Investigate the immunogenic and protective effect of trivalent chimeric protein containing IpaD-StxB-TolC antigens as a vaccine candidate against S. dysenteri and S. flexneri.


Journal

Microbial pathogenesis
ISSN: 1096-1208
Titre abrégé: Microb Pathog
Pays: England
ID NLM: 8606191

Informations de publication

Date de publication:
May 2023
Historique:
received: 07 12 2022
revised: 08 03 2023
accepted: 09 03 2023
medline: 11 4 2023
pubmed: 17 3 2023
entrez: 16 3 2023
Statut: ppublish

Résumé

Shigella spp. causes bloody diarrhea and leads to death, especially in children. Chimeric proteins containing virulence factors can prevent Shigella infection. The purpose of this study is to investigate the immunogenic and protective effect of trivalent chimeric protein containing IpaD-StxB-TolC antigens against shiga toxin, S. dysenteri and S. flexneri in vitro and in vivo conditions. Recombinant vector was transferred to E. coli BL21. The expression of the chimeric protein was confirmed by SDS PAGE and purified using the Ni-NTA column. Mice were immunized with recombinant protein and antibody titer was evaluated by ELISA. 10, 25 and 50 LD The expression and purification of the recombinant protein with 60.6 kDa was done. ELISA showed increased antibody titer against the chimeric protein. MTT assay indicated that 1/8000 dilution of the sera had a 51% of cell viability against the toxin in Vero cell line. The challenge of mice immunized with toxin showed that the mice had complete protection against 10 and 25 LD This study showed that chimeric proteins can create favorable immunogenicity in the host as vaccine candidates.

Sections du résumé

BACKGROUNDS BACKGROUND
Shigella spp. causes bloody diarrhea and leads to death, especially in children. Chimeric proteins containing virulence factors can prevent Shigella infection. The purpose of this study is to investigate the immunogenic and protective effect of trivalent chimeric protein containing IpaD-StxB-TolC antigens against shiga toxin, S. dysenteri and S. flexneri in vitro and in vivo conditions.
METHODS METHODS
Recombinant vector was transferred to E. coli BL21. The expression of the chimeric protein was confirmed by SDS PAGE and purified using the Ni-NTA column. Mice were immunized with recombinant protein and antibody titer was evaluated by ELISA. 10, 25 and 50 LD
RESULTS RESULTS
The expression and purification of the recombinant protein with 60.6 kDa was done. ELISA showed increased antibody titer against the chimeric protein. MTT assay indicated that 1/8000 dilution of the sera had a 51% of cell viability against the toxin in Vero cell line. The challenge of mice immunized with toxin showed that the mice had complete protection against 10 and 25 LD
CONCLUSION CONCLUSIONS
This study showed that chimeric proteins can create favorable immunogenicity in the host as vaccine candidates.

Identifiants

pubmed: 36924900
pii: S0882-4010(23)00099-2
doi: 10.1016/j.micpath.2023.106066
pii:
doi:

Substances chimiques

Antigens, Bacterial 0
Bacterial Vaccines 0
Recombinant Proteins 0
Shiga Toxins 0
Recombinant Fusion Proteins 0
Antibodies, Bacterial 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

106066

Informations de copyright

Copyright © 2023 Elsevier Ltd. All rights reserved.

Auteurs

Javad Fathi (J)

Applied Microbiology Research Center, Systems Biology and Poisonings Institute, Baqiyatallah University of Medical Sciences, Tehran, Iran. Electronic address: javadfathi70@yahoo.com.

Jafar Amani (J)

Applied Microbiology Research Center, Systems Biology and Poisonings Institute, Baqiyatallah University of Medical Sciences, Tehran, Iran. Electronic address: jafar.amani@gmail.com.

Shahram Nazarian (S)

Department of Biological Sciences, Faculty of Science, Imam Hossein University, Tehran, Iran. Electronic address: kpnazari@ihu.ac.ir.

Nahal Hadi (N)

Department of Bacteriology and Virology, School of Medicine, Shiraz University of Medical Sciences, Shiraz, Iran.

Seyed Ali Mirhosseini (SA)

Applied Microbiology Research Center, Systems Biology and Poisonings Institute, Baqiyatallah University of Medical Sciences, Tehran, Iran.

Reza Ranjbar (R)

Molecular Biology Research Center, Systems Biology and Poisonings Institute, Baqiyatallah University of Medical Sciences, Tehran, Iran.

Hossein Samiei Abianeh (HS)

Department of Medical Biotechnology and Nanotechnology, Faculty of Medicine, Mashhad University of Medical Sciences, Mashhad, Iran.

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Classifications MeSH