Evidence map›Paper›PMID 18947189›Full record

ArticleAnalytical chemistry2008

Thermostable llama single domain antibodies for detection of botulinum A neurotoxin complex.

Ellen R Goldman, George P Anderson, Jerry Conway, Laura J Sherwood, Melissa Fech, BaoHan Vo, Jinny L Liu, Andrew Hayhurst

Abstract read
In one paragraph

Article in Analytical chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
4.2field-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

20 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Single Domain Antibodies as New Biomarker Detectors.Diagnostics (Basel, Switzerland) · 2017
    Review
  5. Review
  6. Article
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  8. Review
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  10. Article
  11. Electrochemical sensing of cortisol: a recent update.Applied biochemistry and biotechnology · 2014
    Review
  12. Article
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  14. 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

8 authors at 2 institutions in 1 country.

Ellen R GoldmanCenter for Bio/Molecular Science and Engineering, U.S. Naval Research Laboratory, 4555 Overlook Avenue SW, Washington, DC 20375, USA. ellen.goldman@nrl.navy.mil
George P Anderson
Jerry Conway
Laura J Sherwood
Melissa Fech
BaoHan Vo
Jinny L Liu
Andrew Hayhurst
Texas Biomedical Research Institute · USClark Atlanta University · US

Funding

EXTRAMURAL RESEARCH FACILITIES CONSTRUCTIONC06RR012087 · NCRR · SOUTHWEST FOUNDATION FOR BIOMEDICAL RES · PI VANDEBERG, JOHN L · 1996 to 1996
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NCRR NIH HHS C06 RR012087NCRR NIH HHS C06 RR12087
6 · The paper itself

Abstract

Immunoglobulins from animals of the Camelidae family boast unique forms that do not incorporate light chains. Antigen binding in these unconventional heavy-chain homodimers is mediated through a single variable domain. When expressed recombinantly these variable domains are termed single domain antibodies (sdAb) and are among the smallest naturally IgG-derived antigen binding units. SdAb possess good solubility, thermostability, and can refold after heat and chemical denaturation making them promising alternative recognition elements. We have constructed a library of phage-displayed sdAb from a llama immunized with a cocktail of botulinum neurotoxin (BoNT) complex toxoids and panned the library for binders for BoNT A complex toxoid. Six unique binders were isolated and found to specifically bind BoNT A complex in toxoid and untoxoided forms and when used in optimal combinations in buffer and milk could detect 100 pg/mL untoxoided complex. All sdAb retained their ability to specifically bind target after heating to 85 degrees C for 1 h, in contrast to conventional polyclonal sera. All of the sdAb were highly specific for subtype A1 rather than A2 and demonstrated binding to the 33 kDa hemagglutinin, potentially to a somewhat overlapping linear epitope. The unique properties of these sdAb may provide advantages for many diagnostic applications where long-term storage and in-line monitoring require very rugged yet highly specific recognition elements.

Indexed as

Amino Acid SequenceAnimalsAntibodiesAntibody AffinityAntibody SpecificityBotulinum Toxins, Type ACamelids, New WorldEpitopesMolecular Sequence DataProtein StabilitySerotypingSolubilityTemperatureToxoidsAntibodiesBotulinum Toxins, Type AEpitopesToxoids

Identifiers

PMID18947189
PMCPMC2829253
OpenAlexW2083811176

What OpenQuestion holds

Textmetadata
LicenceTDM
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.