Evidence map›Paper›PMID 21930905›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Heavy chain-only antibodies and tetravalent bispecific antibody neutralizing Staphylococcus aureus leukotoxins.

Benoît-Joseph Laventie, Hendrik Jan Rademaker, Maher Saleh, Ernie de Boer, Rick Janssens, Tristan Bourcier, Audrey Subilia, Luc Marcellin, Rien van Haperen, Joyce H G Lebbink and 4 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

36 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
  2. Article
  3. In Vivo Pathogenicity of Methicillin-SusceptibleLife (Basel, Switzerland) · 2022
    Article
  4. An anti-CTLA-4 heavy chain-only antibody with enhanced TProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Toxins · 2021
    Review
  6. Biochemistry, structure, and cellular internalization of a four nanobody-bearing Fc dimer.Protein science : a publication of the Protein Society · 2021
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. The Pathogenesis of Staphylococcus aureus Eye Infections.Pathogens (Basel, Switzerland) · 2018
    Review
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 3 institutions in 2 countries.

Benoît-Joseph LaventieFaculté de Médecine, Physiopathologie et Médecine Translationnelle, Institut de Bactériologie, Centre Hospitalier Régional Universitaire, Université de Strasbourg, 67000 Strasbourg, France.
Hendrik Jan Rademaker
Maher Saleh
Ernie de Boer
Rick Janssens
Tristan Bourcier
Audrey Subilia
Luc Marcellin
Rien van Haperen
Joyce H G Lebbink
Tao Chen
Gilles Prévost
Frank Grosveld
Dubravka Drabek
Erasmus MC · NLHôpitaux Universitaires de Strasbourg · FRUniversité de Strasbourg · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Panton-Valentine leukocidin (PVL) is a pore-forming toxin associated with current outbreaks of community-associated methicillin-resistant strains and implicated directly in the pathophysiology of Staphylococcus aureus-related diseases. Humanized heavy chain-only antibodies (HCAb) were generated against S. aureus PVL from immunized transgenic mice to neutralize toxin activity. The active form of PVL consists of the two components, LukS-PV and LukF-PV, which induce osmotic lysis following pore formation in host defense cells. One anti-LukS-PV HCAb, three anti-LukF-PV HCAbs with affinities in the nanomolar range, and one engineered tetravalent bispecific HCAb were tested in vitro and in vivo, and all prevented toxin binding and pore formation. Anti-LukS-PV HCAb also binds to γ-hemolysin C (HlgC) and inhibits HlgC/HlgB pore formation. Experiments in vivo in a toxin-induced rabbit endophthalmitis model showed that these HCAbs inhibit inflammatory reactions and tissue destruction, with the tetravalent bispecific HCAb performing best. Our findings show the therapeutic potential of HCAbs, and in particular, bispecific antibodies.

Indexed as

Amino Acid SequenceAnimalsAntibodies, BispecificAntibodies, NeutralizingAntibody AffinityAntibody SpecificityEnzyme-Linked Immunosorbent AssayExotoxinsHumansImmunoglobulin Heavy ChainsMolecular Sequence DataRabbitsSequence Homology, Amino AcidStaphylococcus aureusAntibodies, BispecificAntibodies, NeutralizingExotoxinsImmunoglobulin Heavy Chainsleukotoxin

Identifiers

PMID21930905
PMCPMC3182740
OpenAlexW2149347797

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.