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

Sang Taek Jung

doi:10.1007/s12257-012-0711-0

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

Sang Taek Jung

Research output: Contribution to journal › Review article › peer-review

11 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 language	English
Pages (from-to)	625-636
Number of pages	12
Journal	Biotechnology and Bioprocess Engineering
Volume	18
Issue number	4
DOIs	https://doi.org/10.1007/s12257-012-0711-0
Publication status	Published - 2013 Jul
Externally published	Yes

Keywords

Fc engineering
antibody engineering
effector functions
therapeutic antibody

ASJC Scopus subject areas

Biotechnology
Bioengineering
Applied Microbiology and Biotechnology
Biomedical Engineering

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1007/s12257-012-0711-0

Cite this

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title = "Tailoring immunoglobulin Fc for highly potent and serum-stable therapeutic antibodies",

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.",

keywords = "Fc engineering, antibody engineering, effector functions, therapeutic antibody",

author = "Jung, {Sang Taek}",

note = "Funding Information: This research was supported by the Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Science, ICT and Future Planning (2013R1A1A1004576).",

year = "2013",

month = jul,

doi = "10.1007/s12257-012-0711-0",

language = "English",

volume = "18",

pages = "625--636",

journal = "Biotechnology and Bioprocess Engineering",

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TY - JOUR

T1 - Tailoring immunoglobulin Fc for highly potent and serum-stable therapeutic antibodies

AU - Jung, Sang Taek

N1 - Funding Information: This research was supported by the Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Science, ICT and Future Planning (2013R1A1A1004576).

PY - 2013/7

Y1 - 2013/7

N2 - 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.

AB - 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.

KW - Fc engineering

KW - antibody engineering

KW - effector functions

KW - therapeutic antibody

UR - http://www.scopus.com/inward/record.url?scp=84882579911&partnerID=8YFLogxK

U2 - 10.1007/s12257-012-0711-0

DO - 10.1007/s12257-012-0711-0

M3 - Review article

AN - SCOPUS:84882579911

SN - 1226-8372

VL - 18

SP - 625

EP - 636

JO - Biotechnology and Bioprocess Engineering

JF - Biotechnology and Bioprocess Engineering

IS - 4

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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