Evidence map›Paper›PMID 25484063›Full record

ArticlemAbs2014

Characterization of a plant-produced recombinant human secretory IgA with broad neutralizing activity against HIV.

Matthew Paul, Rajko Reljic, Katja Klein, Pascal M W Drake, Craig van Dolleweerd, Martin Pabst, Markus Windwarder, Elsa Arcalis, Eva Stoger, Friedrich Altmann and 4 more

Open access · goldAbstract read
In one paragraph

Article in mAbs, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
5.4field-weighted citation impact, top 5% 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

34 citing papers in PubMed, 54 citations in OpenAlex.

  1. Plant-Based Systems for Producing Therapeutic Proteins: Current Status and Future Prospects.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026
    Review
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Recombinant neutralizing secretory IgA antibodies for preventing mucosal acquisition and transmission of SARS-CoV-2.Molecular therapy : the journal of the American Society of Gene Therapy · 2024
    Article
  8. Plant-based biopharmaceutical engineering.Nature reviews bioengineering · 2023
    Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. EfficientFrontiers in chemistry · 2020
    Article
  18. Article
  19. Review
  20. 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

14 authors at 6 institutions in 5 countries.

Matthew Paula The Hotung Molecular Immunology Group; Institute for Infection & Immunity; St George's ; University of London ; London , UK.
Rajko Reljic
Katja Klein
Pascal M W Drake
Craig van Dolleweerd
Martin Pabst
Markus Windwarder
Elsa Arcalis
Eva Stoger
Friedrich Altmann
Catherine Cosgrove
Angela Bartolf
Susan Baden
Julian K-C Ma
BOKU University · ATSt George's, University of London · GBSt. George's School · USUniversidad de Londres · MXImperial Valley College · USInstitute of Infection and Immunity · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recombinant Secretory IgA (SIgA) complexes have the potential to improve antibody-based passive immunotherapeutic approaches to combat many mucosal pathogens. In this report, we describe the expression, purification and characterization of a human SIgA format of the broadly neutralizing anti-HIV monoclonal antibody (mAb) 2G12, using both transgenic tobacco plants and transient expression in Nicotiana benthamiana as expression hosts (P2G12 SIgA). The resulting heterodecameric complexes accumulated in intracellular compartments in leaf tissue, including the vacuole. SIgA complexes could not be detected in the apoplast. Maximum yields of antibody were 15.2 μg/g leaf fresh mass (LFM) in transgenic tobacco and 25 μg/g LFM after transient expression, and assembly of SIgA complexes was superior in transgenic tobacco. Protein L purified antibody specifically bound HIV gp140 and neutralised tier 2 and tier 3 HIV isolates. Glycoanalysis revealed predominantly high mannose structures present on most N-glycosylation sites, with limited evidence for complex glycosylation or processing to paucimannosidic forms. O-glycan structures were not identified. Functionally, P2G12 SIgA, but not IgG, effectively aggregated HIV virions. Binding of P2G12 SIgA was observed to CD209 / DC-SIGN, but not to CD89 / FcalphaR on a monocyte cell line. Furthermore, P2G12 SIgA demonstrated enhanced stability in mucosal secretions in comparison to P2G12 IgG mAb.

Indexed as

Antibodies, NeutralizingBinding SitesBody Fluidsenv Gene Products, Human Immunodeficiency VirusFemaleGlycosylationHIVHumansImmunoblottingImmunoglobulin A, SecretoryMicroscopy, ElectronMicroscopy, FluorescenceNicotianaPlant LeavesPlants, Genetically ModifiedPolysaccharidesAntibodies, Neutralizingenv Gene Products, Human Immunodeficiency VirusImmunoglobulin A, SecretoryPolysaccharidesRecombinant Proteinsantibody stabilityDC-SIGN, dendritic cell – specific intercellular adhesion molecule 3 grabbing non-integringlycosylationHIV microbicideLFM, leaf fresh massmolecular farmingSC, secretory componentsecretory IgASEM, standard error of the mean; SIgA, secretory IgA

Identifiers

PMID25484063
PMCPMC4622858
OpenAlexW1967888916

What OpenQuestion holds

Textmetadata
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.