Evidence map›Paper›PMID 22412927›Full record

ArticlePloS one2012

Rugged single domain antibody detection elements for Bacillus anthracis spores and vegetative cells.

Scott A Walper, George P Anderson, P Audrey Brozozog Lee, Richard H Glaven, Jinny L Liu, Rachel D Bernstein, Dan Zabetakis, Linwood Johnson, Jill M Czarnecki, Ellen R Goldman

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 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

15 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
  2. Review
  3. Rapid Microscopic Detection ofMicroorganisms · 2020
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Improving the biophysical properties of anti-ricin single-domain antibodies.Biotechnology reports (Amsterdam, Netherlands) · 2015
    Article
  11. S-layers: principles and applications.FEMS microbiology reviews · 2014
    Article
  12. Article
  13. Article
  14. Article
  15. 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 4 institutions in 1 country.

Scott A WalperNaval Research Laboratory, Washington D. C., United States of America.
George P Anderson
P Audrey Brozozog Lee
Richard H Glaven
Jinny L Liu
Rachel D Bernstein
Dan Zabetakis
Linwood Johnson
Jill M Czarnecki
Ellen R Goldman
Naval Research Laboratory Center for Bio/Molecular Science and EngineeringNova Research Company (United States) · USNaval Medical Research Command · USUnited States Naval Research Laboratory · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Significant efforts to develop both laboratory and field-based detection assays for an array of potential biological threats started well before the anthrax attacks of 2001 and have continued with renewed urgency following. While numerous assays and methods have been explored that are suitable for laboratory utilization, detection in the field is often complicated by requirements for functionality in austere environments, where limited cold-chain facilities exist. In an effort to overcome these assay limitations for Bacillus anthracis, one of the most recognizable threats, a series of single domain antibodies (sdAbs) were isolated from a phage display library prepared from immunized llamas. Characterization of target specificity, affinity, and thermal stability was conducted for six sdAb families isolated from rounds of selection against the bacterial spore. The protein target for all six sdAb families was determined to be the S-layer protein EA1, which is present in both vegetative cells and bacterial spores. All of the sdAbs examined exhibited a high degree of specificity for the target bacterium and its spore, with affinities in the nanomolar range, and the ability to refold into functional antigen-binding molecules following several rounds of thermal denaturation and refolding. This research demonstrates the capabilities of these sdAbs and their potential for integration into current and developing assays and biosensors.

Indexed as

Amino Acid SequenceAnthraxAntibodies, BacterialAntibody AffinityAntibody SpecificityBacillus anthracisHumansImmunoassayKineticsMolecular Sequence DataProtein StabilitySequence AlignmentSingle-Chain AntibodiesSpores, BacterialTemperatureAntibodies, BacterialSingle-Chain Antibodies

Identifiers

PMID22412927
PMCPMC3295763
OpenAlexW2013003092

What OpenQuestion holds

Textmetadata
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.