Selection and Characterization of Single-Domain Antibodies for Detection of Lassa Nucleoprotein.

George P Anderson, Jinny L Liu, Lisa C Shriver-Lake, Ellen R Goldman

Open access · goldAbstract read

In one paragraph

Article in Antibodies (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing papers in PubMed

0.1field-weighted citation impact, top 47% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

Design, Production, Characterization, and Use of Peptide Antibodies.Antibodies (Basel, Switzerland) · 2023
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

4 authors at 1 institution in 1 country.

George P AndersonNaval Research Laboratory, Center for Biomolecular Science and Engineering, Washington, DC 20375, USA.ORCID 0000-0001-7545-9893

Jinny L LiuNaval Research Laboratory, Center for Biomolecular Science and Engineering, Washington, DC 20375, USA.

Lisa C Shriver-LakeNaval Research Laboratory, Center for Biomolecular Science and Engineering, Washington, DC 20375, USA.ORCID 0000-0002-9894-6640

Ellen R GoldmanNaval Research Laboratory, Center for Biomolecular Science and Engineering, Washington, DC 20375, USA.

United States Naval Research Laboratory · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lassa virus is the etiologic agent of Lassa fever, an acute and often fatal illness endemic to West Africa. It is important to develop new reagents applicable either for the specific diagnosis or as improved therapeutics for the treatment of Lassa fever. Here, we describe the development and initial testing of llama-derived single-domain antibodies that are specific for the Lassa virus nucleoprotein. Four sequence families based on complementarity-determining region (CDR) homology were identified by phage-based enzyme-linked immunosorbent assays, however, the highest affinity clones all belonged to the same sequence family which possess a second disulfide bond between Framework 2 and CDR3. The affinity and thermal stability were evaluated for each clone. A MagPlex-based homogeneous sandwich immunoassay for Lassa virus-like particles was also demonstrated to show their potential for further development as diagnostic reagents.

Indexed as

Arenaviridae familyLassa virusMagPlexsingle-domain antibody

Identifiers

PMID33348599

DOI10.3390/antib9040071

PMCPMC7768477

OpenAlexW3113370748

What OpenQuestion holds

Textmetadata

LicenceCC BY

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Registered trials

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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.