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Local protein instability predictive of helper T-cell epitopes
1Dept of Biochemistry, Tulane University School of Medicine, New Orleans, LA 70112, USA. landry@mailhost.tcs.tulane.edu
Although selectivity at the levels of peptide binding to major histocompatibility complex (MHC) class II and recognition by T cells may partially account for immunodominance patterns, it is clear that differential antigen processing also exerts a strong effect. Here, Sam Landry correlates immunodominant epitopes with nearby structurally unstable segments, as identified by hydrogen-deuterium exchange nuclear magnetic resonance (NMR), and suggests that epitope presentation is directed by preferential proteolytic cleavage at the unstable sites.
Although selectivity at the levels of peptide binding to major histocompatibility complex (MHC) class II and recognition by T cells may partially account for immunodominance patterns, it is clear that differential antigen processing also exerts a strong effect. Here, Sam Landry correlates immunodominant epitopes with nearby structurally unstable segments, as identified by hydrogen-deuterium exchange nuclear magnetic resonance (NMR), and suggests that epitope presentation is directed by preferential proteolytic cleavage at the unstable sites.