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

The DOI matches its Crossref record; 94 of the 95 references it cites were found in a registry or an index.

IgG Fc engineering to modulate antibody effector functions

Open access
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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Crossref · 10.1007/s13238-017-0473-8

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Figures

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.
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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Metadata

Authors
Wang, X., Mathieu, M., & Brezski, R. J.
Affiliations
Genentech (US)
Corresponding author
Brezski, Randall J.
ORCID
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
Licence
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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