Poster Session II
Project Type
Poster
Project Funding and Affiliations
Northern Rockies Center For Hydrodynamics, S10OD036366 (PI: Demeler) University of Montana VPR funds, 2025 CBSD Phase III Pilot Award and CTM Undergraduate Internship Program,
Faculty Mentor’s Full Name
Asia Riel
Faculty Mentor’s Department
Chemistry/Biochemistry
Additional Mentor
Borries Demeler
Abstract / Artist's Statement
Macrophage Inducible C-Type Lectin receptor (Mincle) is a pattern recognition receptor on myeloid cells, which modulates the immune system by recognizing small molecules that activate the signaling cascade to release inflammatory and immune response mediators. [1] C-type lectin receptors have been known to form higher order structures to produce elevated, coordinated immune responses. However, this has not been fully established experimentally with Mincle and known ligands. [2,3] Stabilized by an extracellular disulfide bond, Mincle in mammalian cells can exist as a preformed dimer. [3] This suggests that activation-induced oligomerization in Mincle could be a ligand-specifying factor in the type and intensity of immune response.
The Chemistry team within the Center for Translational Medicine’s Adjuvant Research Team has identified and synthesized multiple ligands with varying cytokine profiles. Using Sedimentation Analytical Ultracentrifugation, we seek to probe the dimerization of extracellular domain Mincle in the presence of these ligands. This data will elucidate potential mechanisms of Mincle activation and help guide future ligand formation.
Category
Life Sciences
Ligand Induced Mincle Dimerization for Informing Tuberculosis Adjuvant Formulation
UC South Ballroom
Macrophage Inducible C-Type Lectin receptor (Mincle) is a pattern recognition receptor on myeloid cells, which modulates the immune system by recognizing small molecules that activate the signaling cascade to release inflammatory and immune response mediators. [1] C-type lectin receptors have been known to form higher order structures to produce elevated, coordinated immune responses. However, this has not been fully established experimentally with Mincle and known ligands. [2,3] Stabilized by an extracellular disulfide bond, Mincle in mammalian cells can exist as a preformed dimer. [3] This suggests that activation-induced oligomerization in Mincle could be a ligand-specifying factor in the type and intensity of immune response.
The Chemistry team within the Center for Translational Medicine’s Adjuvant Research Team has identified and synthesized multiple ligands with varying cytokine profiles. Using Sedimentation Analytical Ultracentrifugation, we seek to probe the dimerization of extracellular domain Mincle in the presence of these ligands. This data will elucidate potential mechanisms of Mincle activation and help guide future ligand formation.