数字农科院2.0

A C-type lectin from domestic silkworm (Bombyx mori) is involved in bacterial recognition and participates in prophenoloxidase activation

文献类型: 外文期刊

作者: Yan Huang;Jing Zhang;Jingyao Shi;Jie Wu;Dan Zhang;Qiaoling Zhao;Dongxu Shen

作者机构:

关键词: Binding;Bombyx mori;C-type lectins;Melanization

期刊名称: Journal of Asia-Pacific Entomology

ISSN: 1226-8615

年卷期: 2026 年 29 卷 1 期

页码:

收录情况: SCIE(2025版)

摘要: C-type lectins (CTLs), which belong to the superfamily of glycan-binding proteins, are characterized by the presence of one or more carbohydrate recognition domains (CRDs). CTLs are involved in biological processes, such as immune recognition, intercellular signaling, cell adhesion, and pathogen clearance, and are widely distributed across diverse organisms, from invertebrates to vertebrates. In this study, we investigated the function of the C-type lectin gene named BmIML-2, in the innate immune response of the domestic silkworm, Bombyx mori. First, our results suggested that BmIML-2 was highly expressed in fat body and its transcript levels were significantly up-regulated after induction by different species of bacteria. Afterwards, BmIML-2 was recombinantly expressed using a prokaryotic expression system to delve into its physiological function. Binding assays showed that recombinant BmIML-2 (rBmIML-2) exhibits binding capacity to bacteria, including Escherichia coli, Micrococcus luteus, Staphylococcus aureus and Bacillus subtilis. In addition, Enzyme linked immunosorbent assay (ELISA) demonstrated that rBmIML-2 also binds to cell wall components, such as lipopolysaccharide (LPS) and peptidoglycan (PGN), with more intensely binding affinity to the former. Furthermore, encapsulation assays in vitro suggested that rBmIML-2 was able to accelerate encapsulation and melanization mediated by hemocytes. Finally, we demonstrated that rBmIML-2 significantly potentiates the stimulation pathway of prophenoloxidase (PPO) in plasma. In summary, our results demonstrate that BmIML-2 can act as a pattern recognition receptor (PRR) involved in the host innate immune response.

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