Group 1 - Immutep Limited has published findings in Science Immunology that clarify how human LAG-3 binds to its main ligand MHC Class II, providing a foundation for developing blocking LAG-3 therapeutics, including its anti-LAG-3 small molecule program [1][3] - The study reveals the crystal structure of a human LAG-3/HLA-II complex, which is significant for future therapeutic developments targeting LAG-3 [1][3] - Eftilagimod alfa (efti) has been shown to preferentially bind to a subset of MHC Class II molecules on antigen-presenting cells, leading to their activation [1][3] Group 2 - The research was conducted under the supervision of Professor Jamie Rossjohn at Monash University's Biomedicine Discovery Institute, highlighting the importance of industry-academia collaborations in advancing LAG-3 research [2] - The findings contribute to a deeper understanding of the LAG-3 immune control mechanism, which is a clinically validated target of interest across various sectors [2][3] - The study emphasizes the unique action of efti as an MHC-II agonist, which preferentially binds to specific MHC-II molecules clustered in lipid raft microdomains on antigen-presenting cells [3]
Immutep and Monash University Announce First Publication Detailing How Human LAG-3 Binds to MHC Class II