Evidence map›Paper›PMID 27415624›Full record

ArticlePloS one2016

Anti-Hemagglutinin Antibody Derived Lead Peptides for Inhibitors of Influenza Virus Binding.

Henry Memczak, Daniel Lauster, Parimal Kar, Santiago Di Lella, Rudolf Volkmer, Volker Knecht, Andreas Herrmann, Eva Ehrentreich-Förster, Frank F Bier, Walter F M Stöcklein

Open access · goldAbstract read
In one paragraph

Article in PloS one, 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
1.9field-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

13 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Antiviral Peptides as Anti-Influenza Agents.International journal of molecular sciences · 2022
    Review
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  12. Article
  13. Multivalent Peptide-Nanoparticle Conjugates for Influenza-Virus Inhibition.Angewandte Chemie (International ed. in English) · 2017
    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

10 authors at 6 institutions in 2 countries.

Henry MemczakDepartment of Bioanalytics and Biosensorics, Fraunhofer Institute for Cell Therapy and Immunology, Branch Bioanalytics and Bioprocesses, Potsdam, Germany.
Daniel LausterDepartment of Biology, Humboldt Universität zu Berlin, Berlin, Germany.
Parimal KarDepartment of Theory and Bio-Systems, Max-Planck-Institute of Colloids and Interfaces, Potsdam, Germany.
Santiago Di LellaDepartment of Biology, Humboldt Universität zu Berlin, Berlin, Germany.
Rudolf VolkmerInstitute of Immunology, Charité, Berlin, Germany.
Volker KnechtDepartment of Theory and Bio-Systems, Max-Planck-Institute of Colloids and Interfaces, Potsdam, Germany.
Andreas HerrmannDepartment of Biology, Humboldt Universität zu Berlin, Berlin, Germany.
Eva Ehrentreich-FörsterDepartment of Bioanalytics and Biosensorics, Fraunhofer Institute for Cell Therapy and Immunology, Branch Bioanalytics and Bioprocesses, Potsdam, Germany.
Frank F BierInstitute of Biochemistry and Biology, University of Potsdam, Potsdam, Germany.
Walter F M StöckleinDepartment of Bioanalytics and Biosensorics, Fraunhofer Institute for Cell Therapy and Immunology, Branch Bioanalytics and Bioprocesses, Potsdam, Germany.
Fraunhofer Institute for Cell Therapy and Immunology · DEHumboldt-Universität zu Berlin · DEMax Planck Institute of Colloids and Interfaces · DECharité - Universitätsmedizin Berlin · DEConsejo Nacional de Investigaciones Científicas y Técnicas · ARUniversity of Potsdam · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antibodies against spike proteins of influenza are used as a tool for characterization of viruses and therapeutic approaches. However, development, production and quality control of antibodies is expensive and time consuming. To circumvent these difficulties, three peptides were derived from complementarity determining regions of an antibody heavy chain against influenza A spike glycoprotein. Their binding properties were studied experimentally, and by molecular dynamics simulations. Two peptide candidates showed binding to influenza A/Aichi/2/68 H3N2. One of them, termed PeB, with the highest affinity prevented binding to and infection of target cells in the micromolar region without any cytotoxic effect. PeB matches best the conserved receptor binding site of hemagglutinin. PeB bound also to other medical relevant influenza strains, such as human-pathogenic A/California/7/2009 H1N1, and avian-pathogenic A/Mute Swan/Rostock/R901/2006 H7N1. Strategies to improve the affinity and to adapt specificity are discussed and exemplified by a double amino acid substituted peptide, obtained by substitutional analysis. The peptides and their derivatives are of great potential for drug development as well as biosensing.

Indexed as

AnimalsAntibodies, NeutralizingAntibodies, ViralCell LineDogsEpitopesHemagglutinin Glycoproteins, Influenza VirusHumansInfluenza, HumanMolecular Dynamics SimulationVirus AttachmentAntibodies, NeutralizingAntibodies, ViralEpitopesHemagglutinin Glycoproteins, Influenza Virus

Identifiers

PMID27415624
PMCPMC4944999
OpenAlexW2462010702

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.