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Open AccessArticle

Identification, Characterization and Synthesis of Walterospermin, a Sperm Motility Activator from the Egyptian Black Snake Walterinnesia aegyptia Venom

1
Department of Cellular and Integrative Physiology, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229-3900, USA
2
Zoology Department, Faculty of Science, Minia University, El-Minia 61519, Egypt
3
Smartox Biotechnology, 6 rue des Platanes, 38120 Saint-Egrève, France
4
PROMETHEE Proteomic Platform, University Grenoble Alpes, LBFA et BEeSy, 38041 Grenoble, France
5
PROMETHEE Proteomic Platform, INSERM U1055, 38041 Grenoble, France
6
PROMETHEE Proteomic Platform, Institut de Biologie et de Pathologie, IAB, CHU Grenoble Alpes, 38000 Grenoble, France
7
Institut Pour l’Avancée des Biosciences (IAB), INSERM U1209, CNRS UMR 5309, 38700 La Tronche, France
8
Université Grenoble Alpes, 38000 Grenoble, France
9
L’institut du thorax, INSERM, CNRS, UNIV NANTES, F-44007 Nantes, France
10
Université de Nice Sophia-Antipolis, LabEx «Ion Channels, Science & Therapeutics», F-06560 Valbonne, France
11
Archamps BioPark, 260 Avenue Marie Curie, Archamps Technopole, F-74166 Saint Julien en Genevois, France
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2020, 21(20), 7786; https://doi.org/10.3390/ijms21207786
Received: 1 September 2020 / Revised: 13 October 2020 / Accepted: 15 October 2020 / Published: 21 October 2020
(This article belongs to the Special Issue Peptides for Health Benefits 2020)
Animal venoms are small natural mixtures highly enriched in bioactive components. They are known to target at least two important pharmacological classes of cell surface receptors: ion channels and G protein coupled receptors. 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. 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. Using RP-HPLC and cation exchange chromatography, we identified a new toxin of 6389.89 Da (termed walterospermin) that activates sperm motility. 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. 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. 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 synthetic peptide shows promising activation of sperm motility from a variety of species, including humans. Its fluorescently-labelled analog predominantly marks the flagellum, a localization in agreement with a receptor that controls motility function. View Full-Text
Keywords: Snake venom; Walterinnesia aegyptia; bioactive components; sperm motility; proteomics; mass spectrometry; peptide sequencing; drug screening. Snake venom; Walterinnesia aegyptia; bioactive components; sperm motility; proteomics; mass spectrometry; peptide sequencing; drug screening.
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Abd El-Aziz, T.M.; Jaquillard, L.; Bourgoin-Voillard, S.; Martinez, G.; Triquigneaux, M.; Zoukimian, C.; Combemale, S.; Hograindleur, J.-P.; Al Khoury, S.; Escoffier, J.; Michelland, S.; Bulet, P.; Beroud, R.; Seve, M.; Arnoult, C.; De Waard, M. Identification, Characterization and Synthesis of Walterospermin, a Sperm Motility Activator from the Egyptian Black Snake Walterinnesia aegyptia Venom. Int. J. Mol. Sci. 2020, 21, 7786.

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