Structure of the CAMPATH-1 antigen, a glycosylphosphatidylinositol-anchored glycoprotein which is an exceptionally good target for complement lysis

Author:

Xia M Q1,Hale G1,Lifely M R2,Ferguson M A J3,Campbell D3,Packman L4,Waldmann H1

Affiliation:

1. Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, U.K.

2. The Wellcome Research Laboratories, Langley Court, Beckenham BR3 3BS, U.K.

3. Department of Biochemistry, University of Dundee, Dundee DDl 4HN, U.K.

4. Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 lQW, U.K.

Abstract

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.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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