Evidence map›Paper›PMID 42324676›Full record

ArticlePest management science2026

Multifunctional lysozymes from the assassin bug Sycanus bifidus: Insecticidal proteins with anticoagulant and melanization inhibition properties.

Yuhan Liu, Wenkai Liang, Yuqin Wang, Chaoyan Wu, Wenxiu Wang, Ping Gao, Jiaying Zhu

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Article in Pest management science, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

7 authors.

Yuhan Liu *Key Laboratory of Forest Disaster Warning and Control of Yunnan Province, Southwest Forestry University, Kunming, China.
Wenkai Liang *Key Laboratory of Forest Disaster Warning and Control of Yunnan Province, Southwest Forestry University, Kunming, China.
Yuqin WangKey Laboratory of Forest Disaster Warning and Control of Yunnan Province, Southwest Forestry University, Kunming, China.
Chaoyan WuKey Laboratory of Forest Disaster Warning and Control of Yunnan Province, Southwest Forestry University, Kunming, China.
Wenxiu WangKey Laboratory of Forest Disaster Warning and Control of Yunnan Province, Southwest Forestry University, Kunming, China.
Ping GaoKey Laboratory of Forest Disaster Warning and Control of Yunnan Province, Southwest Forestry University, Kunming, China.
Jiaying ZhuKey Laboratory of Forest Disaster Warning and Control of Yunnan Province, Southwest Forestry University, Kunming, China.ORCID https://orcid.org/0000-0002-4533-8203

Funding

National Natural Science Foundation of China 32360686Science and Technology Innovation Team of Yunnan Provincial Department of EducationXing Dian Talents Support Program of Yunnan Province to Jiaying Zhu
6 · The paper itself

Abstract

backgroundPredatory hemipterans deploy complex venom cocktails to immobilize preys, yet the specific roles of many individual venom components remain poorly understood.

resultsFour lysozyme genes were identified from the genome of the predatory assassin bug Sycanus bifidus (Hemiptera: Reduviidae), comprising one i-type (SbLyzi) and three c-type lysozyme genes (SbLyzc1-3). Transcriptomic and quantitative (q)PCR analyses revealed that these lysozymes were expressed at different levels in various venom glands. Of them, SbLyzc1-3 with signal peptides displayed significant transcriptions in the venom glands, implicating these lysozymes as venom constituents. Functional assays found that SbLyzc1 and SbLyzc2 showed antibacterial activity against Pseudomonas aeruginosa and Enterococcus faecalis. Three lysozymes (SbLyzi, SbLyzc1 and SbLyzc3) suppressed thrombin-induced fibrin clot formation, indicating anticoagulant activity, with SbLyzc1 exhibiting the greatest potency [half-maximal inhibitory concentration (IC

conclusionThese findings demonstrate that lysozymes from S. bifidus possess multifunctional biological activities and SbLyzc1-3 act as significant venom components involved in capturing prey, providing new insights into the functional diversity of lysozymes in predatory bugs and their potential application in biological control strategies. © 2026 Society of Chemical Industry.

Indexed as

AnticoagulantsHeteropteraInsecticidesInsect ProteinsMuramidaseAmino Acid SequenceAnimalsMelanogenesisTenebrioAnticoagulantsInsecticidesInsect ProteinsMuramidaseanticoagulantinsecticidelysozymephenoloxidasevenom

Identifiers

PMID42324676
PMCPMC13569098

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.