Sexual Selection and Proteinaceous Diversity in the Femoral Gland Secretions of Lacertid Lizards

• Published in: Diversity (Basel) Vol. 15; no. 6; p. 777
• Main Authors: Mangiacotti, Marco, Baeckens, Simon, Fumagalli, Marco, Martín, José, Scali, Stefano, Sacchi, Roberto
• Format: Journal Article
• Language: English
• Published: Basel MDPI AG 01.06.2023
• Subjects: Animal reproduction; Carbon dioxide; Carbonic anhydrase; chemical communication; Communication; Comparative analysis; Datasets; Evolution; femoral glands; Femur; Glands; Hypotheses; Ions; Lipids; Lizards; Males; Mass spectrometry; Mass spectroscopy; Molecular weight; Natural selection; Phylogenetics; Phylogeny; Proteins; Scientific imaging; Secretions; Semiochemicals; Sexual dimorphism; Sexual selection; Sexual selection in animals; Social aspects; Social behavior; Social factors; Social interactions; Squamata; Massachusetts; Italy
• ISSN: 1424-2818; 1424-2818
• DOI: 10.3390/d15060777

Sexual selection contributes to the diversity of chemical signals in various animal groups. Lizards are good model species to study how sexual selection shapes signal diversity, as they are a chemically oriented taxonomic group with different levels of social interactions. Many lizard species bear epidermal glands secreting a waxy mixture of lipids and proteins, which are used in intraspecific communication. Previous among-species comparative analyses failed to find a relationship between the strength of sexual selection with the composition of the lipid blend in lizards. Here, we extend the investigation to the proteinaceous fraction. By using a phylogenetically informed approach, we correlated the average electrophoretic profiles of the protein from the femoral glands of 36 lacertid lizard species with the level of sexual dimorphism in size and shape, which are proxies for the strength of sexual selection. We found that as sexual size dimorphism advances, five distinct molecular weight regions in the protein profile increased their expression. Using tandem mass spectrometry, we successfully identified one of these five proteins: a carbonic anhydrase—an enzyme catalyzing the reversible hydration of carbon dioxide. Our findings suggest that proteins may be the target of sexual selection, as an active semiochemicals or as a dynamic support to other molecules: sexual selection may act indirectly on semiochemicals (namely lipids) by modifying the matrix (namely proteins).