Structure of a patient-derived antibody in complex with allergen reveals simultaneous conventional and superantigen-like recognition.

ABSTRACT: Antibodies classically bind antigens via their complementarity-determining regions, but an alternative mode of interaction involving V-domain framework regions has been observed for some B cell "superantigens." We report the crystal structure of an antibody employing both modes of interaction simultaneously and binding two antigen molecules. This human antibody from an allergic individual binds to the grass pollen allergen Phl p 7. Not only are two allergen molecules bound to each antibody fragment (Fab) but also each allergen molecule is bound by two Fabs: One epitope is recognized classically, the other in a superantigen-like manner. A single allergen molecule thus cross-links two identical Fabs, contrary to the one-antibody-one-epitope dogma, which dictates that a dimeric allerge

SUBMITTER: Mitropoulou AN 

PROVIDER: S-EPMC6140506 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature