| Summary: | Predatory stink bugs capture prey by injecting salivary venom from their venom glands using specialized stylets. Understanding venom function has been impeded by a scarcity of knowledge of their venom composition. We therefore examined the proteinaceous components of the salivary venom of the predatory stink bug <i>Arma custos</i> (Fabricius, 1794) (Hemiptera: Pentatomidae). We used gland extracts and venoms from fifth-instar nymphs or adult females to perform shotgun proteomics combined with venom gland transcriptomics. We found that the venom of <i>A. custos</i> comprised a complex suite of over a hundred individual proteins, including oxidoreductases, transferases, hydrolases, ligases, protease inhibitors, and recognition, transport and binding proteins. Besides the uncharacterized proteins, hydrolases such as venom serine proteases, cathepsins, phospholipase A<sub>2</sub>, phosphatases, nucleases, alpha-amylases, and chitinases constitute the most abundant protein families. However, salivary proteins shared by and unique to other predatory heteropterans were not detected in the <i>A. custos</i> venom. Injection of the proteinaceous (>3 kDa) venom fraction of <i>A. custos</i> gland extracts or venom into its prey, the larvae of the oriental armyworm <i>Mythimna separata</i> (Walker, 1865), revealed insecticidal activity against lepidopterans. Our data expand the knowledge of heteropteran salivary proteins and suggest predatory asopine bugs as a novel source for bioinsecticides.
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