Evidence map›Paper›PMID 26982805›Full record

ArticlePLoS pathogens2016

Antigen-Specific Antibody Glycosylation Is Regulated via Vaccination.

Alison E Mahan, Madeleine F Jennewein, Todd Suscovich, Kendall Dionne, Jacquelynne Tedesco, Amy W Chung, Hendrik Streeck, Maria Pau, Hanneke Schuitemaker, Don Francis and 6 more

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 110 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
110citing papers in PubMed, 1 pooled it
16.5field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

110 citing papers in PubMed, 1 synthesis or guideline pooled it, 145 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Trial
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Endothelial cells sialylate IgG within the FcRn-mediated recycling pathway.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Role of Antibody Glycosylation in Health, Disease, and Therapy.Handbook of experimental pharmacology · 2025
    Review
  16. Article
  17. Article
  18. Review
  19. Review
  20. Review

50 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

16 authors at 5 institutions in 2 countries.

Alison E MahanRagon Institute of MGH, MIT and Harvard, Cambridge, Massachusetts, United States of America.
Madeleine F JenneweinRagon Institute of MGH, MIT and Harvard, Cambridge, Massachusetts, United States of America.
Todd SuscovichRagon Institute of MGH, MIT and Harvard, Cambridge, Massachusetts, United States of America.
Kendall DionneRagon Institute of MGH, MIT and Harvard, Cambridge, Massachusetts, United States of America.
Jacquelynne TedescoRagon Institute of MGH, MIT and Harvard, Cambridge, Massachusetts, United States of America.
Amy W ChungRagon Institute of MGH, MIT and Harvard, Cambridge, Massachusetts, United States of America.
Hendrik StreeckMilitary HIV Research Program, Walter Reed Medical Research Institute, Bethesda, Maryland, United States of America.
Maria PauCrucell, Leiden, Netherlands.
Hanneke SchuitemakerCrucell, Leiden, Netherlands.
Don FrancisGlobal Solutions for Infectious Diseases, South San Francisco, California, United States of America.
Patricia FastInternational AIDS Vaccine Initiative, New York, New York, United States of America.
Dagna LauferInternational AIDS Vaccine Initiative, New York, New York, United States of America.
Bruce D WalkerRagon Institute of MGH, MIT and Harvard, Cambridge, Massachusetts, United States of America.
Lindsey BadenDepartment of Medicine, Brigham and Women's Hospital, Boston, Massachusetts, United States of America.
Dan H BarouchRagon Institute of MGH, MIT and Harvard, Cambridge, Massachusetts, United States of America.
Galit AlterRagon Institute of MGH, MIT and Harvard, Cambridge, Massachusetts, United States of America.
Ragon Institute of MGH, MIT and Harvard · USInternational AIDS Vaccine Initiative · USBrigham and Women's Hospital · USGlobal Solutions for Infectious Diseases · USUniversity of Amsterdam · NL

Funding

Preclinical Evaluation of Novel Adenovirus Prime-Boost HIV-1 VaccineU19AI078526 · NIAID · BETH ISRAEL DEACONESS MEDICAL CENTER · PI BAROUCH, DAN H. · 2008 to 2012
$44.0M
Preclinical Evaluation of Novel Ad/MVA and Ad/Protein HIV-1 VaccinesU19AI096040 · NIAID · BETH ISRAEL DEACONESS MEDICAL CENTER · PI SEAMAN, MICHAEL SCOTT · 2012 to 2016
$18.0M
MOLECULAR BASIS OF VIRAL INFECTIVITYT32AI007245 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI Aaron Gregory Schmidt · 1985 to 2026
$11.3M
Tuning Fc-effector functions of HIV-specific antibodiesR01AI102660 · NIAID · MASSACHUSETTS GENERAL HOSPITAL · PI ALTER, GALIT · 2012 to 2015
$3.0M
NIAID NIH HHS AI078526NIAID NIH HHS AI096040NIAID NIH HHS R01 AI102660NIAID NIH HHS R01 AI 102660-02NIAID NIH HHS T32 AI007245NIAID NIH HHS U19 AI078526NIAID NIH HHS U19 AI096040
6 · The paper itself

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.  .

Indexed as

VaccinationAntibody-Dependent Cell CytotoxicityCohort StudiesFemaleGlycoproteinsGlycosylationHIV AntibodiesHIV AntigensHIV InfectionsHIV SeropositivityHumansImmunoglobulin Fc FragmentsImmunoglobulin GMalePhagocytosisGlycoproteinsglycosylated IgGHIV AntibodiesHIV AntigensImmunoglobulin Fc FragmentsImmunoglobulin G

Identifiers

PMID26982805
PMCPMC4794126
OpenAlexW2299193714

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.