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Epitope Mapping of Mouse Monoclonal Antibody EP-5C7 Which Neutralizes Both Human E- And P-selectin

N Tsurushita, H Fu, J Melrose, E L Berg

Biochem Biophys Res Commun. 1998 Jan 6;242(1):197-201.

PMID: 9439635

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.

Chemicals Related in the Paper:

Catalog Number Product Name Structure CAS Number Price
IAR42414173 Anti-E-Selectin (CD62E) antibody, Mouse monoclonal Anti-E-Selectin (CD62E) antibody, Mouse monoclonal Price
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