Immunoinformatics analysis of Brucella melitensis to approach a suitable vaccine against brucellosis

Hashemzadeh, Pejman; nezhad, Saba Asgari; Khoshkhabar, Hossein

doi:10.1186/s43141-023-00614-6

Cited by 3 publications

(1 citation statement)

References 64 publications

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“…Up to now, several human brucellosis vaccine candidates have been reported, including live attenuated vaccines, subunit vaccines, recombinant protein-based vaccines, vectored vaccines, and DNA vaccines ( Perkins et al., 2010 ). An ideal vaccine for use in humans would be considered for its safety, immunogenicity, and protective efficacy ( Hashemzadeh et al., 2023 ). It is well known that the inclusion of adjuvants within vaccines can enhance vaccine-induced protection and thus offer an alternative approach to vaccine development.…”

Section: Brucella Vaccines For Humansmentioning

confidence: 99%

Brucella infection and Toll-like receptors

Yu,

Gu,

Wang

et al. 2024

Front. Cell. Infect. Microbiol.

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Brucella consists of gram-negative bacteria that have the ability to invade and replicate in professional and non-professional phagocytes, and its prolonged persistence in the host leads to brucellosis, a serious zoonosis. Toll-like receptors (TLRs) are the best-known sensors of microorganisms implicated in the regulation of innate and adaptive immunity. In particular, TLRs are transmembrane proteins with a typical structure of an extracellular leucine-rich repeat (LRR) region and an intracellular Toll/interleukin-1 receptor (TIR) domain. In this review, we discuss Brucella infection and the aspects of host immune responses induced by pathogens. Furthermore, we summarize the roles of TLRs in Brucella infection, with substantial emphasis on the molecular insights into its mechanisms of action.

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Section: Brucella Vaccines For Humansmentioning

confidence: 99%

Brucella infection and Toll-like receptors

Yu,

Gu,

Wang

et al. 2024

Front. Cell. Infect. Microbiol.

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Design and evaluation of a novel multi-epitope antigen for evaluate the diagnostic immunity responses against Leishmania infantum infection

Hashemzadeh,

Bandehpour,

Kheirandish

et al. 2024

Preprint

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Background Leishmania infantum is the causative agent of visceral leishmaniasis in the Mediterranean region. The diagnosis of complex visceral leishmaniasis and delays in the diagnosis of the infection are associated with the death of patients. Proper diagnosis of infection is an important measure in controlling and preventing the disease. However, studies have shown that the accuracy of antigens used in current diagnostic tests is insufficient, for this reason, researchers are trying to identify multi-epitope antigens as diagnostic markers to increase the specificity and sensitivity of diagnostic tests. In this study, the design and expression of Leishmania infantum multi-epitope antigens were carried out in two parts of the structure design using bioinformatics tools and the laboratory part for the production of the recombinant protein. Materials and Methods The aim of this study was to design and computationally analyze and express Leishmania infantum multi-epitope antigens. In this study, nine antigenic proteins (CPB, H1, KMP11, GP63, HASPB, A2, K39, LACK, and PSA) were selected. Bioinformatics analyzes such as prediction of immune cell epitopes, design of recombinant structure, antigenicity, allergenicity, evaluation of physicochemical properties, solubility, prediction of secondary structure and tertiary structure, refinement and validation of 3D model structure and finally in silico cloning optimization of protein construct were performed. After synthesis of the designed recombinant gene fusion sequence in pUC57 cloning vector, its subcloning was performed in pET26b prokaryotic expression vector using BamHI/ HindIII restriction enzymes. The expression of recombinant multi-epitope antigen was performed in E. coli B (BL21) strain using IPTG inducer and confirmed by SDS-PAGE and western blotting techniques. Results The results of computational analysis showed that the complete structure, which is suitable for immunogenicity and is non-allergenic, was successfully cloned into pET-26b and expressed as a complete protein. Conclusion Finally, the protein was approved. Based on the expression of recombinant proteins and bioinformatics analysis, this structure can be studied in mouse models and its safety can be evaluated.

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