Correction: Antigen-Specific Antibody Glycosylation Is Regulated via Vaccination
| Autor: | Todd J. Suscovich, Lindsey R. Baden, Maria Pau, Dagna Laufer, Hanneke Schuitemaker, Bruce D. Walker, Hendrik Streeck, Patricia E. Fast, Dan H. Barouch, Donald P. Francis, Kendall Dionne, Alison E. Mahan, Amy W. Chung, Galit Alter, Madeleine F. Jennewein, Jacquelynne Tedesco |
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| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
lcsh:Immunologic diseases. Allergy Male Glycosylation HIV Antigens Immunology HIV Infections HIV Antibodies Microbiology Cohort Studies 03 medical and health sciences chemistry.chemical_compound Phagocytosis Antigen specific Virology HIV Seropositivity Genetics Humans Molecular Biology lcsh:QH301-705.5 Side panel Fucosylation biology Chemistry Vaccination Antibody-Dependent Cell Cytotoxicity Correction Igg glycosylation Cell biology Immunoglobulin Fc Fragments 030104 developmental biology lcsh:Biology (General) Immunoglobulin G biology.protein Parasitology Female Antibody lcsh:RC581-607 |
| Zdroj: | PLoS Pathogens PLoS Pathogens, Vol 12, Iss 6, p e1005694 (2016) |
| ISSN: | 1553-7374 1553-7366 |
| Popis: | Antibody effector functions, such as antibody-dependent cellular cytotoxicity, complement deposition, and antibody-dependent phagocytosis, play a critical role in immunity against multiple pathogens, particularly in the absence of neutralizing activity. Two modifications to the IgG constant domain (Fc domain) regulate antibody functionality: changes in antibody subclass and changes in a single N-linked glycan located in the CH2 domain of the IgG Fc. Together, these modifications provide a specific set of instructions to the innate immune system to direct the elimination of antibody-bound antigens. While it is clear that subclass selection is actively regulated during the course of natural infection, it is unclear whether antibody glycosylation can be tuned, in a signal-specific or pathogen-specific manner. Here, we show that antibody glycosylation is determined in an antigen- and pathogen-specific manner during HIV infection. Moreover, while dramatic differences exist in bulk IgG glycosylation among individuals in distinct geographical locations, immunization is able to overcome these differences and elicit antigen-specific antibodies with similar antibody glycosylation patterns. Additionally, distinct vaccine regimens induced different antigen-specific IgG glycosylation profiles, suggesting that antibody glycosylation is not only programmable but can be manipulated via the delivery of distinct inflammatory signals during B cell priming. These data strongly suggest that the immune system naturally drives antibody glycosylation in an antigen-specific manner and highlights a promising means by which next-generation therapeutics and vaccines can harness the antiviral activity of the innate immune system via directed alterations in antibody glycosylation in vivo. . |
| Databáze: | OpenAIRE |
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