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Tsurushita, N. et al.

Tsurushita, Fu, Melrose, Berg,

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

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.[1]

References

Epitope mapping of mouse monoclonal antibody EP-5C7 which neutralizes both human E- and P-selectin. Tsurushita, N., Fu, H., Melrose, J., Berg, E.L. Biochem. Biophys. Res. Commun. (1998) [Pubmed]

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