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Antigen-Specific Antibody Glycosylation Is Regulated via Vaccination

 
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Author
Mahan, Alison E.
Jennewein, Madeleine F.HARVARD
Suscovich, Todd
Dionne, Kendall
Tedesco, Jacquelynne
Chung, Amy W.
Streeck, Hendrik
Pau, Maria
Schuitemaker, Hanneke
Francis, Don
Fast, Patricia
Laufer, Dagna
Walker, Bruce D.HARVARDORCID  0000-0001-6122-9245
Baden, LindseyHARVARD
Barouch, Dan H.HARVARD
Alter, Galit
Note: Order does not necessarily reflect citation order of authors.
Published Version
https://doi.org/10.1371/journal.ppat.1005456
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Citation
Mahan, A. E., M. F. Jennewein, T. Suscovich, K. Dionne, J. Tedesco, A. W. Chung, H. Streeck, et al. 2016. “Antigen-Specific Antibody Glycosylation Is Regulated via Vaccination.” PLoS Pathogens 12 (3): e1005456. doi:10.1371/journal.ppat.1005456. http://dx.doi.org/10.1371/journal.ppat.1005456.
Abstract
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.
Other Sources
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4794126/pdf/
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This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page
http://nrs.harvard.edu/urn-3:HUL.InstRepos:26318736

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