Crystal structure of Sol i 2 : a major allergen from fire ant venom

Borer, Aline S. and Wassmann, Paul and Schmidt, Margit and Hoffman, Donald R. and Zhou, Jing-Jiang and Wright, Christine and Schirmer, Tilman and Marković-Housley, Zora. (2011) Crystal structure of Sol i 2 : a major allergen from fire ant venom. Journal of molecular biology, Vol. 415, H. 4. pp. 635-648.

Full text not available from this repository.

Official URL: http://edoc.unibas.ch/dok/A6001531

Downloads: Statistics Overview


Sol i 2 is a potent allergen from the venom of red imported fire ant, which contains allergens Sol i 1, Sol i 2, Sol i 3, and Sol i 4 that are known to be powerful triggers of anaphylaxis. Sol i 2 causes IgE antibody production in about one-third of individuals stung by fire ants. Baculovirus recombinant dimeric Sol i 2 was crystallized as a native and selenomethionyl-derivatized protein, and its structure has been determined by single-wavelength anomalous dispersion at 2.6 Å resolution. The overall fold of each subunit consists of five helices that enclose a central hydrophobic cavity. The structure is stabilized by three intramolecular disulfide bridges and one intermolecular disulfide bridge. The nearest structural homologue is the sequence-unrelated odorant binding protein and pheromone binding protein LUSH of the fruit fly Drosophila, which may suggest a similar biological function. To test this hypothesis, we measured the reversible binding of various pheromones, plant odorants, and other ligands to Sol i 2 by the changes in N-phenyl-1-naphthylamine fluorescence emission upon binding of ligands that compete with N-phenyl-1-naphthylamine. The highest binding affinity was observed for hydrophobic ligands such as aphid alarm pheromone (E)-b-farnesene, analogs of ant alarm pheromones, and plant volatiles decane, undecane, and b-caryophyllene. Conceivably, Sol i 2 may play a role in capturing and/or transporting small hydrophobic ligands such as pheromones, odors, fatty acids, or short-living hydrophobic primers. Molecular surface analysis, in combination with sequence alignment, can explain the serological cross-reactivity observed between some ant species.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Schirmer)
UniBasel Contributors:Schirmer, Tilman and Housley-Markovic, Zora
Item Type:Article, refereed
Article Subtype:Research Article
Note:Publication type according to Uni Basel Research Database: Journal article
Related URLs:
Identification Number:
Last Modified:07 Aug 2015 12:05
Deposited On:11 Oct 2012 15:18

Repository Staff Only: item control page