A novel synthetic naive human antibody library allows the isolation of antibodies against a new epitope of oncofetal fibronectin.

ABSTRACT: Human monoclonal antibodies (mAbs) can routinely be isolated from phage display libraries against virtually any protein available in sufficient purity and quantity, but library design can influence epitope coverage on the target antigen. Here we describe the construction of a novel synthetic human antibody phage display library that incorporates hydrophilic or charged residues at position 52 of the CDR2 loop of the variable heavy chain domain, instead of the serine residue found in the corresponding germline gene. The novel library was used to isolate human mAbs to various antigens, including the alternatively-spliced EDA domain of fibronectin, a marker of tumor angiogenesis. In particular, the mAb 2H7 was proven to bind to a novel epitope on EDA, which does not overlap with the one recogn

SUBMITTER: Villa A 

PROVIDER: S-EPMC3149707 | biostudies-literature | 2011 May-Jun

REPOSITORIES: biostudies-literature