The mechanism underlying toxicity of a venom peptide against insects reveals how ants are master at disrupting membranes.

ABSTRACT: 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 U₉ function, a linear, amphiphilic and polycationic peptide isolated from ant Tetramorium bicarinatum 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 U₉ and M-Tb1a and explored the mechanisms underlying their cytotoxicity against insect cells. After showing that both peptides induce

SUBMITTER: Ascoet S 

PROVIDER: S-EPMC9985030 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature