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Tsibouris, C.

Publications and source records attributed to Tsibouris, C..

2 recordsLinked to original sources

Sparse input representations explain odor discrimination in complex, concentration-varying mixtures

In natural environments, animals must detect behaviorally relevant odors despite variability in both odor mixture composition and stimulus intensity. Although mice can identify salient odors embedded in complex mixtures, how target concentration and background complexity jointly constrain discrimination remains unclear. We trained mice in a two-alternative forced choice task to identify target odors embedded in mixtures containing up to 16 background components. After performance stabilized, we systematically varied target odor concentration. Discrimination accuracy declined with decreasing target concentration but showed little additional dependence on background complexity. Using a biophysically grounded model of olfactory bulb glomerular responses, we show that linear decoding reproduces behavioral performance when intrinsic neural noise dominates over background-driven variability. Manifold capacity analysis revealed that neural representations remain efficiently structured for odor discrimination despite variation in background complexity. These results define a noise-limited regime of olfactory discrimination in which target detectability is primarily constrained by neural sensitivity rather than background interference.

neuroscience↗

The structure of NAD+ consuming protein Acinetobacter baumannii TIR domain shows unique kinetics and conformations.

Toll-like and Interleukin-1/18 receptor resistance (TIR) domain-containing proteins function as important signaling and immune regulatory molecules. TIR domain-containing proteins identified in eukaryotic and prokaryotic species also exhibit NAD+ hydrolase activity in select bacteria, plants, and mammalian cells. We report the crystal structure of the Acinetobacter baumannii TIR domain protein (AbTir-TIR) with confirmed NAD+ hydrolysis and map the conformational effects of its interaction with NAD+ using HDX-MS. NAD+ results in mild decreases in deuterium uptake at the dimeric interface. In addition, AbTir-TIR exhibits EX1 kinetics indicative of large cooperative conformational changes which are slowed down upon substrate binding. Additionally, we have developed label-free imaging using 2pFLIM which shows differences in bacteria expressing native and mutant NAD+ hydrolase-inactivated AbTir-TIREA protein. Our observations are consistent with substrate-induced conformational changes reported in other TIR model systems with NAD+ hydrolase activity. These studies provide further insight into bacterial TIR protein mechanisms and their varying roles in biology.

biochemistry↗