Landry S J
Dept of Biochemistry, Tulane University School of Medicine, New Orleans, LA 70112, USA.
Immunol Today. 1997 Nov;18(11):527-32. doi: 10.1016/s0167-5699(97)01152-3.
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.
尽管肽与主要组织相容性复合体（MHC）II类的结合以及T细胞识别水平上的选择性可能部分解释免疫显性模式，但很明显，差异抗原加工也发挥着强大作用。在此，山姆·兰德里将免疫显性表位与通过氢氘交换核磁共振（NMR）确定的附近结构不稳定片段相关联，并表明表位呈递是由不稳定位点的优先蛋白水解切割所指导的。
