Epitope mapping of mouse monoclonal antibody EP-5C7 which neutralizes both human E- and P-selectin

Biochemical and Biophysical Research Communications
N TsurushitaE L Berg

Abstract

The epitope of mouse monoclonal antibody (mAb) EP-5C7, which binds to and blocks both human E- and P-selectin, was mapped onto the protein structure of E-selectin. Analyses with E- and L-selectin chimeric proteins and randomly mutagenized E-selectins demonstrated that the EP-5C7 epitope consists of the amino acid residues at positions 21, 22, 23, 119 and 120 of E-selectin. The binding of three neutralizing anti-E-selectin mAb's (E-1E4, H18/7 and CL2), whose epitopes were found to overlap with the E-selectin binding site for carbohydrate ligands, was not affected by the amino acid substitutions at these five positions. Inspection of the three-dimensional structure of E-selectin indicated that the EP-5C7 epitope is located near the junction between the lectin and EGF-like domains. The ligand binding site was distant from the EP-5C7 epitope, suggesting that the amino acid residues in the EP-5C7 epitope play an important role other than ligand binding in selectin-mediated cell adhesion.

References

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Citations

Feb 15, 2008·Annals of Biomedical Engineering·G HaririD Hallahan
Jun 23, 2009·Cellular Immunology·Martin BerglundOlof H Hultgren
Aug 19, 2006·Biotechnology and Bioengineering·Anthony Sang Won HamMichael B Lawrence
Jan 17, 2003·American Journal of Physiology. Cell Physiology·Owen J T McCartyKonstantinos Konstantopoulos
Jan 17, 2014·The Journal of Immunology : Official Journal of the American Association of Immunologists·Sebastian B RieseKonrad Buscher

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