ArticleInsect molecular biology2018
Major venom proteins of the fire ant Solenopsis invicta: insights into possible pheromone-binding function from mass spectrometric analysis.
Article in Insect molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 23 citations in OpenAlex.
- Article
- Therapeutic Potential ofBiomolecules · 2024Article
- Revealing the pH-dependent conformational changes in sol g 2.1 protein and potential ligands binding.Scientific reports · 2024Article
- Article
- 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
- Chemistry and Functions of Imported Fire Ant Venom.Toxins · 2023Review
- Global View on Ant Venom Allergy: from Allergenic Components to Clinical Management.Clinical reviews in allergy & immunology · 2022Review
- An integrated transcriptomic and proteomic approach to identify the main Torymus sinensis venom components.Scientific reports · 2021Article
- Antennal Proteome of the Solenopsis invicta (Hymenoptera: Formicidae): Caste Differences in Olfactory Receptors and Chemosensory Support Proteins.Journal of insect science (Online) · 2020Article
- Identification, expression and characterization of the recombinant Sol g 4.1 protein from the venom of the tropical fire antThe journal of venomous animals and toxins including tropical diseases · 2018Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Proteins in the venom of the fire ant Solenopsis invicta have been suggested to function in pheromone binding. Venom from queens and workers contains different isoforms of these proteins, consistent with the differing pheromones they secrete, but questions remain about the venom protein composition and glandular source. We found that the queen venom contains a previously uncharacterized pheromone-binding protein paralogue known as Sol i 2X1. Using imaging mass spectrometry, we located the main venom proteins in the poison sac, implying that pheromones might have to compete with venom alkaloids for binding. Using the known structure of the worker venom protein Sol i 2w, we generated three-dimensional homology models of the worker venom protein Sol i 4.02, and of the two main venom proteins in queens and female alates, Sol i 2q and Sol i 2X1. Surprisingly, the models show that the proteins have relatively small internal hydrophobic binding pockets that are blocked by about 10 amino acids of the C-terminal region. For these proteins to function as carriers of hydrophobic ligands, a conformational change would be required to displace the C-terminal region, somewhat like the mechanism known to occur in the silk moth pheromone-binding protein.
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Registered trials
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