Designing a Multi-Epitope Antigen for Serodiagnosis of Strongyloides stercoralis  Based on L3Nie.01 and IgG Immunoreactive Epitopes

Ahmad  Movahedpour; Zohreh Mostafavi-Pour; Bahador  Sarkari; Mortaza Taheri-Anganeh; Navid  Nezafat; Amir  Savardashtaki; Younes  Ghasemi

doi:10.18502/ajmb.v14i2.8886

Ahmad Movahedpour Department of Medical Biotechnology, School of Advanced Medical Sciences and Technologies, Shiraz University of Medical Sciences Shiraz, Iran
Zohreh Mostafavi-Pour Recombinant Protein Laboratory, Department of Biochemistry, School of Medicine, Shiraz University of Medical Sciences, Shiraz, Iran
Bahador Sarkari Department of Parasitology and Mycology, School of Medicine, Shiraz University of Medical Sciences, Shiraz, Iran
Mortaza Taheri-Anganeh Cellular and Molecular Research Center, Cellular and Molecular Medicine Institute, Urmia University of Medical Sciences, Urmia, Iran
Navid Nezafat Pharmaceutical Sciences Research Center, Shiraz University of Medical Science, Shiraz, Iran
Amir Savardashtaki Department of Medical Biotechnology, School of Advanced Medical Sciences and Technologies, Shiraz University of Medical Sciences Shiraz, Iran
Younes Ghasemi Pharmaceutical Sciences Research Center, Shiraz University of Medical Science, Shiraz, Iran

DOI: https://doi.org/10.18502/ajmb.v14i2.8886

Keywords: Antigens, Multi-epitopes, Serological diagnosis, Strongyloides stercoralis

Abstract

Background: Serological diagnosis of Strongyloides stercoralis (S. stercoralis) is frequently challenging because of cross-reactivity with other parasitic nematodes. Therefore, it is necessary to introduce novel serological tests with high performance to properly diagnose this neglected parasitic infection. The purpose of the current study was to design a multi-epitope construct for the diagnosis of S. stercoralis.

Methods: For the purpose of this study, first, highly antigenic segments and potential immunodominant epitopes of S. stercoralis were identified from two antigenic proteins, and then all of the selected parts were linked by an appropriate linker. Next, the physico-chemical features of the designed construct were analyzed. Then, tertiary structures of the construct were built and evaluated to find out the best one. Lastly, the amino acid sequence was reverse-translated and optimized for over-expression in Escherchia coli (E. coli).

Results: The bioinformatic evaluation indicated that the designed protein construct could be hydrophilic, thermostable, and acidic and the estimated half-life was more than 10 hr in E. coli.

Conclusion: According to the results of the study, the designed construct could be used as an efficient antigen in the ELISA system for serological diagnosis of human strongyloidiasis.