Evidence map›Paper›PMID 33586761›Full record

ArticleProtein engineering, design & selection : PEDS2021

Construction, characterization and crystal structure of a fluorescent single-chain Fv chimera.

Nileena Velappan, Devin Close, Li-Wei Hung, Leslie Naranjo, Colin Hemez, Natasha DeVore, Donna K McCullough, Antonietta M Lillo, Geoffrey S Waldo, Andrew R M Bradbury

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Protein engineering, design & selection : PEDS, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.4field-weighted citation impact, top 31% 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

4 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. 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 6 institutions in 1 country.

Nileena VelappanBioscience Division, Los Alamos National Laboratory, Los Alamos, NM 87545, USA.
Devin CloseARUP Laboratories, Institute for Clinical and Experimental Pathology, Salt Lake City, UT 84108, USA.
Li-Wei HungBioscience Division, Los Alamos National Laboratory, Los Alamos, NM 87545, USA.
Leslie NaranjoBioscience Division, Los Alamos National Laboratory, Los Alamos, NM 87545, USA.
Colin HemezGraduate Program in Biophysics, Harvard University, Boston, MA 02115 USA.
Natasha DeVoreChemistry Department, Missouri State University, Springfield, MO 65897, USA.
Donna K McCulloughMicrobiology Department, University of Tennessee, Knoxville, TN 37996, USA.
Antonietta M LilloBioscience Division, Los Alamos National Laboratory, Los Alamos, NM 87545, USA.
Geoffrey S WaldoBioscience Division, Los Alamos National Laboratory, Los Alamos, NM 87545, USA.
Andrew R M BradburySpecifica Inc., Santa Fe, NM 87505, USA.
Los Alamos National Laboratory · USARUP Laboratories (United States) · USHarvard University · USMissouri State University · USSpecifica (United States) · USUniversity of Tennessee at Knoxville · US

Funding

UNM TRAININGP50GM085273 · NIGMS · UNIVERSITY OF NEW MEXICO HEALTH SCIS CTR · PI EDWARDS, JEREMY S · 2009 to 2018
$26.1M
NIGMS NIH HHS P50 GM085273
6 · The paper itself

Abstract

In vitro display technologies based on phage and yeast have a successful history of selecting single-chain variable fragment (scFv) antibodies against various targets. However, single-chain antibodies are often unstable and poorly expressed in Escherichia coli. Here, we explore the feasibility of converting scFv antibodies to an intrinsically fluorescent format by inserting the monomeric, stable fluorescent protein named thermal green, between the light- and heavy-chain variable regions. Our results show that the scTGP format maintains the affinity and specificity of the antibodies, improves expression levels, allows one-step fluorescent assay for detection of binding and is a suitable reagent for epitope binning. We also report the crystal structure of an scTGP construct that recognizes phosphorylated tyrosine on FcεR1 receptor of the allergy pathway.

Indexed as

Single-Chain AntibodiesFluorescent DyesFluorescent DyesSingle-Chain Antibodiescrystal structureepitope binningimproved expression and functionalityintrinsically fluorescent scFv antibodiessoluble scFv antibodies

Identifiers

PMID33586761
PMCPMC7901706
OpenAlexW3133416963

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.