ArticleThe journal of venomous animals and toxins including tropical diseases2018
Identification, expression and characterization of the recombinant Sol g 4.1 protein from the venom of the tropical fire ant
Article in The journal of venomous animals and toxins including tropical diseases, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 14 citations in OpenAlex.
- Therapeutic Potential ofBiomolecules · 2024Article
- Revealing the pH-dependent conformational changes in sol g 2.1 protein and potential ligands binding.Scientific reports · 2024Article
- Structure-based epitope prediction and assessment of cross-reactivity of Myrmecia pilosula venom-specific IgE and recombinant Sol g proteins (Solenopsis geminata).Scientific reports · 2024Article
- Protein-Ligand Binding and Structural Modelling Studies of Pheromone-Binding Protein-like Sol g 2.1 fromMolecules (Basel, Switzerland) · 2024Article
- Characterization and Localization of Sol g 2.1 Protein fromInternational journal of molecular sciences · 2023Article
- Review
- A combined protein toxin screening based on the transcriptome and proteome of Solenopsis invicta.Proteome science · 2022Article
- Unique venom proteins fromToxicon: X · 2021Article
- Article
- Heterologous expression and mutagenesis of recombinantThe journal of venomous animals and toxins including tropical diseases · 2019Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundFire ant venom is a complex mixture consisting of basic piperidine alkaloids, various biologically active peptides and protein components, including a variety of major allergenic proteins. Tropical fire ant
methodsIn the present study, the cDNA cloning, sequencing and three-dimensional structure of Sol g 4.1 venom protein are described. The recombinant Sol g 4.1 protein (rSol g 4.1) was produced in
resultsThe molecular weight of Sol g 4.1 protein is 16 kDa, as determined by SDS-PAGE. The complete cDNA is 414 bp in length and contains a leader sequence of 19 amino acids. The protein consists of six cysteines that presumably form three disulfide bonds, based on a predicted three-dimensional model, creating the interior hydrophobic pocket and stabilizing the structure. The rSol g 4.1 protein was expressed in inclusion bodies, as determined by SDS-PAGE. Dialysis techniques were used to refold the recombinant protein into the native form. Its secondary structure, which primarily consists of α-helices, was confirmed by circular dichroism analysis, and the three-dimensional model was also verified. The results of allergenic analysis performed on mice showed that the obtained protein was predicted to be allergenically active. Moreover, we report on the possible role of the Sol g 4.1 venom protein, which significantly reduced the PD
conclusionsThe primary structure of Sol g 4.1 showed high similarity to that of venom proteins in the
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