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Sci Rep ; 5: 12411, 2015 Jul 23.
Artigo em Inglês | MEDLINE | ID: mdl-26202883

RESUMO

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


Assuntos
Reações Antígeno-Anticorpo/imunologia , Imunidade Inata/imunologia , Receptor ErbB-2/química , Receptor ErbB-2/imunologia , Sequência de Aminoácidos , Animais , Sítios de Ligação , Humanos , Camundongos , Dados de Sequência Molecular , Ligação Proteica , Relação Estrutura-Atividade
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