Evidence map›Paper›PMID 27307451›Full record

ArticleClinical and vaccine immunology : CVI2016

Human IgG1, IgG3, and IgG3 Hinge-Truncated Mutants Show Different Protection Capabilities against Meningococci Depending on the Target Antigen and Epitope Specificity.

S Giuntini, D M Granoff, P T Beernink, O Ihle, D Bratlie, T E Michaelsen

Open access · diamondAbstract read
In one paragraph

Article in Clinical and vaccine immunology : CVI, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
4.0field-weighted citation impact, top 7% 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

35 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. An RNA-to-RNA pipeline for rapid antiviral antibody development.Molecular therapy : the journal of the American Society of Gene Therapy · 2026
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  19. Virulence · 2021
    Article
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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

6 authors at 2 institutions in 2 countries.

S GiuntiniCenter for Immunobiology and Vaccine Development, UCSF Benioff Children's Hospital Oakland Research Institute, Oakland, California, USA.
D M GranoffCenter for Immunobiology and Vaccine Development, UCSF Benioff Children's Hospital Oakland Research Institute, Oakland, California, USA.
P T BeerninkCenter for Immunobiology and Vaccine Development, UCSF Benioff Children's Hospital Oakland Research Institute, Oakland, California, USA.ORCID 0000-0001-5734-083X
O IhleDivision of Infectious Disease Control, Department of Bacteriology and Immunology, Norwegian Institute of Public Health, Oslo, Norway.
D BratlieDivision of Infectious Disease Control, Department of Bacteriology and Immunology, Norwegian Institute of Public Health, Oslo, Norway.
UCSF Benioff Children's Hospital · USNorwegian Institute of Public Health · NO

Funding

Novel vaccine strategies for prevention of N. meningitidis group B diseaseR01AI046464 · NIAID · OMVAX, INC. · PI MOE, GREGORY ROBERT · 2000 to 2024
$12.1M
The effect of binding of fH to meningococcal fHbp vaccine on antibody protectionR01AI114701 · NIAID · CHILDREN'S HOSPITAL & RES CTR AT OAKLAND · PI BEERNINK, PETER T. · 2015 to 2019
$3.3M
CONSTRUCTION OF THE VACCINE CENTERC06RR016226 · NCRR · CHILDREN'S HOSPITAL &RES CTR AT OAKLAND · PI LUCAS, ALEXANDER H. · 2002 to 2002
$2.0M
Improved mutant meningococcal factor H binding protein vaccinesR01AI099125 · NIAID · CHILDREN'S HOSPITAL & RES CTR AT OAKLAND · PI BEERNINK, PETER T. · 2012 to 2015
$1.9M
NCRR NIH HHS C06 RR016226NIAID NIH HHS R01 AI046464NIAID NIH HHS R01 AI099125NIAID NIH HHS R01 AI114701
6 · The paper itself

Abstract

We compared the bactericidal activity of recombinant sets of chimeric IgG monoclonal antibodies against two important outer membrane meningococcal vaccine antigens: PorA and factor H binding protein (FHbp). The sets contained human Fc portions from IgG1, IgG3, and two IgG3 mutants (IgG3m15 and IgGm17) with hinge regions of 15 and 17 amino acids encoded by hinge exons h2 and h1, respectively (human IgG3 has a hinge region of 62 amino acids encoded by hinge exons h1, h2, h3, and h4, while human IgG1 has a hinge region of only 15 amino acids encoded by one hinge exon) and mouse V regions. IgG1 showed higher bactericidal activity than IgG3 when directed against PorA (an abundant antigen), while IgG3 was more bactericidal than IgG1 when directed against FHbp (a sparsely and variably distributed antigen). On the other hand, the IgG3 hinge-truncated antibodies IgG3m15 and IgGm17 showed higher bactericidal activity than both IgG1 and IgG3 regardless of the target antigen. Thus, the Fc region of IgG3 antibodies appears to have an enhanced complement-activating function, independent of their long hinge region, compared to IgG1 antibodies. The greater activity of the truncated IgG3 hinge mutants indicates that the long hinge of IgG3 seems to downregulate through an unknown mechanism the inherent increased complement-activating capability of IgG3 Fc when the antibody binds to a sparse antigen.

Indexed as

Blood Bactericidal ActivityAdultAnimalsAntibodies, BacterialAntigens, BacterialBacterial ProteinsComplement ActivationEpitopesHumansImmunoglobulin GMiceNeisseria meningitidisPorinsRecombinant ProteinsAntibodies, BacterialAntigens, BacterialBacterial ProteinsEpitopesfactor H-binding protein, Neisseria meningitidisImmunoglobulin Gporin protein, NeisseriaPorinsRecombinant Proteins

Identifiers

PMID27307451
PMCPMC4979173
OpenAlexW2441943177

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.