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Epitope identification for human neutrophil flavocytochrome b monoclonals 48 and 449

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Abstract: Flavocytochrome b558 (Cyt b) is important in generating superoxide and other toxic oxygen species involved in inflammation and host defense. Monoclonal antibodies (mAbs) 48 and 449 bind the gp91phox and p22phox subunits of Cyt b, respectively, and have been used to characterize this enzyme complex. Until now, data were unavailable to predict which regions of the protein were bound by each antibody. Random sequence phage‐display peptide library analysis of each antibody was used to select peptides that mimic the sequence of each protein epitope. Phage sequences selected by mAb 48 presented the consensus peptide sequence, DRDVXTGL, which closely resembles 498EKDVITGL505 of gp91phox. Phage selected by mAb 449 contributed the consensus WRWPGPQVL, resembling in part 182GPQV185 of p22phox. Confirmation for this second epitope was provided by peptide walking analysis. Identifying the protein residues bound by these antibodies makes each a more informative probe for Cyt b analysis.
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Keywords: epitope mapping; flavocytochrome b; monoclonal antibodies; neutrophil; phage display

Document Type: Research Article

Affiliations: 1: Department of Microbiology, Montana State University, Bozeman, Montana, USA, 2: Julius Friedrich Cohnheim‐Minerva Center for Phagocyte Research, Department of Human Microbiology, Sackler School of Medicine, Tel Aviv University, Tel Aviv, Israel, and 3: Central Laboratory of the Netherlands Blood Transfusion Service and Laboratory for Experimental and Clinical Immunology, Academic Medical Center, University of Amsterdam, The Netherlands

Publication date: December 1, 2000

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