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Two Human Neonatal IgM Antibodies Encoded by Different Variable-Region Genes Bind the Same Linear Peptide: Evidence for a Stereotyped Repertoire of Epitope Recognition¹

Bradley T. Messmer^*, James J. Sullivan^*, Nicholas Chiorazzi, Toby C. Rodman^* and David S. Thaler^2,*

^* Sackler Laboratory for Molecular Genetics and Informatics, The Rockefeller University, New York, NY, 10021; and Department of Rheumatology and Clinical Immunology, North Shore University Hospital, New York University School of Medicine, Manhasset, NY 11030

Two monoclonal IgM Abs have been produced from lymphocytes isolated from two human umbilical cord bloods. These mAbs recognize a conformational epitope present in a CNBr digestion fraction of lactoferrin. Linear epitopes recognized by each mAb were selected from several phage display peptide libraries. In each case, phages displaying a peptide with a motif defined by [WF],G,[EQS],N were recovered. Phages displaying that motif bound equally well to either mAb but did not bind to control IgM. A peptide bearing this motif competed with the phage-displayed peptides for binding to either mAb. The same peptide also competes with a component of the CNBr digestion fraction of lactoferrin for Ab binding in ELISA. The Abs use different families of V_H, J_H, and V_K gene cassettes but use the same J_K cassette. All segments are virtually identical to their germline gene counterparts. This work provides further evidence that certain innate specificities are stereotyped among individuals.

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