Ravi Yadav
Structural and functional studies of lactoferrin binding proteins from Neisseria
Contact Info:Training Group(s):
Biomolecular Structure and Biophysics
Current Research Interests:
Neisseria are exclusive human pathogens causing meningitis, septicemia, bacteremia and gonorrhea diseases. During pathogenesis, Neisseria bacterium employs TonB-dependent surface receptors to obtain iron from iron-containing host glycoproteins mainly transferrin, lactoferrin, and hemoglobin. Lactoferrin binding protein (Lbp) system hijacks lactoferrin and potentially extracts iron from it to evade the host nutritional immunity. Lbp system is composed of two components: lactoferrin binding protein A (LbpA), an outer membrane protein, and lactoferrin binding protein B (LbpB), an extracellular surface anchored lipoprotein. Additionally, LbpB provides protection against host and synthetic cationic antimicrobial peptides. However, the molecular mechanisms of Lbp system’s functions are unknown due to the absence of structural and biochemical studies. In our work, we employ several structural biology techniques such as SAXS, X-ray crystallography, and CryoEM along with biochemical and biophysical techniques to gain insight into the structural basis of Lbp system's iron import and antimicrobial peptide protection function.- Student Profile
