Predominant structural configuration of natural antibody repertoires enables potent antibody responses against protein antigens.

摘要: Humoral immunity against diverse pathogens is rapidly elicited from natural antibody repertoires of limited complexity. But the organizing principles underlying that facilitate this are not well-understood. We used HER2 as a model immunogen and reverse-engineered murine response through constructing an artificial library encoded with rudimentary sequence structural characteristics learned high throughput sequencing variable domains. Antibodies selected in vitro phage-displayed synthetic bound to affinity specificities, which reproduced specificities responses. conclude shaped allow functional antibodies be efficiently, within complexity limit individual repertoire, bind protein antigens specificity affinity. Phage-displayed libraries, conjunction high-throughput sequencing, can thus designed replicate responses generate novel antigens.