Tailoring immunoglobulin Fc for highly potent and serum-stable therapeutic antibodies

Research output: Contribution to journalReview article

9 Citations (Scopus)

Abstract

Antibody Fc region, a recruiter and a frontline commander in the combat against cancer and infectious pathogens, mediates potent immune effector functions by engaging Fc receptors and serum complement proteins. Recent studies indicate that the Fc region is particularly amenable to modifications that enhance potency and serum stability through amino acid substitution and glycan modification. In order to modulate the interaction of the Fc domain with Fc-binding ligands (FcγRs, C1q, and FcRn), various engineering strategies have been employed; these studies are discussed in this review.

Original languageEnglish
Pages (from-to)625-636
Number of pages12
JournalBiotechnology and Bioprocess Engineering
Volume18
Issue number4
DOIs
Publication statusPublished - 2013 Jul 1
Externally publishedYes

Fingerprint

Immunoglobulin Fc Fragments
Fc Receptors
Pathogens
Amino Acid Substitution
Antibodies
Polysaccharides
Amino acids
Blood Proteins
Complement System Proteins
Substitution reactions
Ligands
Proteins
Amino Acids
Serum
Neoplasms
Therapeutics

Keywords

  • antibody engineering
  • effector functions
  • Fc engineering
  • therapeutic antibody

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology
  • Biomedical Engineering

Cite this

Tailoring immunoglobulin Fc for highly potent and serum-stable therapeutic antibodies. / Jung, Sang Taek.

In: Biotechnology and Bioprocess Engineering, Vol. 18, No. 4, 01.07.2013, p. 625-636.

Research output: Contribution to journalReview article

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