Evidence map›Paper›PMID 30602609›Full record

ArticleJournal of virology2019

Structural Basis of Nanobodies Targeting the Prototype Norovirus.

Kerstin Ruoff, Turgay Kilic, Jessica Devant, Anna Koromyslova, Alessa Ringel, Alexander Hempelmann, Celina Geiss, Juliane Graf, Michelle Haas, Imme Roggenbach and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of virology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.5field-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

22 citing papers in PubMed, 34 citations in OpenAlex.

  1. Review
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  8. Review
  9. INTRA- AND INTER-HOST EVOLUTION OF HUMAN NOROVIRUS IN HEALTHY ADULTS.bioRxiv : the preprint server for biology · 2024
    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

11 authors at 2 institutions in 1 country.

Kerstin Ruoff *Schaller Research Group at the University of Heidelberg and the DKFZ, Heidelberg, Germany.
Turgay Kilic *Schaller Research Group at the University of Heidelberg and the DKFZ, Heidelberg, Germany.
Jessica Devant *Schaller Research Group at the University of Heidelberg and the DKFZ, Heidelberg, Germany.
Anna KoromyslovaSchaller Research Group at the University of Heidelberg and the DKFZ, Heidelberg, Germany.
Alessa RingelMax Planck Institute for Molecular Genetics, Berlin, Germany.
Alexander HempelmannSchaller Research Group at the University of Heidelberg and the DKFZ, Heidelberg, Germany.
Celina GeissSchaller Research Group at the University of Heidelberg and the DKFZ, Heidelberg, Germany.
Juliane GrafSchaller Research Group at the University of Heidelberg and the DKFZ, Heidelberg, Germany.
Michelle HaasSchaller Research Group at the University of Heidelberg and the DKFZ, Heidelberg, Germany.
Imme RoggenbachSchaller Research Group at the University of Heidelberg and the DKFZ, Heidelberg, Germany.
Grant HansmanSchaller Research Group at the University of Heidelberg and the DKFZ, Heidelberg, Germany g.hansman@dkfz.de.ORCID 0000-0001-8735-4618
Heidelberg University · DEMax Planck Institute for Molecular Genetics · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human norovirus infections are a major disease burden. In this study, we analyzed three new norovirus-specific Nanobodies that interacted with the prototype human norovirus (i.e., genogroup I genotype 1 [GI.1]). We showed that the Nanobodies bound on the side (Nano-7 and Nano-62) and top (Nano-94) of the capsid-protruding (P) domain using X-ray crystallography. Nano-7 and Nano-62 bound at a similar region on the P domain, but the orientations of these two Nanobodies clashed with the shell (S) domain and neighboring P domains on intact particles. This finding suggested that the P domains on the particles should shift in order for Nano-7 and Nano-62 to bind to intact particles. Interestingly, both Nano-7 and Nano-94 were capable of blocking norovirus virus-like particles (VLPs) from binding to histo-blood group antigens (HBGAs), which are important cofactors for norovirus infection. Previously, we showed that the GI.1 HBGA pocket could be blocked with the soluble human milk oligosaccharide 2-fucosyllactose (2'FL). In the current study, we showed that a combined treatment of Nano-7 or Nano-94 with 2'FL enhanced the blocking potential with an additive (Nano-7) or synergistic (Nano-94) effect. We also found that GII Nanobodies with 2'FL also enhanced inhibition. The Nanobody inhibition likely occurred by different mechanisms, including particle aggregation or particle disassembly, whereas 2'FL blocked the HBGA binding site. Overall, these new data showed that the positive effect of the addition of 2'FL was not limited to a single mode of action of Nanobodies or to a single norovirus genogroup.

Indexed as

Binding SitesBlood Group AntigensCaliciviridae InfectionsCapsidCapsid ProteinsCrystallography, X-RayEpitopesEscherichia coliNorovirusProtein BindingSingle-Domain AntibodiesBlood Group AntigensCapsid ProteinsEpitopesSingle-Domain AntibodiesnorovirusX-ray crystallography

Identifiers

PMID30602609
PMCPMC6401464
OpenAlexW2908300215

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.