Evidence map›Paper›PMID 37715951›Full record

ArticleCell reports2023

A combination of two resistance mechanisms is critical for tick-borne encephalitis virus escape from a broadly neutralizing human antibody.

Pavel Svoboda, Jan Haviernik, Petr Bednar, Milos Matkovic, Tomás Cervantes Rincón, Jennifer Keeffe, Martin Palus, Jiri Salat, Marianna Agudelo, Michel C Nussenzweig and 3 more

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

5 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Tick-Borne Encephalitis (TBE): From Tick to Pathology.Journal of clinical medicine · 2023
    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

13 authors at 10 institutions in 5 countries.

Pavel SvobodaVeterinary Research Institute, Brno, Czech Republic; Institute of Parasitology, Biology Centre of the Czech Academy of Sciences, Ceske Budejovice, Czech Republic; Department of Experimental Biology, Faculty of Science, Masaryk University, Brno, Czech Republic; Department of Pharmacology and Pharmacy, Faculty of Veterinary Medicine, University of Veterinary Sciences, Brno, Czech Republic.
Jan HaviernikVeterinary Research Institute, Brno, Czech Republic; Department of Experimental Biology, Faculty of Science, Masaryk University, Brno, Czech Republic.
Petr BednarVeterinary Research Institute, Brno, Czech Republic; Department of Experimental Biology, Faculty of Science, Masaryk University, Brno, Czech Republic; Faculty of Science, University of South Bohemia, Ceske Budejovice, Czech Republic.
Milos MatkovicInstitute for Research in Biomedicine, Università della Svizzera Italiana, Bellinzona, Switzerland.
Tomás Cervantes RincónInstitute for Research in Biomedicine, Università della Svizzera Italiana, Bellinzona, Switzerland.
Jennifer KeeffeCalifornia Institute of Technology, Pasadena, CA, USA.
Martin PalusVeterinary Research Institute, Brno, Czech Republic; Institute of Parasitology, Biology Centre of the Czech Academy of Sciences, Ceske Budejovice, Czech Republic.
Jiri SalatVeterinary Research Institute, Brno, Czech Republic; Institute of Parasitology, Biology Centre of the Czech Academy of Sciences, Ceske Budejovice, Czech Republic.
Marianna AgudeloLaboratory of Molecular Immunology, The Rockefeller University, New York, NY, USA.
Michel C NussenzweigLaboratory of Molecular Immunology, The Rockefeller University, New York, NY, USA; Howard Hughes Medical Institute, New York, NY, USA.
Andrea CavalliInstitute for Research in Biomedicine, Università della Svizzera Italiana, Bellinzona, Switzerland; Swiss Institute of Bioinformatics, Lausanne, Switzerland.
Davide F RobbianiInstitute for Research in Biomedicine, Università della Svizzera Italiana, Bellinzona, Switzerland. Electronic address: drobbiani@irb.usi.ch.
Daniel RuzekVeterinary Research Institute, Brno, Czech Republic; Institute of Parasitology, Biology Centre of the Czech Academy of Sciences, Ceske Budejovice, Czech Republic; Department of Experimental Biology, Faculty of Science, Masaryk University, Brno, Czech Republic; Joint Faculty of Veterinary Medicine, Yamaguchi University, Yamaguchi City, Japan. Electronic address: ruzekd@paru.cas.cz.
Università della Svizzera italiana · CHInstitute of Parasitology of the Slovak Academy of Sciences · SKCalifornia Institute of Technology · USHoward Hughes Medical Institute · USMasaryk University · CZRockefeller University · USSewanee: The University of the South · USSIB Swiss Institute of Bioinformatics · CHUniversity of Veterinary Sciences Brno · CZYamaguchi University · JP

Funding

Understanding B cell memory in response to diverse virus infectionsU19AI111825 · NIAID · ROCKEFELLER UNIVERSITY · PI BOURNAZOS, STYLIANOS · 2014 to 2023
$26.0M
University of Washington Arboviral Research Network (UWARN)U01AI151698 · NIAID · UNIVERSITY OF WASHINGTON · PI Michael Gale, PETER MACGARR RABINOWITZ · 2020 to 2026
$13.3M
Virology CoreP01AI138938 · NIAID · ROCKEFELLER UNIVERSITY · PI NUSSENZWEIG, MICHEL C · 2018 to 2022
$8.4M
NIAID NIH HHS P01 AI138938NIAID NIH HHS U01 AI151698NIAID NIH HHS U19 AI111825
6 · The paper itself

Abstract

Tick-borne encephalitis virus (TBEV) is a flavivirus that causes human neuroinfections and represents a growing health problem. The human monoclonal antibody T025 targets envelope protein domain III (EDIII) of TBEV and related tick-borne flaviviruses, potently neutralizing TBEV in vitro and in preclinical models, representing a promising candidate for clinical development. We demonstrate that TBEV escape in the presence of T025 or T028 (another EDIII-targeting human monoclonal antibody) results in virus variants of reduced pathogenicity, characterized by distinct sets of amino acid changes in EDII and EDIII that are jointly needed to confer resistance. EDIII substitution K311N impairs formation of a salt bridge critical for T025-epitope interaction. EDII substitution E230K is not on the T025 epitope but likely induces quaternary rearrangements of the virus surface because of repulsion of positively charged residues on the adjacent EDI. A combination of T025 and T028 prevents virus escape and improves neutralization.

Indexed as

Encephalitis, Tick-BorneEncephalitis Viruses, Tick-BorneAntibodies, MonoclonalAntibodies, ViralEpitopesHumansAntibodies, MonoclonalAntibodies, ViralEpitopesCP: ImmunologyCP: Microbiologyescape mutantmonoclonal antibodyneutralizationtick-borne encephalitistick-borne encephalitis virus

Identifiers

PMID37715951
PMCPMC10591882
OpenAlexW4386809409

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.