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A Linear Region of a Monoclonal Antibody Conformational Epitope Mapped on p185HER2 Oncoprotein by Rosaria Orlandi; Cristina Formantici; Sylvie Ménard; Cinda M. Boyer; Jon R. Wiener; Maria Colnaghi is a scholarly article available to read on EtoBox.

What is A Linear Region of a Monoclonal Antibody Conformational Epitope Mapped on p185HER2 Oncoprotein about?

## Analysis of epitopes recognized by therapeutic monoclonal antibodies (mAb) is critical in clinical applica tions and in structure/function studies of target antigen. mAb MGr6 recognizes the extracellular domain of the p185 HER2 oncoprotein and is a promising candidate for cancer immunodiagnosis and immunotherapy. Thus, epitope location and structure on p185 HER2 need to be investigated. The use of MGr6-selected phagedisplayed peptides for epitope analysis served to dissect the MGr6 epitope into at least two subregions, mimicked by CHSDC-and (L)P-(L)K(L) phage displayed peptides, respectively. Comparison of amino acid sequences of CHSDC peptides with the p185 HER2 protein sequence and analysis of MGr6 reactivity with p185 HER2 deletion mutants identified the linear subregion CCHEQCAAG of the MGr6 epitope, corresponding to amino acids 235-243 of the p185 HER2 protein. This continuous subregion is part of a larger conf ormational epitope, and other amino acids, including a proline, a lysine and leucine residues contained in (L)P-(L)K(L) phage-displayed peptides appear to contribute to the formation of the MGr6 epitope surface.

Author

Rosaria Orlandi; Cristina Formantici; Sylvie Ménard; Cinda M. Boyer; Jon R. Wiener; Maria Colnaghi

Publisher

Walter de Gruyter GmbH

Published

1997

Language

EN