Publications by authors named "Evgeniya Bystritskaya"

A Gram-negative, aerobic, rod-shaped, non-motile, yellow-pigmented bacterium, KMM 9835, was isolated from the sediment sample obtained from the Amur Bay of the Sea of Japan seashore, Russia. Phylogenetic analyses based on the 16S rRNA gene and whole genome sequences positioned the novel strain KMM 9835 in the genus as a separate line sharing the highest 16S rRNA gene sequence similarities of 96.6% and 96.

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Here, we investigated general porin regulation in 488, the causative agent of Far Eastern scarlet-like fever, in response to sublethal concentrations of antibiotics. We chose four antibiotics of different classes and measured gene expression using qRT-PCR and GFP reporter systems. Our data showed temporal regulation of the general porin genes and caused by antibiotic stress.

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We carried out a detailed investigation of PL7 alginate lyases across the genus. The main findings were obtained using the methods of comparative genomics and spatial structure modeling, as well as a phylogenomic approach. Initially, in order to elucidate the alginolytic potential of , we calculated the content of polysaccharide lyase (PL) genes in each genome.

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We obtained two novel draft genomes of type strains with estimated genome sizes of 5.14 Mb for KMM 3526 and 5.16 Mb for KMM 3676.

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Twenty-three bacterial strains were isolated from the secreted mucus trapping net of themarine polychaete Chaetopterus variopedatus (phylum Annelida) and twenty strains were identifiedusing 16S rRNA gene analysis. Strain CB1-14 was recognized as a new species of the genus Vibriousing the eight-gene multilocus sequence analysis (MLSA) and genome sequences of nineteen typeVibrio strains. This Vibrio sp.

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The low permeability of porin channels is the possible reason for Gram-negative bacterial resistance to antibiotics. The adaptive accumulation of lysophosphatidylethanolamine (LPE) in Yersinia pseudotuberculosis induces conformational changes of OmpF porin that may hinder the transport of antibiotics through this channel. The present study was aimed to test whether the changes in LPE content affect the resistance of bacteria to ampicillin.

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Article Synopsis
  • Tick-borne encephalitis is a serious public health issue with limited treatment options, highlighting the need for effective vaccines targeting the virus's key antigenic domain, domain III of the E protein.* -
  • This study aimed to create a chimeric protein by fusing domain III of the E protein with a bacterial protein (OmpF) to enhance immunogenicity and reduce toxicity, leading to successful expression in E. coli.* -
  • The resulting chimeric protein was confirmed to elicit an antibody response in mice, suggesting its potential as a candidate for developing preventive vaccines against tick-borne encephalitis.*
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The genus Yersinia includes species with a wide range of eukaryotic hosts (from fish, insects, and plants to mammals and humans). One of the major outer membrane proteins, the porin OmpC, is preferentially expressed in the host gut, where osmotic pressure, temperature, and the concentrations of nutrients and toxic products are relatively high. We consider here the molecular evolution and phylogeny of Yersinia ompC.

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The capability of Yersinia ruckeri to survive in the aquatic systems reflects its adaptation (most importantly through the alteration of membrane permeability) to the unfavorable environments. The nonspecific porins are a key factor contributing to the permeability. Here we studied the influence of the stimuli, such as temperature, osmolarity, and oxygen availability on regulation of Y.

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