Ascoët Steven, Touchard Axel, Téné Nathan, Lefranc Benjamin, Leprince Jérôme, Paquet Françoise, Jouvensal Laurence, Barassé Valentine, Treilhou Michel, Billet Arnaud, Bonnafé Elsa
BTSB-UR 7417, Université de Toulouse, Institut National Universitaire Jean-François Champollion, Place de Verdun, 81000 Albi, France.
CNRS, UMR Ecologie des Forêts de Guyane, AgroParisTech, CIRAD, INRA, Université de Guyane, Université des Antilles, Campus Agronomique, BP316 97310 Kourou, France.
iScience. 2023 Feb 8;26(3):106157. doi: 10.1016/j.isci.2023.106157. eCollection 2023 Mar 17.
Hymenopterans represent one of the most abundant groups of venomous organisms but remain little explored due to the difficult access to their venom. The development of proteo-transcriptomic allowed us to explore diversity of their toxins offering interesting perspectives to identify new biological active peptides. This study focuses on U function, a linear, amphiphilic and polycationic peptide isolated from ant venom. It shares physicochemical properties with M-Tb1a, exhibiting cytotoxic effects through membrane permeabilization. In the present study, we conducted a comparative functional investigation of U and M-Tb1a and explored the mechanisms underlying their cytotoxicity against insect cells. After showing that both peptides induced the formation of pores in cell membrane, we demonstrated that U induced mitochondrial damage and, at high concentrations, localized into cells and induced caspase activation. This functional investigation highlighted an original mechanism of U questioning on potential valorization and endogen activity in . venom.
膜翅目昆虫是最丰富的有毒生物群体之一，但由于难以获取其毒液，对其研究仍很少。蛋白质转录组学的发展使我们能够探索其毒素的多样性，为鉴定新的生物活性肽提供了有趣的视角。本研究聚焦于U功能肽，这是一种从蚂蚁毒液中分离出的线性、两亲性和聚阳离子肽。它与M-Tb1a具有相同的物理化学性质，通过细胞膜通透化表现出细胞毒性作用。在本研究中，我们对U功能肽和M-Tb1a进行了比较功能研究，并探讨了它们对昆虫细胞产生细胞毒性的潜在机制。在证明这两种肽都能诱导细胞膜形成孔道后，我们发现U功能肽会诱导线粒体损伤，并且在高浓度时会进入细胞并诱导半胱天冬酶激活。这项功能研究突出了U功能肽的一种独特机制，引发了对其在毒液中的潜在价值和内源性活性的质疑。
