Bypassing glycosylation: Engineering aglycosylated full-length IgG antibodies for human therapy

Sang Taek Jung, Tae Hyun Kang, William Kelton, George Georgiou

Research output: Contribution to journalReview articlepeer-review

89 Citations (Scopus)

Abstract

In recent years a number of aglycosylated therapeutic antibodies have entered the clinic. The clinical evaluation of these antibodies has served to dispel concerns that the absence of the ubiquitous N297 glycan in the Fc of IgG might result in immunogenicity, poor in vivo stability or unfavorable pharmacokinetics. Importantly, recent studies have now demonstrated that aglycosylated antibodies can be engineered to display novel effector functions and mechanisms of action that do not appear to be possible with their glycosylated counterparts. Moreover, the ability to manufacture aglycosylated antibodies in lower eukaryotes or in bacteria provides significant bioprocessing advantages in terms of shorter bioprocess development and running times and by completely bypassing the problems associated with the glycan heterogeneity of conventional antibodies. These advantages are poised to catapult aglycosylated antibodies to the forefront of protein therapeutics.

Original languageEnglish
Pages (from-to)858-867
Number of pages10
JournalCurrent Opinion in Biotechnology
Volume22
Issue number6
DOIs
Publication statusPublished - 2011 Dec
Externally publishedYes

Bibliographical note

Funding Information:
Research on Fc engineering and IgG expression in bacteria has been supported by the Clayton Foundation for Research , the Norman Hackerman Advanced Research Program (NHARP) of the Texas Higher Education Coordinating Board grant 003658-0066-2009 , and the Cancer Prevention and Research Institute of Texas (CPRIT) grant HIRP100612 . We are thankful to Drs. Yariv Wine and Sai Reddy for comments on the manuscript.

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biomedical Engineering

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