diversity, evolutionary characteristics, and virulence and resistance profiles.
View Article and Find Full Text PDFAppl Biochem Biotechnol
March 2022
State Key Laboratory of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi, 214122, China.
Bacillus subtilis has many attributes that make it a popular host for recombinant protein production. Although its protein production ability has been enhanced through protease gene disruption, residual proteases like quality control HtrA and HtrB can limit protein yield by degrading inadequately folded proteins present during overexpression. In this study, two strategies were employed to increase production of industrial enzyme pullulanase: enhancing extracellular pullulanase folding and optimizing its signal peptide.
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