Comprehensive Analysis and Biological Characterization of Venom Components from Solitary Scoliid Wasp Campsomeriella annulata annulata

Venoms of solitary wasps are utilized for prey capture (insects and spiders), paralyzing them with a stinger injection to be offered as food for their larvae. Thus, the identification and characterization of the components of solitary wasp venoms can have biotechnological application. In the present study, the venom components profile of a solitary scoliid wasp, Campsomeriella annulata annulata, was investigated through a comprehensive analysis using LC-MS and -MS/MS. Online mass fingerprinting revealed that the venom extract contains 138 components, and MS/MS analysis identified 44 complete sequences of the peptide components. The peptides are broadly divided into two classes: bradykinin-related peptides, and linear α-helical peptides. Among the components of the first class, the two main peptides, α-campsomerin (PRLRRLTGLSPLR) and β-campsomerin (PRLRRLTGLSPLRAP), had their biological activities evaluated. Both peptides had no effects on metallopeptidases [human neprilysin (NEP) and angiotensin-converting enzyme (ACE)] and acetylcholinesterase (AChE), and had no cytotoxic effects. Studies with PC12 neuronal cells showed that only α-campsomerin was able to enhance cell viability, while β-campsomerin had no effect. It is noteworthy that the only difference between the primary structures from these peptides is the presence of the AP extension at the C-terminus of β-campsomerin, compared to α-campsomerin. Among the linear α-helical peptides, annulatin (ISEALKSIIVG-NH2) was evaluated for its biological activities. Annulatin showed histamine releasing activity from mast cells and low hemolytic activity, but no antimicrobial activities against all microbes tested were observed. Thus, in addition to providing unprecedented information on the whole components, the three peptides selected for the study suggest that molecules present in solitary scoliid wasp venoms may have interesting biological activities.

Toxicosis of Snake, Scorpion, Honeybee, Spider, and Wasp Venoms: Part 2

Toxicosis is a poisoning caused by venomous animals such as snake, scorpion, honeybee, spider and wasp. Their poisons contain amino acids, peptides, proteins, enzymes and metallic ions that are responsible for neurotoxicity, hemotoxicity and myotoxicity. Because of in vivo therapeutic challenges posed by toxicosis, there is need for ideal therapeutic agents against envenomation caused by venomous animals. Findings have shown that toxicosis could be treated symptomatically. Snake and scorpion antivenins could be used for treatment of poisoning caused by snake, scorpion, honeybee, spider and wasp. The amount of antivenin is dependent on the quantity of venom injected into the affected individuals. Moreso, sympotomatic treatments are also done according to the systems affected. Hospitalization is necessary for assessment of therapeutic success.

Toxicosis of Snake, Scorpion, Honeybee, Spider, and Wasp Venoms: Part 1

Toxicosis is a poisoning caused by venomous animals such as snake, scorpion, honeybee, spider, and wasp. Their poisons contain amino acids, peptides, proteins, enzymes, and metallic ions that are responsible for neurotoxicity, hemotoxicity, and myotoxicity. Because of in vivo therapeutic challenges posed by toxicosis, there is need for ideal therapeutic agents against envenomation caused by venomous animals. Findings have shown that toxicosis could be treated symptomatically. Snake and scorpion antivenins could be used for treatment of poisoning caused by snake, scorpion, honeybee, spider, and wasp. The amount of antivenin is dependent on the quantity of venom injected into the affected individuals. More so, symptomatic treatments are also done according to the systems affected. Hospitalization is necessary for assessment of therapeutic success.

Proteo-Transcriptomic Characterization of the Venom from the Endoparasitoid Wasp Pimpla turionellae with Aspects on Its Biology and Evolution

Within mega-diverse Hymenoptera, non-aculeate parasitic wasps represent 75% of all hymenopteran species. Their ovipositor dual-functionally injects venom and employs eggs into (endoparasitoids) or onto (ectoparasitoids) diverse host species. Few endoparasitoid wasps such as Pimpla turionellae paralyze the host and suppress its immune responses, such as encapsulation and melanization, to guarantee their offspring’s survival. Here, the venom and its possible biology and function of P. turionellae are characterized in comparison to the few existing proteo-transcriptomic analyses on parasitoid wasp venoms. Multiple transcriptome assembly and custom-tailored search and annotation strategies were applied to identify parasitoid venom proteins. To avoid false-positive hits, only transcripts were finally discussed that survived strict filter settings, including the presence in the proteome and higher expression in the venom gland. P. turionella features a venom that is mostly composed of known, typical parasitoid enzymes, cysteine-rich peptides, and other proteins and peptides. Several venom proteins were identified and named, such as pimplin2, 3, and 4. However, the specification of many novel candidates remains difficult, and annotations ambiguous. Interestingly, we do not find pimplin, a paralytic factor in Pimpla hypochondriaca, but instead a new cysteine inhibitor knot (ICK) family (pimplin2), which is highly similar to known, neurotoxic asilid1 sequences from robber flies.

Chemical and Biological Characteristics of Antimicrobial α-Helical Peptides Found in Solitary Wasp Venoms and Their Interactions with Model Membranes

Solitary wasps use their stinging venoms for paralyzing insect or spider prey and feeding them to their larvae. We have surveyed bioactive substances in solitary wasp venoms, and found antimicrobial peptides together with some other bioactive peptides. Eumenine mastoparan-AF (EMP-AF) was the first to be found from the venom of the solitary eumenine wasp Anterhynchium flavomarginatum micado, showing antimicrobial, histamine-releasing, and hemolytic activities, and adopting an α-helical secondary structure under appropriate conditions. Further survey of solitary wasp venom components revealed that eumenine wasp venoms contained such antimicrobial α-helical peptides as the major peptide component. This review summarizes the results obtained from the studies of these peptides in solitary wasp venoms and some analogs from the viewpoint of (1) chemical and biological characterization; (2) physicochemical properties and secondary structure; and (3) channel-like pore-forming properties.

New Mastoparan Peptides in the Venom of the Solitary Eumenine Wasp Eumenes micado

Comprehensive LC-MS and MS/MS analysis of the crude venom extract from the solitary eumenine wasp Eumenes micado revealed the component profile of this venom mostly consisted of small peptides. The major peptide components, eumenine mastoparan-EM1 (EMP-EM1: LKLMGIVKKVLGAL-NH2) and eumenine mastoparan-EM2 (EMP-EM2: LKLLGIVKKVLGAI-NH2), were purified and characterized by the conventional method. The sequences of these new peptides are homologous to mastoparans, the mast cell degranulating peptides from social wasp venoms; they are 14 amino acid residues in length, rich in hydrophobic and basic amino acids, and C-terminal amidated. Accordingly, these new peptides can belong to mastoparan peptides (in other words, linear cationic α-helical peptides). Indeed, the CD spectra of these new peptides showed predominantly α-helix conformation in TFE and SDS. In biological evaluation, both peptides exhibited potent antibacterial activity, moderate degranulation activity from rat peritoneal mast cells, and significant leishmanicidal activity, while they showed virtually no hemolytic activity on human or mouse erythrocytes. These results indicated that EMP-EM peptides rather strongly associated with bacterial cell membranes rather than mammalian cell membranes.

1Institute of Biotechnology, Vietnam Academy of Science and Technology

Wasp venoms are complex mixtures of various types of compounds, of which proteins and peptides are major components. Beside its toxicity, wasp venom is potential for treatment of diseases. Characterization of venom proteins and peptides is the first and most important step toward its applications in medicine. Vietnam possesses many valuable materials, of which venoms could be used in medicine. In the present work, we aim to identify proteins and peptides in the venom of Vespa velutina (V. velutina), a species of social wasp indigenous to Southeast Asia including Vietnam using proteomic techniques. The venom isolated from V. velutina by manual extraction was digested with trypsin via the FASP (Filter Aided Sample Preparation) method and analyzed with liquid chromatography tandem - mass spectrometry (LC-MS/MS). The following protein identification, protein validation, and peptide de novo sequencing were carried out using the Peaks software. In total, we detected 36 proteins from V. velutina venom and many of them had been reported as venom-specific proteins. According to Gene Ontology Annotation (GOA), V. velutina venom proteins were functionally classified into five categories: binding proteins (53%), catalytic proteins (33%), structural proteins (8%), antioxidants (4%), and proteins with other functions (2%). In addition, 81 peptides were detected in the venom of V. velutina by de novo sequencing, of which 34 peptides (42%) are potential venom peptides. We introduced for the first time the collection of proteins and peptides from V. velutina venom, providing the basis for its further application in medicine.