Development of a non-biased, high-throughput ELISA for the rapid evaluation of immunogenicity and cross-reactivity.

ABSTRACT: Traditional ELISA-based protein analysis has been predicated on the assumption that proteins bind randomly to the solid surface of the ELISA plate polymer (polystyrene or polyvinyl chloride). Random adherence to the plate ensures equal access to all faces of the protein, an important consideration when evaluating immunogenicity of polyclonal serum samples as well as when examining the cross-reactivity of immune serum against different antigenic variants of a protein. In this study we demonstrate that the soluble form of the surface lipoprotein transferrin binding protein B (TbpB) from three different bacterial pathogens (Neisseria meningitidis, Actinobacillus pleuropneumoniae, and Mannheimia haemolytica) bind the ELISA plate in a manner that consistently obscures the transferrin binding fa

SUBMITTER: Fegan JE 

PROVIDER: S-EPMC8107143 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature