Effect of glycosylation on antibody function: implications for genetic engineering

Trends Biotechnol. 1997 Jan;15(1):26-32. doi: 10.1016/S0167-7799(96)10062-7.

Abstract

Antibodies are able to both bind antigens and trigger the responses that eliminate them from circulation. All antibodies are glycosylated at conserved positions in their constant regions, and the presence of carbohydrate can be critical for antigen clearance functions such as complement activation. The structure of the attached carbohydrate can also affect antibody activity. Antibody glycosylation can be influenced by the cell in which it is produced, the conformation of the antibody and cell culture conditions. These variables should be considered in the design and production of antibodies with selected specificity and function.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Antibodies / genetics
  • Antibodies / immunology*
  • Antibody Specificity
  • Carbohydrate Conformation
  • Carbohydrates / chemistry
  • Carbohydrates / physiology
  • Cloning, Molecular
  • Glycosylation
  • Humans
  • Immunoglobulin G / genetics
  • Immunoglobulin G / immunology
  • Recombinant Proteins / genetics
  • Recombinant Proteins / immunology

Substances

  • Antibodies
  • Carbohydrates
  • Immunoglobulin G
  • Recombinant Proteins