Moreover, it has strong homology with several other hitherto cloned Elapidae and Viperidae snake toxins suggesting that it belongs to a family of compounds able to regulate sperm function. The peptide is 57 amino acid residues long and contains three disulfide bridges and was found to be identical to the previously cloned Wa Kunitz-type protease inhibitor II (Wa Kln-II) sequence. Walterospermin was de novo sequenced using a combination of matrix assisted laser desorption ionization time of flight mass spectrometry (MALDI-TOF/TOF MS/MS) and liquid chromatography electrospray ionization quadrupole time-of-flight mass spectrometry (LC-ESI-QTOF MS/MS) following reduction, alkylation, and enzymatic proteolytic digestion with trypsin, chymotrypsin or V8 protease. Using RP-HPLC and cation exchange chromatography, we identified a new toxin of 6389.89 Da (termed walterospermin) that activates sperm motility.
Herein, we screened for bioactive compounds from the venom of the Egyptian black snake Walterinnesia aegyptia (Wa) that possess the property to activate sperm motility in vitro from male mice OF1.
Since sperm cells express a wide variety of ion channels and membrane receptors, required for the control of cell motility and acrosome reaction, two functions that are defective in infertility issues, animal venoms should contain interesting compounds capable of modulating these two essential physiological functions. They are known to target at least two important pharmacological classes of cell surface receptors: ion channels and G protein coupled receptors.
Tarek Mohamed Abd El-Aziz Department of Cellular and Integrative Physiology, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229-3900, USA Lucie Jaquillard Smartox Biotechnology, 6 rue des Platanes, 38120 Saint-Egrève, France Sandrine Bourgoin-Voillard PROMETHEE Proteomic Platform, University Grenoble Alpes, LBFA et BEeSy, 38041 Grenoble, France Guillaume Martinez Institut pour l’Avancée des Biosciences (IAB), INSERM U1209, CNRS UMR 5309, 38700 La Tronche, France Mathilde Triquigneaux Smartox Biotechnology, 6 rue des Platanes, 38120 Saint-Egrève, France Claude Zoukimian Smartox Biotechnology, 6 rue des Platanes, 38120 Saint-Egrève, France Stéphanie Combemale Smartox Biotechnology, 6 rue des Platanes, 38120 Saint-Egrève, France Jean-Pascal Hograindleur Institut pour l’Avancée des Biosciences (IAB), INSERM U1209, CNRS UMR 5309, 38700 La Tronche, France Sawsan Al Khoury L’institut du thorax, INSERM, CNRS, UNIV NANTES, F-44007 Nantes, France Jessica Escoffier Institut pour l’Avancée des Biosciences (IAB), INSERM U1209, CNRS UMR 5309, 38700 La Tronche, France Sylvie Michelland PROMETHEE Proteomic Platform, University Grenoble Alpes, LBFA et BEeSy, 38041 Grenoble, France Philippe Bulet Institut pour l’Avancée des Biosciences (IAB), INSERM U1209, CNRS UMR 5309, 38700 La Tronche, France Rémy Beroud Smartox Biotechnology, 6 rue des Platanes, 38120 Saint-Egrève, France Michel Seve PROMETHEE Proteomic Platform, University Grenoble Alpes, LBFA et BEeSy, 38041 Grenoble, France Christophe Arnoult Institut pour l’Avancée des Biosciences (IAB), INSERM U1209, CNRS UMR 5309, 38700 La Tronche, France Michel De Waard Smartox Biotechnology, 6 rue des Platanes, 38120 Saint-Egrève, France DOI Journal volume & issueĪnimal venoms are small natural mixtures highly enriched in bioactive components.