Congratulations to the TSS Spring 2026 Symposium poster prize winners!

Francis Santoriello (Princeton University), Junwon Yang (NJIT), and Alexandra Kwasnik (Rutgers -- New Brunswick) were honored as poster prize winners at the Theobald Smith Society’s Spring 2026 Symposium.

Francis Santoriello, a postdoctoral researcher in Dr. Bonnie Bassler’s lab at Princeton University, presented “A family of linear plasmid phages that detect a conserved quorum-sensing autoinducer is dispersed across multiple bacterial species.” His work focuses on temperate phages, which alternate between lysogeny, a maintenance state within the bacterial host, and lytic replication, in which the host is killed and new phage particles are released. While many temperate phages trigger lysis in response to host cell stress, VP882-like phages can instead use quorum-sensing signals to induce lysis at high host cell density. By mining sequence databases, Santoriello identified VP882-like phages across multiple bacterial species from clinical and environmental sources worldwide. His findings show that these phages can detect the conserved autoinducer DPO and respond by activating lytic replication, suggesting that ϕVP882 belongs to a globally dispersed family of quorum-sensing-responsive temperate phages.

Junwon Yang, a postdoctoral researcher in Dr. Mengyan Li’s lab at NJIT, presented “Divergent catalytic strategies of group-6 propane monooxygenases in propane-stimulated 1,4-dioxane biodegradation.” His research examines group-6 propane monooxygenases (PRMs), enzymes that catalyze the initial oxidation of 1,4-dioxane, a widespread contaminant of emerging concern. Because PRM expression can be induced by propane, PRM-containing microorganisms are promising for propane-based biostimulation strategies. Yang compared representative PRMs from three phylogenetic clusters and found substantial differences in substrate affinity, catalytic capacity, resistance to chlorinated solvent inhibition, and activity toward dioxane and propane. His results link enzyme kinetics to ecological strategy and provide a mechanistic basis for selecting microbial populations and optimizing conditions for dioxane-contaminated environmental remediation.

Alexandra Kwasnik, a master’s student in Dr. Zachery Lonergan’s lab at Rutgers -- New Brunswick, presented “Lon protease supports aconitase activity in response to nitric oxide stress in Pseudomonas aeruginosa.” Her work investigates how P. aeruginosa, an opportunistic bacterial pathogen, adapts to nitric oxide stress during infection. Kwasnik studied the Lon AAA+ protease, an ATP-dependent enzyme involved in proteome homeostasis, and found that deletion of lon caused a significant growth defect under nitric oxide stress. Transcriptional profiling and biochemical assays showed that Lon influences iron-sulfur cluster-related processes and supports aconitase activity during nitrosative stress. Her findings suggest that Lon contributes to P. aeruginosa nitric oxide resistance and that targeting Lon may enhance nitric oxide toxicity against the pathogen.