Abstract
Human pathogens Neisseria gonorrhoeae and N. meningitides are unique in their utilization of opacity-associated (Opa) proteins to mediate bacterial uptake into non-phagocytic cells. Opa proteins engage either heparan sulfate proteoglycan (HSPG) receptors or carcinoembryonic antigen-related cellular adhesion molecules (CEACAMs) to hijack host cellular mechanisms, which induces bacterial engulfment. The Opa family of proteins are eight stranded β-barrels with four extracellular loops. Regions in loops two and three contain hypervariable sequences among Opa variants and dictate receptor specificity. We aim to investigate the structural determinants of Opa-receptor interactions. Overall loop dynamics of Opa60, a CEACAM-binding Opa variant, were determined using CW-EPR and combined with the limited NMR relaxation data. Results indicate that the loops and hypervariable regions are highly mobile on the nanosecond timescale. Initial DEER experiments measured distances between Opa60 and CEACAM in the complex and preliminary models consistent with these distances will be presented. Determining the interactions between Opa and CEACAM will provide an understanding of the molecular interactions that mediate the entry of a foreign body into non-phagocytic cells.
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