Evidence map›Paper›PMID 22438910›Full record

ArticlePloS one2012

Llama antibody fragments recognizing various epitopes of the CD4bs neutralize a broad range of HIV-1 subtypes A, B and C.

Nika Strokappe, Agnieszka Szynol, Marlèn Aasa-Chapman, Andrea Gorlani, Anna Forsman Quigley, David Lutje Hulsik, Lei Chen, Robin Weiss, Hans de Haard, Theo Verrips

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

44 citing papers in PubMed, 66 citations in OpenAlex.

  1. Review
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  19. Single Domain Antibodies as New Biomarker Detectors.Diagnostics (Basel, Switzerland) · 2017
    Review
  20. 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 5 institutions in 4 countries.

Nika StrokappeBiomolecular Imaging, Department Biology, Faculty of Science, Utrecht University, Utrecht, The Netherlands.
Agnieszka Szynol
Marlèn Aasa-Chapman
Andrea Gorlani
Anna Forsman Quigley
David Lutje Hulsik
Lei Chen
Robin Weiss
Hans de Haard
Theo Verrips
Utrecht University · NLUniversity College London · GBMRC Laboratory for Molecular Cell Biology · GBNational Institute of Allergy and Infectious Diseases · USUniversité Joseph Fourier · FR

Funding

Medical Research Council G0801176
6 · The paper itself

Abstract

Many of the neutralising antibodies, isolated to date, display limited activities against the globally most prevalent HIV-1 subtypes A and C. Therefore, those subtypes are considered to be an important target for antibody-based therapy. Variable domains of llama heavy chain antibodies (VHH) have some superior properties compared with classical antibodies. Therefore we describe the application of trimeric forms of envelope proteins (Env), derived from HIV-1 of subtype A and B/C, for a prolonged immunization of two llamas. A panel of VHH, which interfere with CD4 binding to HIV-1 Env were selected with use of panning. The results of binding and competition assays to various Env, including a variant with a stabilized CD4-binding state (gp120(Ds2)), cross-competition experiments, maturation analysis and neutralisation assays, enabled us to classify the selected VHH into three groups. The VHH of group I were efficient mainly against viruses of subtype A, C and B'/C. The VHH of group II resemble the broadly neutralising antibody (bnmAb) b12, neutralizing mainly subtype B and C viruses, however some had a broader neutralisation profile. A representative of the third group, 2E7, had an even higher neutralization breadth, neutralizing 21 out of the 26 tested strains belonging to the A, A/G, B, B/C and C subtypes. To evaluate the contribution of certain amino acids to the potency of the VHH a small set of the mutants were constructed. Surprisingly this yielded one mutant with slightly improved neutralisation potency against 92UG37.A9 (subtype A) and 96ZM651.02 (subtype C). These findings and the well-known stability of VHH indicate the potential application of these VHH as anti-HIV-1 microbicides.

Indexed as

Antibodies, NeutralizingHIV AntibodiesAmino Acid SequenceAmino Acid SubstitutionAnimalsBinding, CompetitiveCamelids, New WorldCD4 AntigensComplementarity Determining RegionsCross Reactionsenv Gene Products, Human Immunodeficiency VirusEpitopesHIV-1HIV Envelope Protein gp120HumansImmunizationAntibodies, NeutralizingCD4 AntigensComplementarity Determining Regionsenv Gene Products, Human Immunodeficiency VirusEpitopesgp120 protein, Human immunodeficiency virus 1gp140 envelope protein, Human immunodeficiency virus 1HIV AntibodiesHIV Envelope Protein gp120Immunoglobulin Heavy ChainsImmunoglobulin Variable Region

Identifiers

PMID22438910
PMCPMC3305327
OpenAlexW1980758834

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.