Evidence map›Paper›PMID 27784765›Full record

ArticleThe Biochemical journal2016

Neisseria meningitidis factor H-binding protein bound to monoclonal antibody JAR5: implications for antibody synergy.

Enrico Malito, Paola Lo Surdo, Daniele Veggi, Laura Santini, Heather Stefek, Brunella Brunelli, Enrico Luzzi, Matthew J Bottomley, Peter T Beernink, Maria Scarselli

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

13 citing papers in PubMed, 19 citations in OpenAlex.

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  8. Cocrystal structure of meningococcal factor H binding protein variant 3 reveals a new crossprotective epitope recognized by human mAb 1E6.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 1 institution in 1 country.

Enrico MalitoGSK Vaccines srl, Via Fiorentina 1, Siena 53100, Italy.
Paola Lo SurdoGSK Vaccines srl, Via Fiorentina 1, Siena 53100, Italy.
Daniele VeggiGSK Vaccines srl, Via Fiorentina 1, Siena 53100, Italy.
Laura SantiniGSK Vaccines srl, Via Fiorentina 1, Siena 53100, Italy.
Heather StefekCenter for Immunobiology and Vaccine Development, UCSF Benioff Children's Hospital, Oakland, CA, U.S.A.
Brunella BrunelliGSK Vaccines srl, Via Fiorentina 1, Siena 53100, Italy.
Enrico LuzziGSK Vaccines srl, Via Fiorentina 1, Siena 53100, Italy.
Matthew J BottomleyGSK Vaccines srl, Via Fiorentina 1, Siena 53100, Italy.
Peter T BeerninkCenter for Immunobiology and Vaccine Development, UCSF Benioff Children's Hospital, Oakland, CA, U.S.A.
Maria ScarselliGSK Vaccines srl, Via Fiorentina 1, Siena 53100, Italy.
Toscana Life Sciences · IT

Funding

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
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
NIAID NIH HHS R01 AI099125NIAID NIH HHS R01 AI114701
6 · The paper itself

Abstract

Factor H-binding protein (fHbp) is an important antigen of Neisseria meningitidis that is capable of eliciting a robust protective immune response in humans. Previous studies on the interactions of fHbp with antibodies revealed that some anti-fHbp monoclonal antibodies that are unable to trigger complement-mediated bacterial killing in vitro are highly co-operative and become bactericidal if used in combination. Several factors have been shown to influence such co-operativity, including IgG subclass and antigen density. To investigate the structural basis of the anti-fHbp antibody synergy, we determined the crystal structure of the complex between fHbp and the Fab (fragment antigen-binding) fragment of JAR5, a specific anti-fHbp murine monoclonal antibody known to be highly co-operative with other monoclonal antibodies. We show that JAR5 is highly synergic with monoclonal antibody (mAb) 12C1, whose structure in complex with fHbp has been previously solved. Structural analyses of the epitopes recognized by JAR5 and 12C1, and computational modeling of full-length IgG mAbs of JAR5 and 12C1 bound to the same fHbp molecule, provide insights into the spatial orientation of Fc (fragment crystallizable) regions and into the possible implications for the susceptibility of meningococci to complement-mediated killing.

Indexed as

Antibodies, MonoclonalAntigens, BacterialBacterial ProteinsComplement Factor HEpitopesImmunoglobulin Fab FragmentsImmunoglobulin GNeisseria meningitidisProtein BindingProtein Structure, SecondaryAntibodies, MonoclonalAntigens, BacterialBacterial ProteinsComplement Factor HEpitopesfactor H-binding protein, Neisseria meningitidisImmunoglobulin Fab FragmentsImmunoglobulin GfHbpmonoclonal antibodiesNeisseriaprotein structure

Identifiers

PMID27784765
PMCPMC6398935
OpenAlexW2542266457

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.