A5005033097- Helicobacter pylori-related gastroenterology studies
- Bacterial Genetics and Biotechnology
- Enzyme Structure and Function
- Microbial Metabolites in Food Biotechnology
- Vibrio bacteria research studies
- Neurological diseases and metabolism
- Salmonella and Campylobacter epidemiology
- Polyamine Metabolism and Applications
- Redox biology and oxidative stress
- Porphyrin Metabolism and Disorders
- Cancer-related gene regulation
- Eosinophilic Esophagitis
- Cerebrovascular and genetic disorders
- Genomics and Phylogenetic Studies
- Barrier Structure and Function Studies
- Galectins and Cancer Biology
- Prion Diseases and Protein Misfolding
- Trace Elements in Health
- Celiac Disease Research and Management
- Gastrointestinal disorders and treatments
- Microbial metabolism and enzyme function
- Biochemical and Molecular Research
- Protein Kinase Regulation and GTPase Signaling
- CRISPR and Genetic Engineering
- Protein Structure and Dynamics
University of Gdańsk
2015-2024
Friedrich-Alexander-Universität Erlangen-Nürnberg
2019-2023
Campylobacter jejuni secretes HtrA (high temperature requirement protein A), a serine protease that is involved in virulence. Here, we investigated the interaction of with host occludin, tight junction strand component. Immunofluorescence studies demonstrated infection polarized intestinal Caco-2 cells C. strain 81-176 resulted redistribution occludin away from junctions into cytoplasm, an effect was also observed human biopsies during acute campylobacteriosis. Occludin knockout were...
The human pathogen Helicobacter pylori is a major risk factor for gastric disease development. Serine protease HtrA an important bacterial virulence that cleaves the cell junction proteins occludin, claudin-8 and E-cadherin, which causes tissue damage. Using casein zymography, we discovered trimer stability varies in clinical H. strains. Subsequent sequence analyses revealed correlated with presence of leucine or serine residue at position 171. importance these amino acids determining was...
The protease high temperature requirement A from the gastric pathogen Helicobacter pylori (HtrA Hp ) belongs to well conserved family of serine proteases. HtrA is an important secreted virulence factor involved in disruption tight and adherens junctions during infection. Very little known about function H. cell physiology due lack htrA knockout strains. Here, using a newly constructed ΔhtrA mutant strain, we found that bacteria deprived showed increased sensitivity certain types stress,...
Abstract Background Serine protease HtrA exhibits both proteolytic and chaperone activities, which are involved in cellular protein quality control. Moreover, is an important virulence factor many pathogens including Helicobacter pylori , for the crucial stage of infection cleavage E-cadherin other cell-to-cell junction proteins. Methods The vitro study H. (HtrA Hp ) activity was carried out using light scattering assays investigation lysozyme aggregates. We produced ∆ htrA deletion point...
Abstract Helicobacter pylori plays an essential role in the pathogenesis of gastritis, peptic ulcer disease, and gastric cancer. The serine protease HtrA, important secreted virulence factor, disrupts epithelium, which enables H . to transmigrate across epithelium inject oncogenic CagA protein into host cells. function periplasmic HtrA for cell is unknown, mainly due unavailability htrA mutants. In fact, has been described as gene this bacterium. We have screened 100 worldwide isolates show...
An increasing resistance of bacteria to the commonly used antimicrobials forces search for alternative or supportive ways cure infections. Targeting virulence factors is one such approaches. The bacterial HtrA proteins are strongly involved in and lack functional many cases impairs invasiveness pathogens. HtrAs act by protecting cells under stressful conditions as well they take direct part invasion host. latter function played predominantly recently identified extracellular fraction HtrA....
The Helicobacter pylori HtrA protein (HtrAHp) is an important virulence factor involved in the infection process by proteolysis of components tight (claudin-8 and occludin) adherens junctions (E-cadherin) between epithelial cells. As a protease chaperone, HtrAHp quality control, which particularly under stress conditions. contains domain two C-terminal PDZ domains (PDZ1 PDZ2). In family, are proposed to play roles, including regulation proteolytic activity. We therefore mutated PDZ1 PDZ2...
Campylobacter jejuni is a predominant zoonotic pathogen causing gastroenteritis and other diseases in humans. An important bacterial virulence factor the secreted serine protease HtrA (HtrACj), which targets tight adherens junctional proteins gut epithelium. Here we have investigated function structure of HtrACj using biochemical assays cryo-electron microscopy. Mass spectrometry analysis identified differences similarities cleavage site specificity for by comparison to counterparts from...
Bacterial HtrAs are proteases engaged in extracytoplasmic activities during stressful conditions and pathogenesis. A model prokaryotic HtrA (HtrA/DegP from Escherichia coli) requires activation to cleave its substrates efficiently. In the inactive state of enzyme, one regulatory loops, termed LA, forms inhibitory contacts area active center. Reduction disulfide bond located middle LA stimulates activity vivo suggesting that this S-S may play a role, although mechanism stimulation is not...
High‐temperature requirement A (HtrA; DegP) from Escherichia coli , an important element of the extracytoplasmic protein quality‐control system, is a member evolutionarily conserved family serine proteases. The characteristic feature this its allosteric mode activation. regulatory loops, L3, L2, L1 and LD play crucial role in transmission signal. Yet, has not been fully elucidated. Therefore, we undertook study to explain individual residues inducing maintaining proteolytic activity HtrA. We...
Helicobacter pylori (H. pylori) expresses the serine protease and chaperone High temperature requirement A (HtrA) that is involved in periplasmic unfolded protein stress response. Additionally, H. pylori-secreted HtrA directly cleaves human cell adhesion molecule E-cadherin leading to a local disruption of intercellular adhesions during pathogenesis. HtrA-mediated cleavage has been observed response broad range pathogens, implying it prevalent mechanism humans. However, less known whether...