Evidence map›Paper›PMID 36422036›Full record

ArticleJournal of fungi (Basel, Switzerland)2022

Recombinant Expression in

Jesús Borrego, Muhammad Umair Naseem, Al Nasar Ahmed Sehgal, Lipsa Rani Panda, Kashmala Shakeel, Attila Gaspar, Cynthia Nagy, Zoltan Varga, Gyorgy Panyi

Open access · goldAbstract read
In one paragraph

Article in Journal of fungi (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.3field-weighted citation impact, top 47% 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

6 citing papers in PubMed, 4 citations in OpenAlex.

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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

9 authors at 1 institution in 1 country.

Jesús BorregoDepartment of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.
Muhammad Umair NaseemDepartment of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.ORCID 0000-0003-3849-6219
Al Nasar Ahmed SehgalDepartment of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.
Lipsa Rani PandaDepartment of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.ORCID 0000-0001-7113-1794
Kashmala ShakeelDepartment of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.ORCID 0000-0002-4284-6640
Attila GasparDepartment of Inorganic and Analytical Chemistry, Faculty of Science and Technology, Institute of Chemistry, University of Debrecen, 4032 Debrecen, Hungary.ORCID 0000-0002-0172-2393
Cynthia NagyDepartment of Inorganic and Analytical Chemistry, Faculty of Science and Technology, Institute of Chemistry, University of Debrecen, 4032 Debrecen, Hungary.
Zoltan VargaDepartment of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.ORCID 0000-0003-1892-6840
Gyorgy PanyiDepartment of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.ORCID 0000-0001-6227-3301
University of Debrecen · HU

Funding

Hungarian National Research, Development, and Innovation Office K143071Stipendium Hungaricum Scholarship by the Tempus Public Foundation SHE-21297-002/2018
6 · The paper itself

Abstract

The Kv1.3 channel has become a therapeutic target for the treatment of various diseases. Several Kv1.3 channel blockers have been characterized from scorpion venom; however, extensive studies require amounts of toxin that cannot be readily obtained directly from venoms. The Pichia pastoris expression system provides a cost-effective approach to overcoming the limitations of chemical synthesis and E. coli recombinant expression. In this work, we developed an efficient system for the production of three potent Kv1.3 channel blockers from different scorpion venoms: Vm24, AnTx, and Ts6. Using the Pichia system, these toxins could be obtained in sufficient quantities (Vm24 1.6 mg/L, AnTx 46 mg/L, and Ts6 7.5 mg/L) to characterize their biological activity. A comparison was made between the activity of tagged and untagged recombinant peptides. Tagged Vm24 and untagged AnTx are nearly equivalent to native toxins in blocking Kv1.3 (Kd = 4.4 pM and Kd = 0.72 nM, respectively), whereas untagged Ts6 exhibits a 53-fold increase in Kd (Kd = 29.1 nM) as compared to the native peptide. The approach described here provides a method that can be optimized for toxin production to develop more selective and effective Kv1.3 blockers with therapeutic potential.

Indexed as

Kv1.3 blockersPichia pastorisrecombinant peptidesscorpion venoms

Identifiers

PMID36422036
PMCPMC9697831
OpenAlexW4309604972

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.