A5033998274- Escherichia coli research studies
- SARS-CoV-2 and COVID-19 Research
- Viral gastroenteritis research and epidemiology
- Glycosylation and Glycoproteins Research
- Animal Virus Infections Studies
- Fluorine in Organic Chemistry
- Enterobacteriaceae and Cronobacter Research
- Cancer Research and Treatments
- Monoclonal and Polyclonal Antibodies Research
- Photosynthetic Processes and Mechanisms
- COVID-19 Clinical Research Studies
- Pediatric Urology and Nephrology Studies
- Carbohydrate Chemistry and Synthesis
- Enzyme Structure and Function
- Medical Imaging and Pathology Studies
- Urinary Bladder and Prostate Research
- Chemical Reactions and Isotopes
- Urinary Tract Infections Management
- Trace Elements in Health
- Biochemical and Structural Characterization
- Influenza Virus Research Studies
- Microbial Community Ecology and Physiology
- Radiopharmaceutical Chemistry and Applications
- Porphyrin Metabolism and Disorders
- Bacterial Genetics and Biotechnology
Cyrus Biotechnology
2024
University of Washington
2020-2021
ETH Zurich
2016-2020
Targeting a range of betacoranaviruses In the past 20 years, three highly pathogenic β-coronaviruses have crossed from animals to humans, including most recent: severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). A spike protein that decorates these viruses has an S1 domain binds host cell receptors and S2 fuses viral membranes allow entry. The is target many neutralizing antibodies but more genetically variable than S2, can exert selective pressure, leading resistant variants....
Abstract Ligand–receptor interactions that are reinforced by mechanical stress, so-called catch-bonds, play a major role in cell–cell adhesion. They critically contribute to widespread urinary tract infections pathogenic Escherichia coli strains. These pathogens attach host epithelia via the adhesin FimH, two-domain protein at tip of type I pili recognizing terminal mannoses on epithelial glycoproteins. Here we establish peptide-complemented FimH as model system for fimbrial function. We...
Uromodulin is the most abundant protein in human urine, and it forms filaments that antagonize adhesion of uropathogens; however, filament structure mechanism protection remain poorly understood. We used cryo-electron tomography to show uromodulin consists a zigzag-shaped backbone with laterally protruding arms. N-glycosylation mapping biophysical assays revealed acts as multivalent ligand for bacterial type 1 pilus adhesin, presenting specific epitopes on regularly spaced Imaging...
Multivalent carbohydrate–lectin interactions at host–pathogen interfaces play a crucial role in the establishment of infections. Although competitive antagonists that prevent pathogen adhesion are promising antimicrobial drugs, molecular mechanisms underlying these complex processes still poorly understood. Here, we characterize between fimbrial adhesin FimH from uropathogenic Escherichia coli strains and its natural high-mannose type N-glycan binding epitopes on uroepithelial glycoproteins....
We demonstrate how two copper atoms are brought together to build a metal center in an essential enzyme for cellular respiration.
Three highly pathogenic β-coronaviruses crossed the animal-to-human species barrier in past two decades: SARS-CoV, MERS-CoV and SARS-CoV-2. SARS-CoV-2 has infected more than 64 million people worldwide, claimed over 1.4 lives is responsible for ongoing COVID-19 pandemic. We isolated a monoclonal antibody, termed B6, cross-reacting with eight β-coronavirus spike glycoproteins, including all five human-infecting β-coronaviruses, broadly inhibiting entry of pseudotyped viruses from coronavirus...
The repeated spillovers of β-coronaviruses in humans along with the rapid emergence SARS-CoV-2 escape variants highlight need to develop broad coronavirus therapeutics and vaccines. Five monoclonal antibodies (mAbs) were isolated from COVID-19 convalescent individuals found cross-react multiple β-coronavirus spike (S) glycoproteins by targeting stem helix. One these mAbs, S2P6, cross-reacts more than twenty human animal S broadly neutralizes pseudotyped viruses sarbecovirus, merbecovirus...