Evidence map›Paper›PMID 26267898›Full record

ArticlePloS one2015

Llama nanoantibodies with therapeutic potential against human norovirus diarrhea.

Lorena Garaicoechea, Andrea Aguilar, Gabriel I Parra, Marina Bok, Stanislav V Sosnovtsev, Gabriela Canziani, Kim Y Green, Karin Bok, Viviana Parreño

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.3field-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

28 citing papers in PubMed, 46 citations in OpenAlex.

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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

9 authors at 3 institutions in 2 countries.

Lorena GaraicoecheaInstituto de Virología, INTA, Castelar, Buenos Aires, Argentina.
Andrea AguilarInstituto de Virología, INTA, Castelar, Buenos Aires, Argentina.
Gabriel I ParraLaboratory of Infectious Diseases, NIAID, National Institutes of Health, Bethesda, Maryland, United States of America.
Marina BokInstituto de Virología, INTA, Castelar, Buenos Aires, Argentina.
Stanislav V SosnovtsevLaboratory of Infectious Diseases, NIAID, National Institutes of Health, Bethesda, Maryland, United States of America.
Gabriela CanzianiInstituto Leloir, Buenos Aires, Argentina.
Kim Y GreenLaboratory of Infectious Diseases, NIAID, National Institutes of Health, Bethesda, Maryland, United States of America.
Karin BokLaboratory of Infectious Diseases, NIAID, National Institutes of Health, Bethesda, Maryland, United States of America.
Viviana ParreñoInstituto de Virología, INTA, Castelar, Buenos Aires, Argentina.
National Institutes of Health · USFundación Instituto Leloir · ARNational Institute of Allergy and Infectious Diseases · US

Funding

Noroviruses and Epidemic GastroenteritisZIAAI000897 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI GREEN, KIM Y. · 2009 to 2025
$29.6M
Intramural NIH HHS
6 · The paper itself

Abstract

Noroviruses are a major cause of acute gastroenteritis, but no vaccines or therapeutic drugs are available. Llama-derived single chain antibody fragments (also called VHH) are small, recombinant monoclonal antibodies of 15 kDa with several advantages over conventional antibodies. The aim of this study was to generate recombinant monoclonal VHH specific for the two major norovirus (NoV) genogroups (GI and GII) in order to investigate their potential as immunotherapy for the treatment of NoV diarrhea. To accomplish this objective, two llamas were immunized with either GI.1 (Norwalk-1968) or GII.4 (MD2004) VLPs. After immunization, peripheral blood lymphocytes were collected and used to generate two VHH libraries. Using phage display technology, 10 VHH clones specific for GI.1, and 8 specific for GII.4 were selected for further characterization. All VHH recognized conformational epitopes in the P domain of the immunizing VP1 capsid protein, with the exception of one GII.4 VHH that recognized a linear P domain epitope. The GI.1 VHHs were highly specific for the immunizing GI.1 genotype, with only one VHH cross-reacting with GI.3 genotype. The GII.4 VHHs reacted with the immunizing GII.4 strain and showed a varying reactivity profile among different GII genotypes. One VHH specific for GI.1 and three specific for GII.4 could block the binding of homologous VLPs to synthetic HBGA carbohydrates, saliva, and pig gastric mucin, and in addition, could inhibit the hemagglutination of red blood cells by homologous VLPs. The ability of Nov-specific VHHs to perform well in these surrogate neutralization assays supports their further development as immunotherapy for NoV treatment and immunoprophylaxis.

Indexed as

AnimalsAntibodies, MonoclonalAntibody SpecificityCamelids, New WorldCapsid ProteinsCell Surface Display TechniquesDiarrheaEpitope MappingEpitopesGastroenteritisGene LibraryHemagglutination Inhibition TestsHumansImmune SeraImmunizationImmunization, PassiveAntibodies, MonoclonalCapsid ProteinsEpitopesImmune SeraRecombinant ProteinsSingle-Chain Antibodies

Identifiers

PMID26267898
PMCPMC4534396
OpenAlexW2283062553

What OpenQuestion holds

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LicenceCC0
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.