Identification, Characterization and Synthesis of Walterospermin, a Sperm Motility Activator from the Egyptian Black Snake Walterinnesia aegyptia Venom - Université Grenoble Alpes Accéder directement au contenu
Article Dans Une Revue International Journal of Molecular Sciences Année : 2020

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

Tarek Mohamed Abd El-Aziz
Lucie Jaquillard
  • Fonction : Auteur
Guillaume Martinez
  • Fonction : Auteur
Mathilde Triquigneaux
  • Fonction : Auteur
Claude Zoukimian
  • Fonction : Auteur
Stéphanie Combemale
  • Fonction : Auteur
Jean-Pascal Hograindleur
  • Fonction : Auteur
Sawsan Al Khoury
  • Fonction : Auteur
Jessica Escoffier
  • Fonction : Auteur
Sylvie Michelland
  • Fonction : Auteur
Philippe Bulet
Rémy Beroud
  • Fonction : Auteur
Christophe Arnoult
  • Fonction : Auteur
Michel de Waard

Résumé

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.

Dates et versions

hal-04550844 , version 1 (18-04-2024)

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Tarek Mohamed Abd El-Aziz, Lucie Jaquillard, Sandrine Bourgoin-Voillard, Guillaume Martinez, Mathilde Triquigneaux, et al.. Identification, Characterization and Synthesis of Walterospermin, a Sperm Motility Activator from the Egyptian Black Snake Walterinnesia aegyptia Venom. International Journal of Molecular Sciences, 2020, 21 (20), pp.7786. ⟨10.3390/ijms21207786⟩. ⟨hal-04550844⟩

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