Gonorrhea is one of the sexually transmitted infections (STI) that are among the most common acute conditions in the world. N. gonorrhoeae, a species of Gram-negative diplococci bacteria, is the causative agent of gonorrhea. Due to the spread of antimicrobial resistance (AMR) isolates globally, gonorrhea has become an intractable problem. Available antibiotics are not able to effectively treat all infections and there is also no vaccine available. Glycans on the surface of the cells are commonly targeted by many pathogens, including N. gonorrhoeae. Our lab showed that N. gonorrhoeae bind to several glycans with different structural and functional classes, especially glycosaminoglycans (GAGs) and mannosyl glycans. 17 mannose-binding proteins of N. gonorrhoeae were isolated and identified by liquid chromatography-mass spectrometry (LC-MS) analysis. The principal focus of my research is to characterize (detect and qualify) the interaction between mannose-binding gonococcal proteins and mannosyl glycans by surface plasmon resonance (SPR) analysis. The specific role of these mannose-binding proteins will be further investigated by performing in vitro N. gonorrhoeae adherence assays with human cervical and male urethral cells in the presence/absence of mannose mimics.