Identification and characterization of fully human anti-CD22 monoclonal antibodies

MAbs. 2009 May-Jun;1(3):297-303. doi: 10.4161/mabs.1.3.8113. Epub 2009 May 5.

Abstract

CD22 is a member of the B cell receptor family and is implicated in B cell function and development. It is expressed on multiple forms of B cell lymphoma and is an attractive cancer therapeutic target. We report here the identification of two fully human anti-CD22 antibodies using phage display methodology. Both antibodies exhibit specific binding to cell surface-associated CD22 in multiple B cell lines. Through ELISA using mammalian cell-expressed sub-domains of CD22 as binding antigen, we mapped the binding epitopes of the newly identified CD22 antibodies to be within the Ig-like domains 5 to 7 of CD22. Their epitopes do not overlap with those of several therapeutic antibodies currently in preclinical or clinical development. These antibodies have potential as cancer therapeutic candidates and research reagents.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, N.I.H., Intramural

MeSH terms

  • Antibodies, Monoclonal / immunology
  • Antibodies, Monoclonal / isolation & purification
  • Antibodies, Monoclonal / metabolism*
  • Antibody Affinity
  • B-Lymphocytes / immunology
  • B-Lymphocytes / metabolism*
  • Epitope Mapping
  • Humans
  • Immunotherapy*
  • Lymphoma, B-Cell / drug therapy*
  • Lymphoma, B-Cell / immunology
  • Peptide Library
  • Protein Binding
  • Sialic Acid Binding Ig-like Lectin 2 / immunology*

Substances

  • Antibodies, Monoclonal
  • Peptide Library
  • Sialic Acid Binding Ig-like Lectin 2