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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.

Original publication




Journal article


Biochem J

Publication Date



293 ( Pt 3)


633 - 640


Amino Acid Sequence, Antibodies, Antigens, CD, Antigens, Neoplasm, Binding Sites, Antibody, CD52 Antigen, Complement System Proteins, Epitopes, Glycoproteins, Glycosylphosphatidylinositols, Hydrolysis, Molecular Sequence Data, Pronase, Protein Conformation, Sequence Homology, Amino Acid