Cardenas, Amaris (Criss)
Gonorrhea, caused by the bacterium Neisseria gonorrhoeae (Gc), is characterized by the influx of neutrophils to sites of infection. Gc has many nonredundant mechanisms to manipulate neutrophil activation and resist killing by neutrophil antimicrobial components. One of these is variation of Gc lipooligosaccharide (LOS). In neutrophil-rich male urethral exudates, the oligosaccharide of LOS becomes modified by sialic acid in a process known as sialylation. Gc incorporates host derive sialic acid into LOS using LOS sialyltransferase (Lst). While sialylation by Lst has been shown to be protective for Gc in different models of infection, how it affects the ability of Gc to survive in association with neutrophils is unclear. I am currently testing how LOS sialylation protects Gc from killing by primary human neutrophils by increasing resistance to antimicrobial components and limiting their production and/or release. I am also testing the possibility that neutrophils modify the sialylation state of Gc by providing sialic acid as substrate and through their sialyltransferase and sialidase activities.