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

Fathi, Javad; Amani, Jafar; Nazarian, Shahram; Hadi, Nahal; Mirhosseini, Seyed Ali; Ranjbar, Reza; Abianeh, Hossein Samiei

doi:10.1016/j.micpath.2023.106066

Cited by 2 publications

(1 citation statement)

References 22 publications

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“…While STxB binds to the Gb3 receptor on the epithelial cells, STxA interacts and cleaves the 28s RNA of the 60S subunit of the ribosome, disrupting protein synthesis (Robert and Wiels 2021). Previous research by scientists (Honari et al 2014;Amani et al 2023) showed the effectiveness of bacterial expression of the IpaDSTxB chimeric gene in triggering an immune response in mice. Additionally, plant-based IpaDSTxB protein produced in N.tabacum has shown effectiveness against shigellosis in mice, although there remains a challenge of low yield of recombinant proteins (RP) (unpublished data).…”

Section: Introductionmentioning

confidence: 99%

Unlocking the Potential of Extensin Signal Peptide and Elastin-like polypeptide Tag fused to Shigella dysenteriae’s IpaDSTxB to Improve Protein Expression and Purification in Nicotiana tabacum and Medicago sativa

Soleimani,

Alizadeh

2024

Preprint

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Plants are often seen as a potent tool in the recombinant protein production industry. However, unlike bacterial expression, it is not a popular method due to the low yield and difficulty of protein extraction and purification. Therefore, developing a new high efficient and easy to purify platform is crucial. One of the best approaches to make extraction easier is to utilize the Extensin Signal peptide (EXT) to translocate the recombinant protein to the outside of the cell, along with incorporating an Elastin-like polypeptide tag (ELP) to enhance purification and accumulation rates. In this research, we transiently expressed Shigella dysenteriae’s IpaDSTxB fused to both NtEXT and ELP in both Nicotiana tabacum and Medicago sativa. Our results demonstrated that N.tabacum, with an average yield of 6.39 ng/µg TSP, outperforms M.sativa, which had an average yield of 3.58 ng/µg TSP. On the other hand, analyzing NtEXT signal peptide indicated that merging EXT to the constructs facilitates translocation of IpaDSTxB to the apoplast by 78.4% and 65.9% in N.tabacum and M.sativa, respectively. Conversely, the mean level for constructs without EXT was below 25% for both plants. Furthermore, our investigation into the orientation of ELP showed that merging it to the C-terminal of IpaDSTxB leads to a higher accumulation rate in both N.tabacum and M.sativa by 1.39 and 1.28 times, respectively. It also facilitates purification rate by over 70% in comparison to 20% of the 6His tag. The results of this research show a highly efficient and easy to purify platform for the expression of heterologous proteins in plant.

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Section: Introductionmentioning

confidence: 99%

Unlocking the Potential of Extensin Signal Peptide and Elastin-like polypeptide Tag fused to Shigella dysenteriae’s IpaDSTxB to Improve Protein Expression and Purification in Nicotiana tabacum and Medicago sativa

Soleimani,

Alizadeh

2024

Preprint

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Enhancing protective immunity against bacterial infection via coating nano‐Rehmannia glutinosa polysaccharide with outer membrane vesicles

Huang,

Sun,

Cui

et al. 2024

J of Extracellular Vesicle

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With the coming of the post‐antibiotic era, there is an increasingly urgent need for safe and efficient antibacterial vaccines. Bacterial outer membrane vesicles (OMVs) have received increased attention recently as a potential subunit vaccine. OMVs are non‐replicative and contain the principle immunogenic bacterial antigen, which circumvents the safety concerns of live‐attenuated vaccines. Here, we developed a novel nano‐vaccine by coating OMVs onto PEGylated nano‐Rehmannia glutinosa polysaccharide (pRL) in a structure consisting of concentric circles, resulting in a more stable vaccine with improved immunogenicity. The immunological function of the pRL‐OMV formulation was evaluated in vivo and in vitro, and the underlying mechanism was studied though transcriptomic analysis. The pRL‐OMV formulation significantly increased dendritic cell (DC) proliferation and cytokine secretion. Efficient phagocytosis of the formulation by DCs was accompanied by DC maturation. Further, the formulation demonstrated superior lymph node targeting, contributing to a potent mixed cellular response and bacterial‐specific antibody response against Bordetella bronchiseptica infection. Specifically, transcriptomic analysis revealed that the immune protection function correlated with T‐cell receptor signalling and Th1/Th2/Th17 differentiation, among other markers of enhanced immunological activity. These findings have implications for the future application of OMV‐coated nano‐carriers in antimicrobial immunotherapy.

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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

Cited by 2 publications

References 22 publications

Unlocking the Potential of Extensin Signal Peptide and Elastin-like polypeptide Tag fused to Shigella dysenteriae’s IpaDSTxB to Improve Protein Expression and Purification in Nicotiana tabacum and Medicago sativa

Unlocking the Potential of Extensin Signal Peptide and Elastin-like polypeptide Tag fused to Shigella dysenteriae’s IpaDSTxB to Improve Protein Expression and Purification in Nicotiana tabacum and Medicago sativa

Enhancing protective immunity against bacterial infection via coating nano‐Rehmannia glutinosa polysaccharide with outer membrane vesicles

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