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PLoS One

Title:		Another cat and mouse game: Deciphering the evolution of the SCGB superfamily and exploring the molecular similarity of major cat allergen Fel d 1 and mouse ABP using computational approaches
Author(s):		Durairaj R; Pageat P; Bienboire-Frosini C;
Address:		"Department of Behavioral and Physiological Mechanisms of Adaptation (D-MPCA), Research Institute in Semiochemistry and Applied Ethology (IRSEA), APT, France. Department of Semiochemicals Identification and Analogs Design (D-ISCA), Research Institute in Semiochemistry and Applied Ethology (IRSEA), APT, France"
Journal Title:		PLoS One
Year:		2018
Volume:		20180517
Issue:		5
Page Number:		e0197618 -
DOI:		10.1371/journal.pone.0197618
ISSN/ISBN:		1932-6203 (Electronic) 1932-6203 (Linking)
Abstract:		"The mammalian secretoglobin (SCGB) superfamily contains functionally diverse members, among which the major cat allergen Fel d 1 and mouse salivary androgen-binding protein (ABP) display similar subunits. We searched for molecular similarities between Fel d 1 and ABP to examine the possibility that they play similar roles. We aimed to i) cluster the evolutionary relationships of the SCGB superfamily; ii) identify divergence patterns, structural overlap, and protein-protein docking between Fel d 1 and ABP dimers; and iii) explore the residual interaction between ABP dimers and steroid binding in chemical communication using computational approaches. We also report that the evolutionary tree of the SCGB superfamily comprises seven unique palm-like clusters, showing the evolutionary pattern and divergence time tree of Fel d 1 with 28 ABP paralogs. Three ABP subunits (A27, BG27, and BG26) share phylogenetic relationships with Fel d 1 chains. The Fel d 1 and ABP subunits show similarities in terms of sequence conservation, identical motifs and binding site clefts. Topologically equivalent positions were visualized through superimposition of ABP A27:BG27 (AB) and ABP A27:BG26 (AG) dimers on a heterodimeric Fel d 1 model. In docking, Fel d 1-ABP dimers exhibit the maximum surface binding ability of AG compared with that of AB dimers and the several polar interactions between ABP dimers with steroids. Hence, cat Fel d 1 is an ABP-like molecule in which monomeric chains 1 and 2 are the equivalent of the ABPA and ABPBG monomers, respectively. These findings suggest that the biological and molecular function of Fel d 1 is similar to that of ABP in chemical communication, possibly via pheromone and/or steroid binding"
Keywords:		"Allergens/chemistry/*genetics Amino Acid Sequence Androgen-Binding Protein/chemistry/*genetics Animals Carrier Proteins/chemistry Cats/*genetics Computational Biology Computer Simulation Dihydrotestosterone/chemistry *Evolution, Molecular Glycoproteins/ch;"
Notes:		"MedlineDurairaj, Rajesh Pageat, Patrick Bienboire-Frosini, Cecile eng Research Support, Non-U.S. Gov't 2018/05/18 PLoS One. 2018 May 17; 13(5):e0197618. doi: 10.1371/journal.pone.0197618. eCollection 2018"