Evidence map›Paper›PMID 25246715›Full record

ArticleThe Korean journal of parasitology2014

High expression of water-soluble recombinant antigenic domains of Toxoplasma gondii secretory organelles.

Zhaoshou Yang, Hye-Jin Ahn, Ho-Woo Nam

Abstract read
In one paragraph

Article in The Korean journal of parasitology, 2014. 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
–field-weighted citation impact
1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

  1. Review
  2. Article
  3. TheBiology open · 2019
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4 · The record

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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

3 authors.

Zhaoshou YangDepartment of Parasitology, College of Medicine, The Catholic University of Korea, Seoul 137-701, Korea.
Hye-Jin AhnDepartment of Parasitology, College of Medicine, The Catholic University of Korea, Seoul 137-701, Korea.
Ho-Woo NamDepartment of Parasitology, College of Medicine, The Catholic University of Korea, Seoul 137-701, Korea.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recombinant antigenic proteins of Toxoplasma gondii are alternative source of antigens which are easily obtainable for serodiagnosis of toxoplasmosis. In this study, highly antigenic secretory organellar proteins, dense granular GRA2 and GRA3, rhoptrial ROP2, and micronemal MIC2, were analyzed by bioinformatics approach to express as water-soluble forms of antigenic domains. The transmembrane region and disorder tendency of 4 secretory proteins were predicted to clone the genes into pGEX-4T-1 vector. Recombinant plasmids were transformed into BL21 (DE3) pLysS E. coli, and GST fusion proteins were expressed with IPTG. As a result, GST fusion proteins with GRA225-105, GRA339-138, ROP2324-561, and MIC21-284 domains had respectively higher value of IgG avidity. The rGST-GRA225-105 and rGST-GRA339-138 were soluble, while rGST-ROP2324-561 and rGST-MIC21-284 were not. GRA231-71, intrinsically unstructured domain (IUD) of GRA2, was used as a linker to enhance the solubility. The rGST-GRA231-71-ROP2324-561, a chimeric protein, appeared to be soluble. Moreover, rGST-GRA231-71-MIC21-284 was also soluble and had higher IgG avidity comparing to rGST-MIC21-284. These 4 highly expressed and water-soluble recombinant antigenic proteins may be promising candidates to improve the serodiagnosis of toxoplasmosis in addition to the major surface antigen of SAG1.

Indexed as

Antigens, ProtozoanGene ExpressionRecombinant ProteinsAnimalsAntibodies, ProtozoanAntibody AffinityImmunoglobulin GMice, Inbred BALB CSerologic TestsSolubilityToxoplasmaToxoplasmosisAntibodies, ProtozoanAntigens, ProtozoanImmunoglobulin GRecombinant Proteinsantigenic domainbioinformaticsGRA2GRA3IgG avidityintrinsically unstructured domainMIC2ROP2Toxoplasma gondii

Identifiers

PMID25246715
PMCPMC4170032

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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.