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Glycosylation of recombinant antibody therapeutics

Royston Jefferis1

  • 1Division of Immunity & Infection, The School of Medicine, University of Birmingham, Vincent Drive, Edgbaston, Birmingham B15 2TT, UK. r.jefferis@bham.ac.uk

Biotechnology Progress
|May 21, 2005
PubMed

The adaptive immune system has the capacity to produce antibodies with a virtually infinite repertoire of specificities. Recombinant antibodies specific for human targets are established in the clinic as therapeutics and represent a major new class of drug. Therapeutic efficacy depends on the formation of complexes with target molecules and subsequent activation of downstream biologic effector mechanisms that result in elimination of the target. The activation of effector mechanisms is dependent on structural characteristics of the antibody molecule that result from posttranslational modifications, in particular, glycosylation. The production of therapeutic antibody with a consistent human glycoform profile has been and remains a considerable challenge to the biopharmaceutical industry. Recent research has shown that individual glycoforms of antibody may provide optimal efficacy for selected outcomes. Thus a further challenge will be the production of a second generation of antibody therapeutics customized for their clinical indication.

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