Structural coincidence of alpha PDGFR epitopes binding to platelet-derived growth factor-AA and a potent neutralizing monoclonal antibody.

摘要: We have generated two groups of deletion mutants the alpha PDGFR and one group chimeras between beta to further investigate structural requirements for binding platelet-derived growth factor (PDGF)-AA a monoclonal antibody against (designated as mAb-alpha R1). The R1 has recently been reported block high affinity PDGF-AA PDGFR. first were carboxyl-terminal encoding immunoglobulin (Ig)-like domains (alpha R1-216), four Ig-like R1-415), or all five R1-530) Since these lacked transmembrane domains, their expression in NIH/3T3 cells resulted secretion truncated PDGFRs. Using conditioned medium from transfectants, we showed that was able immunoprecipitate each secreted form PDGFRs, suggesting epitope recognized by is located within 1 2 Furthermore, exhibited detectable R1-415 R1-530 but failed interact with R1-216, are not sufficient binding. second internal lacking loop R delta 49-100), 150-189), 3 235-290), part loops 4 5 375-450). transfected into 32D which lack both bound expressing 375-450 other three mutants, region required should be In addition, 235-290 bind 49-100 150-189.(ABSTRACT TRUNCATED AT 400 WORDS)