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CAMPATH-1 antibodies recognize a unique molecule on human lymphocytes and are unusually efficient at causing cell lysis with homologous complement. They have been successfully used for lymphocyte depletion in vivo in a variety of diseases. We find that the antigen is a very small glycosylphosphatidylinositol (GPI)-anchored glycoprotein with a mature peptide comprising only 12 amino acids. It can be separated into two distinct antigenic fractions which differ in their susceptibility to phosphatidylinositol-specific phospholipase C. There is one N-linked glycosylation site, but no evidence for O-glycosylation despite the presence of several serine and threonine residues. The antibodies were found to bind, albeit with a generally reduced affinity, to a proteolytic fragment containing the C-terminal tripeptide and the GPI anchor. We postulate that one of the reasons why the CAMPATH-1 antibodies are so good for cell lysis is because they bind to an epitope which is likely to be very close to the lipid bilayer.

Type

Journal article

Journal

Biochem J

Publication Date

01/08/1993

Volume

293 ( Pt 3)

Pages

633 - 640

Keywords

Amino Acid Sequence, Antibodies, Antigens, CD, Antigens, Neoplasm, Binding Sites, Antibody, Complement System Proteins, Epitopes, Glycoproteins, Glycosylphosphatidylinositols, Hydrolysis, Molecular Sequence Data, Pronase, Protein Conformation, Sequence Homology, Amino Acid