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Open AccessArticle

The Major Cat Allergen Fel d 1 Binds Steroid and Fatty Acid Semiochemicals: A Combined In Silico and In Vitro Study

1
Department of Molecular Biology and Chemical Communication (D-BMCC), Research Institute in Semiochemistry and Applied Ethology (IRSEA), Quartier Salignan, 84400 Apt, France
2
Austrian Institute of Technology GmbH, Biosensor Technologies, Konrad-Lorenzstraße, 3430 Tulln, Austria
3
Department of Chemical Ecology (D-EC), Research Institute in Semiochemistry and Applied Ethology (IRSEA), Quartier Salignan, 84400 Apt, France
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2020, 21(4), 1365; https://doi.org/10.3390/ijms21041365
Received: 28 January 2020 / Revised: 12 February 2020 / Accepted: 13 February 2020 / Published: 18 February 2020
The major cat allergen Fel d 1 is a tetrameric glycoprotein of the secretoglobin superfamily. Structural aspects and allergenic properties of this protein have been investigated, but its physiological function remains unclear. Fel d 1 is assumed to bind lipids and steroids like the mouse androgen-binding protein, which is involved in chemical communication, either as a semiochemical carrier or a semiochemical itself. This study focused on the binding activity of a recombinant model of Fel d 1 (rFel d 1) towards semiochemical analogs, i.e., fatty acids and steroids, using both in silico calculations and fluorescence measurements. In silico analyses were first adopted to model the interactions of potential ligands, which were then tested in binding assays using the fluorescent reporter N-phenyl-1-naphthylamine. Good ligands were fatty acids, such as the lauric, oleic, linoleic, and myristic fatty acids, as well as steroids like androstenone, pregnenolone, and progesterone, that were predicted by in silico molecular models to bind into the central and surface cavities of rFel d 1, respectively. The lowest dissociation constants were shown by lauric acid (2.6 µM) and androstenone (2.4 µM). The specific affinity of rFel d 1 to semiochemicals supports a function of the protein in cat’s chemical communication, and highlights a putative role of secretoglobins in protein semiochemistry. View Full-Text
Keywords: secretoglobin; odorant-binding protein; chemical communication; pheromone; N-phenyl-1-naphthylamine; in silico docking; molecular modeling; protein–ligand interactions; 2D interaction maps; ligand-binding assays secretoglobin; odorant-binding protein; chemical communication; pheromone; N-phenyl-1-naphthylamine; in silico docking; molecular modeling; protein–ligand interactions; 2D interaction maps; ligand-binding assays
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MDPI and ACS Style

Bienboire-Frosini, C.; Durairaj, R.; Pelosi, P.; Pageat, P. The Major Cat Allergen Fel d 1 Binds Steroid and Fatty Acid Semiochemicals: A Combined In Silico and In Vitro Study. Int. J. Mol. Sci. 2020, 21, 1365. https://doi.org/10.3390/ijms21041365

AMA Style

Bienboire-Frosini C, Durairaj R, Pelosi P, Pageat P. The Major Cat Allergen Fel d 1 Binds Steroid and Fatty Acid Semiochemicals: A Combined In Silico and In Vitro Study. International Journal of Molecular Sciences. 2020; 21(4):1365. https://doi.org/10.3390/ijms21041365

Chicago/Turabian Style

Bienboire-Frosini, Cécile; Durairaj, Rajesh; Pelosi, Paolo; Pageat, Patrick. 2020. "The Major Cat Allergen Fel d 1 Binds Steroid and Fatty Acid Semiochemicals: A Combined In Silico and In Vitro Study" Int. J. Mol. Sci. 21, no. 4: 1365. https://doi.org/10.3390/ijms21041365

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