Location: Emerging Pests and Pathogens Research
Title: Characterization of the Vespa mandarinia venom gland proteome using high resolution mass spectrometryAuthor
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THOMPSON, LUKE - Cornell University |
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MANN, MARINA - Cornell University |
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CHANG, BRIAN - Consultant |
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Heck, Michelle |
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Submitted to: bioRxiv
Publication Type: Pre-print Publication Publication Acceptance Date: 2/17/2026 Publication Date: N/A Citation: N/A Interpretive Summary: The Northern Giant Hornet (Vespa mandarinia) is an invasive insect that threatens honey bee colonies, agricultural pollination systems, and public health due to the severity of its sting. However, limited information exists regarding the specific proteins and peptides that comprise its venom. Here we characterized the venom gland proteome of V. mandarinia using high-resolution mass spectrometry and identified major toxins and allergens, including phospholipase A1, mastoparans, hyaluronidase, venom allergen 5, and multiple heat shock proteins, as well as antimicrobial peptides and other bioactive components. Complementary proteomic approaches enabled detection of both large venom proteins and small peptides, revealing greater diversity than currently represented in available genome databases. This foundational characterization improves understanding of the biochemical basis of hornet envenomation, may support development of improved diagnostic or treatment strategies for sting victims, and provides insight into bioactive venom compounds that could have future agricultural or biomedical applications. Technical Abstract: The Northern Giant Hornet (Vespa mandarinia) is a large, ecologically impactful insect with few natural predators. V. mandarinia is a serious threat to native bees and honeybee production and a public health concern due to allergic reactions to its stings. In this study, we used high resolution mass spectrometry to analyze and categorize the proteins and peptides expressed within the hornet’s venom gland. Notable identified venom components included phospholipase-A1, several mastoparans, hyaluronidases, and many antimicrobial or allergenic proteins. |
