Evidence map›Paper›PMID 26078040›Full record

ArticleJournal of immunological methods2015

Microscale purification of antigen-specific antibodies.

Eric P Brown, Erica Normandin, Nana Yaw Osei-Owusu, Alison E Mahan, Ying N Chan, Jennifer I Lai, Monica Vaccari, Mangala Rao, Genoveffa Franchini, Galit Alter and 1 more

Abstract read
In one paragraph

Article in Journal of immunological methods, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

17 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Observational
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 4 institutions in 1 country.

Eric P BrownThayer School of Engineering, Dartmouth College, Hanover, NH 03755, United States.
Erica NormandinThayer School of Engineering, Dartmouth College, Hanover, NH 03755, United States.
Nana Yaw Osei-OwusuMolecular and Cellular Biology Program, Dartmouth College, Hanover, NH 03755, United States.
Alison E MahanRagon Institute of MGH, MIT, and Harvard University, Cambridge, MA 02139, United States.
Ying N ChanThayer School of Engineering, Dartmouth College, Hanover, NH 03755, United States.
Jennifer I LaiThayer School of Engineering, Dartmouth College, Hanover, NH 03755, United States.
Monica VaccariAnimal Models and Vaccine Section, National Cancer Institute, Bethesda, MD 20814, United States.
Mangala RaoU.S. Military HIV Research Program, Walter Reed Army Institute of Research, Silver Spring, MD 20910, United States.
Genoveffa FranchiniAnimal Models and Vaccine Section, National Cancer Institute, Bethesda, MD 20814, United States.
Galit AlterRagon Institute of MGH, MIT, and Harvard University, Cambridge, MA 02139, United States.
Margaret E AckermanThayer School of Engineering, Dartmouth College, Hanover, NH 03755, United States. Electronic address: Margaret.e.ackerman@dartmouth.edu.
Dartmouth College · USNational Cancer Institute · USRagon Institute of MGH, MIT and Harvard · USWalter Reed Army Institute of Research · US

Funding

Demystifying the antiviral activity of the IgG3+ antibody responseR01AI080289 · NIAID · MASSACHUSETTS GENERAL HOSPITAL · PI JUELG, BORIS DOMINIK · 2009 to 2024
$4.1M
Applying High-Performance Protein Engineering Tools to HIV Immunogen DesignR01AI102691 · NIAID · DARTMOUTH COLLEGE · PI ACKERMAN, MARGARET E · 2012 to 2015
$2.2M
NIAID NIH HHS NIH 1R01AI102691NIAID NIH HHS R01 AI080289NIAID NIH HHS R01 AI102691PHS HHS 5R01AIL080289-03
6 · The paper itself

Abstract

Glycosylation of the Fc domain is an important driver of antibody effector function. While assessment of antibody glycoform compositions observed across total plasma IgG has identified differences associated with a variety of clinical conditions, in many cases it is the glycosylation state of only antibodies against a specific antigen or set of antigens that may be of interest, for example, in defining the potential effector function of antibodies produced during disease or after vaccination. Historically, glycoprofiling such antigen-specific antibodies in clinical samples has been challenging due to their low prevalence, the high sample requirement for most methods of glycan determination, and the lack of high-throughput purification methods. New methods of glycoprofiling with lower sample requirements and higher throughput have motivated the development of microscale and automatable methods for purification of antigen-specific antibodies from polyclonal sources such as clinical serum samples. In this work, we present a robot-compatible 96-well plate-based method for purification of antigen-specific antibodies, suitable for such population level glycosylation screening. We demonstrate the utility of this method across multiple antibody sources, using both purified plasma IgG and plasma, and across multiple different antigen types, with enrichment factors greater than 1000-fold observed. Using an on-column IdeS protease treatment, we further describe staged release of Fc and Fab domains, allowing for glycoprofiling of each domain.

Indexed as

AntibodiesAntigensGlycosylationHumansImmunoglobulin Fc FragmentsImmunoglobulin GAntibodiesAntigensImmunoglobulin Fc FragmentsImmunoglobulin GAntibodyAntigenEffector functionGlycosylationPurification

Identifiers

PMID26078040
PMCPMC4604017
OpenAlexW632390566

What OpenQuestion holds

Textmetadata
LicenceTDM
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.