In meso crystal structure and docking simulations suggest an alternative proteoglycan binding site in the OpcA outer membrane adhesin

OpcA is an integral outer membrane adhesin protein from Neisseria meningitidis , the causative agent of meningococcal meningitis and septicemia. It binds to sialic acid (SA)‐containing polysaccharides on the surface of epithelial cells. The crystal structure of OpcA showed that the protein adopts a 10‐stranded β‐barrel structure, with five extensive loop regions on the extracellular side of the membrane. These form a crevice structure, lined...