Editorial: Structure, isotypes, targets, and post-translational modifications of immunoglobulins and their role in infection, inflammation and autoimmunity, Volume II

doi:10.3389/fimmu.2022.1041613

Editorial

. 2022 Oct 17:13:1041613.

doi: 10.3389/fimmu.2022.1041613. eCollection 2022.

Editorial: Structure, isotypes, targets, and post-translational modifications of immunoglobulins and their role in infection, inflammation and autoimmunity, Volume II

Jan Novak¹, Laureline Berthelot², Sylvie Hermouet^{3

4}

Affiliations

¹ Department of Microbiology, University of Alabama at Birmingham, Birmingham, AL, United States.
² INSERM, Center for Research in Transplantation and Translational Immunology, UMR 1064, Nantes Université, Nantes, France.
³ INSERM, Immunology and New Concepts in ImmunoTherapy, INCIT, UMR 1302, Nantes Université, Nantes, France.
⁴ Laboratoire d'Hématologie, Centre Hospital Universitaire (CHU) Nantes, Nantes, France.

PMID: 36325328
PMCID: PMC9619208
DOI: 10.3389/fimmu.2022.1041613

Editorial

Editorial: Structure, isotypes, targets, and post-translational modifications of immunoglobulins and their role in infection, inflammation and autoimmunity, Volume II

Jan Novak et al. Front Immunol. 2022.

. 2022 Oct 17:13:1041613.

doi: 10.3389/fimmu.2022.1041613. eCollection 2022.

Authors

Jan Novak¹, Laureline Berthelot², Sylvie Hermouet^{3

4}

Affiliations

¹ Department of Microbiology, University of Alabama at Birmingham, Birmingham, AL, United States.
² INSERM, Center for Research in Transplantation and Translational Immunology, UMR 1064, Nantes Université, Nantes, France.
³ INSERM, Immunology and New Concepts in ImmunoTherapy, INCIT, UMR 1302, Nantes Université, Nantes, France.
⁴ Laboratoire d'Hématologie, Centre Hospital Universitaire (CHU) Nantes, Nantes, France.

PMID: 36325328
PMCID: PMC9619208
DOI: 10.3389/fimmu.2022.1041613

No abstract available

Keywords: DNA rearrangement; Immunoglobulins; autoimmunity; infection; structure.

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Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Comment on

Editorial on the Research Topic Structure, isotypes, targets, and post-translational modifications of immunoglobulins and their role in infection, inflammation and autoimmunity Volume II

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References

1. Nimmerjahn F, Ravetch JV. Divergent immunoglobulin γ subclass activity through selective fc receptor binding. Science (2005) 310:1510–2. doi: 10.1126/science.1118948 - DOI - PubMed
1. Kaneko Y, Nimmerjahn F, Ravetch JV. Anti-inflammatory activity of immunoglobulin G resulting from fc sialylation. Science (2006) 313:670–3. doi: 10.1126/science.1129594 - DOI - PubMed
1. Scallon BJ, Tam SH, McCarthy SG, Cai AN, Raju TS. Higher levels of sialylated fc glycans in immunoglobulin G molecules can adversely impact functionality. Mol Immunol (2007) 44:1524–34. doi: 10.1016/j.molimm.2006.09.005 - DOI - PubMed
1. Ackerman ME, Crispin M, Yu X, Baruah K, Boesch AW, Harvey DJ, et al. . Natural variation in fc glycosylation of HIV-specific antibodies impacts antiviral activity. J Clin Invest (2013) 123:2183–92. doi: 10.1172/JCI65708 - DOI - PMC - PubMed
1. Quast I, Keller CW, Maurer MA, Giddens JP, Tackenberg B, Wang L-X, et al. . Sialylation of IgG fc domain impairs complement-dependent cytotoxicity. J Clin Invest (2015) 125:4160–70. doi: 10.1172/JCI82695 - DOI - PMC - PubMed

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[1] Nimmerjahn F, Ravetch JV. Divergent immunoglobulin γ subclass activity through selective fc receptor binding. Science (2005) 310:1510–2. doi: 10.1126/science.1118948 - DOI - PubMed

[2] Nimmerjahn F, Ravetch JV. Divergent immunoglobulin γ subclass activity through selective fc receptor binding. Science (2005) 310:1510–2. doi: 10.1126/science.1118948 - DOI - PubMed

[3] Kaneko Y, Nimmerjahn F, Ravetch JV. Anti-inflammatory activity of immunoglobulin G resulting from fc sialylation. Science (2006) 313:670–3. doi: 10.1126/science.1129594 - DOI - PubMed

[4] Kaneko Y, Nimmerjahn F, Ravetch JV. Anti-inflammatory activity of immunoglobulin G resulting from fc sialylation. Science (2006) 313:670–3. doi: 10.1126/science.1129594 - DOI - PubMed

[5] Scallon BJ, Tam SH, McCarthy SG, Cai AN, Raju TS. Higher levels of sialylated fc glycans in immunoglobulin G molecules can adversely impact functionality. Mol Immunol (2007) 44:1524–34. doi: 10.1016/j.molimm.2006.09.005 - DOI - PubMed

[6] Scallon BJ, Tam SH, McCarthy SG, Cai AN, Raju TS. Higher levels of sialylated fc glycans in immunoglobulin G molecules can adversely impact functionality. Mol Immunol (2007) 44:1524–34. doi: 10.1016/j.molimm.2006.09.005 - DOI - PubMed

[7] Ackerman ME, Crispin M, Yu X, Baruah K, Boesch AW, Harvey DJ, et al. . Natural variation in fc glycosylation of HIV-specific antibodies impacts antiviral activity. J Clin Invest (2013) 123:2183–92. doi: 10.1172/JCI65708 - DOI - PMC - PubMed

[8] Ackerman ME, Crispin M, Yu X, Baruah K, Boesch AW, Harvey DJ, et al. . Natural variation in fc glycosylation of HIV-specific antibodies impacts antiviral activity. J Clin Invest (2013) 123:2183–92. doi: 10.1172/JCI65708 - DOI - PMC - PubMed

[9] Quast I, Keller CW, Maurer MA, Giddens JP, Tackenberg B, Wang L-X, et al. . Sialylation of IgG fc domain impairs complement-dependent cytotoxicity. J Clin Invest (2015) 125:4160–70. doi: 10.1172/JCI82695 - DOI - PMC - PubMed

[10] Quast I, Keller CW, Maurer MA, Giddens JP, Tackenberg B, Wang L-X, et al. . Sialylation of IgG fc domain impairs complement-dependent cytotoxicity. J Clin Invest (2015) 125:4160–70. doi: 10.1172/JCI82695 - DOI - PMC - PubMed

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Editorial: Structure, isotypes, targets, and post-translational modifications of immunoglobulins and their role in infection, inflammation and autoimmunity, Volume II

Affiliations

Editorial: Structure, isotypes, targets, and post-translational modifications of immunoglobulins and their role in infection, inflammation and autoimmunity, Volume II

Authors

Affiliations

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