Evidence map›Paper›PMID 36214056›Full record

ArticleProtein science : a publication of the Protein Society2022

The production of recombinant platelet-derived growth factor D using the second generation modified vaccinia Ankara viral system.

Abdo J Najy, Tri Pham, Karine Pradeau-Aubreton, Robert Drillien, Hyeong-Reh C Kim

Open access · hybridAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.4field-weighted citation impact, top 32% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. 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

5 authors at 2 institutions in 2 countries.

Abdo J NajyDepartment of Pathology, Barbara Ann Karmanos Institute, Wayne State University School of Medicine, Detroit, Michigan, USA.
Tri PhamDepartment of Pathology, Barbara Ann Karmanos Institute, Wayne State University School of Medicine, Detroit, Michigan, USA.
Karine Pradeau-AubretonInstitut de Génétique et de Biologie Moléculaire et Cellulaire, INSERM U596/CNRS-UMR7104, Université Louis Pasteur, Strasbourg, France.
Robert DrillienInstitut de Génétique et de Biologie Moléculaire et Cellulaire, INSERM U596/CNRS-UMR7104, Université Louis Pasteur, Strasbourg, France.
Hyeong-Reh C KimDepartment of Pathology, Barbara Ann Karmanos Institute, Wayne State University School of Medicine, Detroit, Michigan, USA.ORCID 0000-0002-7960-0580
Wayne State University · USCentre National de la Recherche Scientifique · FR

Funding

PDGF D AND PROSTATE CANCER BONE METASTASISR01CA123362 · NCI · WAYNE STATE UNIVERSITY · PI KIM, HYEONG-REH CHOI · 2010 to 2020
$3.1M
NCI NIH HHS R01 CA123362NCI NIH HHS RO1CA123362
6 · The paper itself

Abstract

The vaccinia virus expression system is known for the efficient production of recombinant proteins with "appropriate" posttranslational modification using desired mammalian cell lines. However, being a replication competent virus, vaccinia virus poses a health threat to immunocompromised individuals and requires biosafety level 2 (BSL2) laboratory precautions, thereby restricting its use by the scientific community. Development of the host range restricted modified vaccinia Ankara (MVA) system has allowed researchers to work with a safer virus even at BSL1. Here, we report on the use of an improved second generation MVA viral system incorporating two selective markers and fluorescent proteins for easier recombinant virus identification. Notably, we demonstrate that this novel system is capable of producing secreted recombinant proteins, a finding not previously reported. Through purification and characterization of wild type and mutant platelet-derived growth factor D (PDGF D) dimer species, we demonstrate this system is capable of producing the latent full-length PDGF D dimer, partially processed intermediate dimer (hemidimer), as well as fully processed growth factor domain dimer that show chemical integrity and biological activity. Importantly, this system is amenable to scaling up for the mass production of recombinant PDGF D (rPDGF D) dimer species.

Indexed as

VacciniaVaccinia virusAnimalsHumansMammalsPlatelet-Derived Growth FactorRecombinant ProteinsVirus ReplicationPlatelet-Derived Growth FactorRecombinant Proteinsfull-length dimergrowth factor domain dimerhemidimerMVAPDGF Drecombinant protein

Identifiers

PMID36214056
PMCPMC9601800
OpenAlexW4303986468

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.