Identification and characterization of fully human anti-CD22 monoclonal antibodies.
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.
Xiao
Xiaodong
X
Protein Interactions Group, CCRNP, NCI-Frederick, NIH, Frederick, MD 21702-1201, USA. xiaox@ncifcrf.gov
Ho
Mitchell
M
Zhu
Zhongyu
Z
Pastan
Ira
I
Dimitrov
Dimiter S
DS
D000911:Antibodies, Monoclonal / Q000276:immunology / Q000302:isolation & purification / Q000378:metabolism*; D000915:Antibody Affinity; D001402:B-Lymphocytes / Q000276:immunology / Q000378:metabolism*; D018604:Epitope Mapping; D006801:Humans; D007167:Immunotherapy; D016393:Lymphoma, B-Cell / Q000188:drug therapy* / Q000276:immunology; D019151:Peptide Library; D011485:Protein Binding; D051918:Sialic Acid Binding Ig-like Lectin 2 / Q000276:immunology*
D000911:Antibodies, Monoclonal; D019151:Peptide Library; D051918:Sialic Acid Binding Ig-like Lectin 2