Cited by 357Monoclonal and Polyclonal Antibodies ResearchProtein purification and stabilityImmune Cell Function and Interaction

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IgG Fc engineering to modulate antibody effector functions

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Wang, Xinhua, Mathieu, Mary, Brezski, Randall J.·2018·Protein & Cell

DOI 10.1007/s13238-017-0473-8PMC PMC5777978

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Abstract

Therapeutic monoclonal antibodies are among the most effective biotherapeutics to date. An important aspect of antibodies is their ability to bind antigen while at the same time recruit immune effector functions. The majority of approved recombinant monoclonal antibody therapies are of the human IgG1 subclass, which can engage both humoral and cellular components of the immune system. The wealth of information generated about antibodies has afforded investigators the ability to molecularly engineer antibodies to modulate effector functions. Here, we review various antibody engineering efforts intended to improve efficacy and safety relative to the human IgG isotype. Further, we will discuss proposed mechanisms by which engineering approaches led to modified interactions with immune components and provide examples of clinical studies using next generation antibodies.

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Figure 1 The Fc domain of human IgG1 is shown (PDBID:3AVE). The positions of amino acids described in Table 1 are shown. Key sequence motifs for FcRn interactions are shown in green (L251-S254; L309-Q311; N434-H435) (Oganesyan et al., 2014). Amino acids 5 angstroms proximal to the FcγR:Fc interface for FcγRI (PDBID:4W4O) (Kiyoshi et al., 2015), FcγRIIa (PDBID:3RY6) (Ramsland et al., 2011), FcγRIIb (PDBID:3WJJ) (Mimoto et al., 2013b), and FcγRIIIb (PDBID:1E4K) (Sondermann et al., 2000) as determined with PyMOL are shown in red (P232-S239; D265-D270; Y296-T299; N325-I332). The amino acids that are critical for interactions with C1q are shown in blue (D270, K322, P329, P331) (Idusogie et al., 2000). Amino acids depicted in black were not identified as critical for interactions with FγRs, FcRn, or C1q. Figure 1 was generated with PyMOL.CC BY · PubMed Central

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Authors: Wang, X., Mathieu, M., & Brezski, R. J.
Affiliations: Genentech (US)
Corresponding author: Brezski, Randall J.
ORCID: Wang, Xinhua
Brezski, Randall J.
Venue: Protein & Cell
Publisher: Oxford University Press (OUP)
Published: 2017-10-06
Volume: 9
Issue: 1
Pages: 63-73
ISSN: 1674-800X (ISSN-L)
1674-8018
DOI: 10.1007/s13238-017-0473-8
PMC: PMC5777978
OpenAlex: W2763907629
Cited by: 356
References: 95
Citations by year: 2026: 28 · 2025: 41 · 2024: 57 · 2023: 35 · 2022: 50 · 2021: 44 · 2020: 44 · 2019: 43 · 2018: 13 · 2017: 1
FWCI: 4.22
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
creativecommons.org/licenses/by/4.0 (unspecified)
Locations: Protein & Cell (publishedVersion, cc-by)
Europe PMC (PubMed Central) (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
Topics: Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
Life Sciences › Immunology and Microbiology › Immunology › Immune Cell Function and Interaction
Keywords: antibody effector functions, human IgG1, therapeutic monoclonal antibodies, antibody engineering, immune effector mechanisms, antibody safety, antibody efficacy
MeSH terms: Animals, Antibodies, Monoclonal, Antigens, Complement System Proteins, Humans, Immunoglobulin G, Receptors, Fc, Protein Engineering

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IgG Fc engineering to modulate antibody effector functions

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