Evidence map›Paper›PMID 32326443›Full record

ArticleAntibodies (Basel, Switzerland)2020

Exploration and Modulation of Antibody Fragment Biophysical Properties by Replacing the Framework Region Sequences.

Thomas Cnudde, Zineb Lakhrif, Justine Bourgoin, Fanny Boursin, Catherine Horiot, Corinne Henriquet, Anne di Tommaso, Matthieu Olivier Juste, Isabella Gizzi Jiacomini, Isabelle Dimier-Poisson and 3 more

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. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.4field-weighted citation impact, top 34% 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

0 citing papers in PubMed, 5 citations in OpenAlex.

No citing paper in PubMed yet.

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

13 authors at 3 institutions in 2 countries.

Thomas CnuddeINRAE, ISP, Université de Tours, F-37000 Tours, France.
Zineb LakhrifINRAE, ISP, Université de Tours, F-37000 Tours, France.
Justine BourgoinINRAE, ISP, Université de Tours, F-37000 Tours, France.
Fanny BoursinINRAE, ISP, Université de Tours, F-37000 Tours, France.
Catherine HoriotINRAE, ISP, Université de Tours, F-37000 Tours, France.
Corinne HenriquetIRCM, Institut de Recherche en Cancérologie de Montpellier, INSERM, U1194, Université Montpellier, ICM Institut Régional du Cancer, 34090 Montpellier, France.ORCID 0000-0002-6210-5794
Anne di TommasoINRAE, ISP, Université de Tours, F-37000 Tours, France.
Matthieu Olivier JusteINRAE, ISP, Université de Tours, F-37000 Tours, France.
Isabella Gizzi JiacominiLaboratório de Imunoquímica, Departamento de Patologia Básica, Universidade Federal do Paraná, Curitiba 81530, PR, Brazil.ORCID 0000-0002-8367-8524
Isabelle Dimier-PoissonINRAE, ISP, Université de Tours, F-37000 Tours, France.
Martine PugnièreIRCM, Institut de Recherche en Cancérologie de Montpellier, INSERM, U1194, Université Montpellier, ICM Institut Régional du Cancer, 34090 Montpellier, France.ORCID 0000-0002-2049-2909
Marie-Nöelle MévélecINRAE, ISP, Université de Tours, F-37000 Tours, France.
Nicolas AubreyINRAE, ISP, Université de Tours, F-37000 Tours, France.ORCID 0000-0003-3211-0186
Université de Tours · FRInserm · FRUniversidade Federal do Paraná · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In order to increase the successful development of recombinant antibodies and fragments, it seems fundamental to enhance their expression and/or biophysical properties, such as the thermal, chemical, and pH stabilities. In this study, we employed a method bases on replacing the antibody framework region sequences, in order to promote more particularly single-chain Fragment variable (scFv) product quality. We provide evidence that mutations of the VH- C-C' loop might significantly improve the prokaryote production of well-folded and functional fragments with a production yield multiplied by 27 times. Additional mutations are accountable for an increase in the thermal (+19.6 °C) and chemical (+1.9 M) stabilities have also been identified. Furthermore, the hereby-produced fragments have shown to remain stable at a pH of 2.0, which avoids molecule functional and structural impairments during the purification process. Lastly, this study provides relevant information to the understanding of the relationship between the antibodies amino acid sequences and their respective biophysical properties.

Indexed as

engineeringframework regionsproductionProtein L (PpL)single-chain Fragment variable (scFv)stabilities

Identifiers

PMID32326443
PMCPMC7344962
OpenAlexW3016884847

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.