A5009303475- Hemoglobin structure and function
- Clostridium difficile and Clostridium perfringens research
- Antimicrobial Resistance in Staphylococcus
- Streptococcal Infections and Treatments
- Force Microscopy Techniques and Applications
- Protein Structure and Dynamics
- Bacterial Genetics and Biotechnology
- Enzyme Structure and Function
- Bacterial biofilms and quorum sensing
- Lipid Membrane Structure and Behavior
- Protein Interaction Studies and Fluorescence Analysis
- Advanced Electron Microscopy Techniques and Applications
- RNA modifications and cancer
- Folate and B Vitamins Research
- Antibiotic Resistance in Bacteria
- Neonatal Health and Biochemistry
- Biochemical and Structural Characterization
University of Parma
2017-2025
Iron-regulated surface determinant B (IsdB) is a protein of Staphylococcus aureus that plays essential roles in host cell invasion by mediating both bacterial adhesion and hemic iron acquisition. Single-molecule experiments have recently revealed the binding IsdB to vitronectin integrins dramatically strengthened under mechanical stress conditions, promoting staphylococcal adhesion. Here we conducted atomic force spectroscopy (AFS) measurements interaction between hemoglobin (Hb), its...
Among multidrug-resistant bacteria, methicillin-resistant Staphylococcus aureus is emerging as one of the most threatening pathogens. S. exploits different mechanisms for its iron supply, but preferred acquisition organic through expression hemoglobin (Hb) receptors. One these, IsdB, belonging to Isd (Iron-Regulated Surface Determinant) system, was shown be essential bacterial growth and virulence. Therefore, interaction IsdB with Hb represents a promising target rational design new class...
Iron surface determinant B (IsdB), a Staphylococcus aureus (SA) protein involved in both heme iron acquisition from host hemoglobin (Hb) and bacterial adhesion, is proven virulence factor that can be targeted for the design of antibacterial molecules or vaccines. Recent single-molecule experiments on IsdB interaction with cell adhesion factors revealed an increase complex lifetime upon applying stronger force (catch bond); this was suggested to favor invasion under shear stress. An increased...
Siderophore production, along with heme scavenging by hemophores, is one of the main mechanisms exploited bacteria to achieve an adequate iron supply. Staphylococcus aureus produces two siderophores, staphyloferrin A (SA) and B (SB), latter produced only most invasive, coagulase-positive S. strains. Along seven steps SB biosynthetic pathway, N-(2-amino-2-carboxyethyl)-l-glutamate synthase (SbnA) catalyzes crucial formation intermediate from O-phospho-L-serine glutamate. Our functional...
In bacteria and plants, serine acetyltransferase (CysE) O-acetylserine sulfhydrylase-A sulfhydrylase (CysK) collaborate to synthesize l-Cys from l-Ser. CysE CysK bind one another with high affinity form the cysteine synthase complex (CSC). We demonstrate that bacterial is activated when bound CysK. activation results release of substrate inhibition, Ki for l-Ser increasing 4 mm free 16 CSC. Feedback inhibition by also relieved in These findings suggest active site allosterically altered...
Significance During infection, the human pathogen Staphylococcus aureus expresses a surface-exposed receptor, Iron surface determinant B (IsdB), that captures free hemoglobin (Hb) and removes heme to retrieve iron, an essential nutrient for bacterial proliferation inside host. Using single-particle cryo-electron microscopy, we solved structure of two complexes between Hb IsdB represent snapshots initial interaction, where is still bound Hb, final complex after completion extraction. The...
Human hemoglobin (Hb) is the preferred iron source of Staphylococcus aureus. This pathogenic bacterium exploits a sophisticated protein machinery called Iron-regulated surface determinant (Isd) system to bind Hb, extract and internalize heme finally degrade it complete acquisition. IsdB, exposed Hb receptor, proven virulence factor S. aureus inhibition its interaction with can be pursued as strategy develop new classes antimicrobials. To identify small molecules able disrupt IsdB:Hb...
Abstract Human hemoglobin (Hb) is the preferred iron source of Staphylococcus aureus . This pathogenic bacterium exploits a sophisticated protein machinery called Iron-regulated surface determinant (Isd) system to bind Hb, extract and internalize heme, finally degrade it complete acquisition. IsdB, exposed Hb receptor, proven virulence factor S. inhibition its interaction with can be pursued as strategy develop new classes antimicrobials. To identify small molecules able disrupt IsdB:Hb...
<title>Abstract</title> Iron surface determinant B (IsdB), a <italic>Staphylococcus aureus</italic> (SA) protein involved in both heme iron acquisition from host hemoglobin (Hb) and bacterial adhesion, is proven virulence factor that can be targeted for the design of antibacterial molecules or vaccines. Recent single-molecule experiments on IsdB interaction with cell adhesion factors revealed an increase complex lifetime upon applying stronger force (catch bond); this was suggested to favor...
Abstract Infections caused by Staphylococcus aureus depend on its ability to acquire nutrients. One essential nutrient is iron, which obtained from the heme of human host hemoglobin (Hb) through a protein machinery called Iron-regulated Surface Determinant (Isd). IsdB in charge extraction Hb, first step chain events leading iron transfer bacterium cell interior. In order elucidate molecular formation initial IsdB:Hb complex extraction, we have performed time-resolved X-ray solution...