Evidence map›Paper›PMID 28428342›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Lysibodies are IgG Fc fusions with lysin binding domains targeting

Assaf Raz, Anna Serrano, Christine Lawson, Maneesha Thaker, Tricia Alston, Stylianos Bournazos, Jeffrey V Ravetch, Vincent A Fischetti

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. 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
2.1field-weighted citation impact, top 14% 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, 29 citations in OpenAlex.

  1. Article
  2. [Use of vaccines to prevent the development of bacterial resistance].Bundesgesundheitsblatt, Gesundheitsforschung, Gesundheitsschutz · 2026
    Review
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  12. Targets of immunomodulation in bacterial endophthalmitis.Progress in retinal and eye research · 2019
    Review
  13. Article
  14. Article
  15. The EMBO journal · 2018
    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

8 authors at 1 institution in 1 country.

Assaf RazLaboratory of Bacterial Pathogenesis and Immunology, The Rockefeller University, New York, NY 10065; araz@rockefeller.edu.
Anna SerranoLaboratory of Bacterial Pathogenesis and Immunology, The Rockefeller University, New York, NY 10065.
Christine LawsonLaboratory of Bacterial Pathogenesis and Immunology, The Rockefeller University, New York, NY 10065.
Maneesha ThakerLaboratory of Bacterial Pathogenesis and Immunology, The Rockefeller University, New York, NY 10065.
Tricia AlstonLaboratory of Bacterial Pathogenesis and Immunology, The Rockefeller University, New York, NY 10065.
Stylianos BournazosLaboratory of Molecular Genetics and Immunology, The Rockefeller University, New York, NY 10065.
Jeffrey V RavetchLaboratory of Molecular Genetics and Immunology, The Rockefeller University, New York, NY 10065.
Vincent A FischettiLaboratory of Bacterial Pathogenesis and Immunology, The Rockefeller University, New York, NY 10065.
Rockefeller University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cell wall of Gram-positive bacteria contains abundant surface-exposed carbohydrate molecules that are highly conserved within and often across species. The potential therapeutic usefulness of high-affinity antibodies to cell wall carbohydrates is unquestioned, however obtaining such antibodies is challenging due to the poor overall immunogenicity of these bacterial targets. Autolysins and phage lysins are peptidoglycan hydrolases, enzymes that have evolved over a billion years to degrade bacterial cell wall. Such wall hydrolases are modular enzymes, composed of discrete domains for high-affinity binding to cell wall carbohydrates and cleavage activity. In this study, we demonstrate that binding domains from autolysins and lysins can be fused to the Fc region of human IgG, creating a fully functional homodimer (or "lysibody") with high-affinity binding and specificity for carbohydrate determinants on the bacterial surface. Furthermore, we demonstrate that this process is reproducible with three different binding domains specific to methicillin-resistant

Indexed as

Cell WallHL-60 CellsHumansImmunoglobulin Fc FragmentsN-Acetylmuramoyl-L-alanine AmidasePhagocytosisPolysaccharides, BacterialRecombinant Fusion ProteinsStaphylococcus aureusImmunoglobulin Fc FragmentsN-Acetylmuramoyl-L-alanine AmidasePolysaccharides, BacterialRecombinant Fusion Proteinsantibodyimmunotherapymonoclonalpeptidoglycan hydrolasevaccine

Identifiers

PMID28428342
PMCPMC5422811
OpenAlexW2605866750

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.