Structural Prediction and Antigenic Analysis of ROP18, MIC4, and SAG1 Proteins to Improve Vaccine Design against Toxoplasma gondii: An In silico Approach.

Autor:	Nayeri T; Infectious and Tropical Diseases Research Center, Dezful University of Medical Sciences, Dezful, Iran., Sarvi S; Department of Parasitology, School of Medicine, Mazandaran University of Medical Sciences, Sari, Iran.; Toxoplasmosis Research Center, Mazandaran University of Medical Sciences, Sari, Iran., Fasihi-Ramandi M; Molecular Biology Research Center, Baqiyatallah University of Medical Sciences, Tehran, Iran., Asgarian-Omran H; Immunology Department, Faculty of Medicine, Mazandaran University of Medical Sciences, Sari, Iran., Ajami A; Immunology Department, Faculty of Medicine, Mazandaran University of Medical Sciences, Sari, Iran., Hosseininejad Z; Department of Parasitology, School of Medicine, Mazandaran University of Medical Sciences, Sari, Iran.; Toxoplasmosis Research Center, Mazandaran University of Medical Sciences, Sari, Iran., Dodangeh S; Qazvin University of Medical Sciences Department of Medical Parasitology and Mycology, Medical Microbiology Research Center, Qazvin University of Medical Sciences, Qazvin, Iran Sari Iran., Daryani A; Department of Parasitology, School of Medicine, Mazandaran University of Medical Sciences, Sari, Iran.; Toxoplasmosis Research Center, Mazandaran University of Medical Sciences, Sari, Iran.
Jazyk:	angličtina
Zdroj:	Infectious disorders drug targets [Infect Disord Drug Targets] 2024 Sep 30. Date of Electronic Publication: 2024 Sep 30.
DOI:	10.2174/0118715265332103240911113422
Abstrakt:	Background: Toxoplasmosis is a cosmopolitan infectious disease in warm-blooded mammals that poses a serious worldwide threat due to the lack of effective medications and vaccines. Aims: The purpose of this study was to design a multi-epitope vaccine using several bioinfor-matics approaches against the antigens of Toxoplasma gondii (T. gondii). Methods: Three proteins of T. gondii, including ROP18, MIC4, and SAG1, were analyzed to predict the most dominant B- and T-cell epitopes. Finally, we designed a chimeric immunogen RMS (ROP18, MIC4, and SAG1) using some domains of ROP18 (N377-E546), MIC4 (D302-G471), and SAG1 (T130-L299) linked by rigid linker A (EAAAK) A. Physicochemical prop-erties, secondary and tertiary structures, antigenicity, and allergenicity of RMS were predicted utilizing immunoinformatic tools and servers. Results: RMS protein had 545 amino acids with a molecular weight (MW) of 58,833.46 Da and a theoretical isoelectric point (IP) of 6.47. The secondary structure of RMS protein con-tained 21.28% alpha-helix, 24.59% extended strand, and 54.13% random coil. In addition, eval-uation of antigenicity and allergenicity showed the protein to be an immunogen and non-aller-gen. The results of the Ramachandran plot indicated that 76.4%, 12.9%, and 10.7% of amino acid residues were incorporated in the favored, allowed, and outlier regions, respectively. ΔG of the best-predicted mRNA secondary structure was -593.80 kcal/mol, which indicated that a stable loop was not formed at the 5' end. Conclusion: Finally, the accuracy and precision of the in silico analysis must be confirmed by successful heterologous expression and experimental studies. (Copyright© Bentham Science Publishers; For any queries, please email at epub@benthamscience.net.)
Databáze:	MEDLINE
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