dc.contributor.author | Mahan, Alison E. | en_US |
dc.contributor.author | Jennewein, Madeleine F. | en_US |
dc.contributor.author | Suscovich, Todd | en_US |
dc.contributor.author | Dionne, Kendall | en_US |
dc.contributor.author | Tedesco, Jacquelynne | en_US |
dc.contributor.author | Chung, Amy W. | en_US |
dc.contributor.author | Streeck, Hendrik | en_US |
dc.contributor.author | Pau, Maria | en_US |
dc.contributor.author | Schuitemaker, Hanneke | en_US |
dc.contributor.author | Francis, Don | en_US |
dc.contributor.author | Fast, Patricia | en_US |
dc.contributor.author | Laufer, Dagna | en_US |
dc.contributor.author | Walker, Bruce D. | en_US |
dc.contributor.author | Baden, Lindsey | en_US |
dc.contributor.author | Barouch, Dan H. | en_US |
dc.contributor.author | Alter, Galit | en_US |
dc.date.accessioned | 2016-04-01T15:49:11Z | |
dc.date.issued | 2016 | en_US |
dc.identifier.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. | en |
dc.identifier.issn | 1553-7366 | en |
dc.identifier.uri | http://nrs.harvard.edu/urn-3:HUL.InstRepos:26318736 | |
dc.description.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. | en |
dc.language.iso | en_US | en |
dc.publisher | Public Library of Science | en |
dc.relation.isversionof | doi:10.1371/journal.ppat.1005456 | en |
dc.relation.hasversion | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4794126/pdf/ | en |
dash.license | LAA | en_US |
dc.subject | Biology and Life Sciences | en |
dc.subject | Physiology | en |
dc.subject | Immune Physiology | en |
dc.subject | Antibodies | en |
dc.subject | Medicine and Health Sciences | en |
dc.subject | Immunology | en |
dc.subject | Immune System Proteins | en |
dc.subject | Biochemistry | en |
dc.subject | Proteins | en |
dc.subject | Glycobiology | en |
dc.subject | Glycosylation | en |
dc.subject | Post-Translational Modification | en |
dc.subject | Immune Response | en |
dc.subject | Inflammation | en |
dc.subject | Pathology and Laboratory Medicine | en |
dc.subject | Signs and Symptoms | en |
dc.subject | Microbiology | en |
dc.subject | Medical Microbiology | en |
dc.subject | Microbial Pathogens | en |
dc.subject | Viral Pathogens | en |
dc.subject | Immunodeficiency Viruses | en |
dc.subject | HIV | en |
dc.subject | Pathogens | en |
dc.subject | Organisms | en |
dc.subject | Viruses | en |
dc.subject | Biology and life sciences | en |
dc.subject | RNA viruses | en |
dc.subject | Retroviruses | en |
dc.subject | Lentivirus | en |
dc.subject | Vaccination and Immunization | en |
dc.subject | Vaccines | en |
dc.subject | Public and Occupational Health | en |
dc.subject | Preventive Medicine | en |
dc.subject | Antigens | en |
dc.subject | Medicine and health sciences | en |
dc.subject | Infectious diseases | en |
dc.subject | Viral diseases | en |
dc.subject | HIV infections | en |
dc.title | Antigen-Specific Antibody Glycosylation Is Regulated via Vaccination | en |
dc.type | Journal Article | en_US |
dc.description.version | Version of Record | en |
dc.relation.journal | PLoS Pathogens | en |
dash.depositing.author | Jennewein, Madeleine F. | en_US |
dc.date.available | 2016-04-01T15:49:11Z | |
dc.identifier.doi | 10.1371/journal.ppat.1005456 | * |
dash.authorsordered | false | |
dash.contributor.affiliated | Jennewein, Maddy | |
dash.contributor.affiliated | Barouch, Dan | |
dash.contributor.affiliated | Walker, Bruce | |
dash.contributor.affiliated | Baden, Lindsey | |
dc.identifier.orcid | 0000-0001-6122-9245 | |