Glycosylation of recombinant antibody therapeutics

Biotechnol Prog. Jan-Feb 2005;21(1):11-6. doi: 10.1021/bp040016j.

Abstract

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.

Publication types

  • Review

MeSH terms

  • Antibodies / metabolism
  • Antibodies / therapeutic use*
  • Glycosylation
  • Humans
  • Immunoglobulin Fc Fragments / chemistry
  • Immunoglobulin Fc Fragments / metabolism
  • Immunoglobulin G / chemistry
  • Immunoglobulin G / metabolism
  • Oligosaccharides / chemistry
  • Oligosaccharides / metabolism
  • Protein Engineering
  • Recombinant Proteins / metabolism
  • Recombinant Proteins / therapeutic use

Substances

  • Antibodies
  • Immunoglobulin Fc Fragments
  • Immunoglobulin G
  • Oligosaccharides
  • Recombinant Proteins