Local protein instability predictive of helper T-cell epitopes.
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.
Landry
S J
SJ
Dept of Biochemistry, Tulane University School of Medicine, New Orleans, LA 70112, USA. landry@mailhost.tcs.tulane.edu
D018360:Crystallography, X-Ray; D018984:Epitopes, T-Lymphocyte / Q000737:chemistry*; D016056:Immunodominant Epitopes / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D010449:Peptide Mapping; D011487:Protein Conformation; D006377:T-Lymphocytes, Helper-Inducer / Q000737:chemistry* / Q000276:immunology
D018984:Epitopes, T-Lymphocyte; D016056:Immunodominant Epitopes