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南美肺鱼 intelectin-2 可能参与固有免疫调节。

Potential Involvement of the South American Lungfish Intelectin-2 in Innate-Associated Immune Modulation.

机构信息

Laboratory of Genomics and Biotechnology, Biological Sciences Institute, Federal University of Pará (UFPA), Belém 66075-110, PA, Brazil.

Laboratory of Biotechnology of Enzymes and Biotransformation, Biological Sciences Institute, Federal University of Pará (UFPA), Belém 66075-110, PA, Brazil.

出版信息

Int J Mol Sci. 2024 Apr 27;25(9):4798. doi: 10.3390/ijms25094798.

DOI:10.3390/ijms25094798
PMID:38732017
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11084424/
Abstract

Intelectins belong to a family of lectins with specific and transitory carbohydrate interaction capabilities. These interactions are related to the activity of agglutinating pathogens, as intelectins play a significant role in immunity. Despite the prominent immune defense function of intelectins, limited information about its structural characteristics and carbohydrate interaction properties is available. This study investigated an intelectin transcript identified in RNA-seq data obtained from the South American lungfish (), namely LpITLN2-B. The structural analyses predicted LpITLN2-B to be a homo-trimeric globular protein with the fibrinogen-like functional domain (FReD), exhibiting a molecular mass of 57 kDa. The quaternary structure is subdivided into three monomers, A, B, and C, and each domain comprises 11 β-sheets: an anti-parallel β-sheet, a β-hairpin, and a disordered β-sheet structure. Molecular docking demonstrates a significant interaction with disaccharides rather than monosaccharides. The preferential interaction with disaccharides highlights the potential interaction with pathogen molecules, such as LPS and Poly(I:C). The hemagglutination assay inhibited lectins activity, especially maltose and sucrose, highlighting lectin activity in samples. Overall, our results show the potential relevance of LpITLN2-B in immune defense against pathogens.

摘要

凝集素属于具有特定和短暂碳水化合物相互作用能力的凝集素家族。这些相互作用与凝集病原体的活性有关，因为凝集素在免疫中起着重要作用。尽管凝集素有突出的免疫防御功能，但关于其结构特征和碳水化合物相互作用特性的信息有限。本研究调查了从南美肺鱼 () 的 RNA-seq 数据中鉴定出的一种凝集素转录本，即 LpITLN2-B。结构分析预测 LpITLN2-B 是一种具有纤维蛋白原样功能域 (FReD) 的同三聚体球形蛋白，分子量为 57 kDa。四级结构分为三个单体 A、B 和 C，每个结构域包含 11 个 β-折叠：反平行 β-折叠、β-发夹和无规 β-折叠结构。分子对接表明与二糖而不是单糖有显著的相互作用。与二糖的优先相互作用突出了与病原体分子（如 LPS 和 Poly(I:C)）的潜在相互作用。血凝试验抑制了凝集素的活性，特别是麦芽糖和蔗糖，突出了 样品中凝集素的活性。总体而言，我们的结果表明 LpITLN2-B 在 免疫防御针对病原体方面具有潜在的相关性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8963/11084424/b02858298f33/ijms-25-04798-g009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8963/11084424/1ba47ba0dff8/ijms-25-04798-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8963/11084424/145d658c4ad4/ijms-25-04798-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8963/11084424/d7b922711173/ijms-25-04798-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8963/11084424/490ba09fe6fc/ijms-25-04798-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8963/11084424/1f1f2556dae3/ijms-25-04798-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8963/11084424/8111a0cf466f/ijms-25-04798-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8963/11084424/2807ab9dd0d0/ijms-25-04798-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8963/11084424/fcd78c742c8e/ijms-25-04798-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8963/11084424/b02858298f33/ijms-25-04798-g009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8963/11084424/1ba47ba0dff8/ijms-25-04798-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8963/11084424/145d658c4ad4/ijms-25-04798-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8963/11084424/d7b922711173/ijms-25-04798-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8963/11084424/490ba09fe6fc/ijms-25-04798-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8963/11084424/1f1f2556dae3/ijms-25-04798-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8963/11084424/8111a0cf466f/ijms-25-04798-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8963/11084424/2807ab9dd0d0/ijms-25-04798-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8963/11084424/fcd78c742c8e/ijms-25-04798-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8963/11084424/b02858298f33/ijms-25-04798-g009.jpg

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本文引用的文献

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Intelectin enhances the phagocytosis of macrophages via CDC42-WASF2-ARPC2 signaling axis in Megalobrama amblycephala.在团头鲂中，整合素通过CDC42-WASF2-ARPC2信号轴增强巨噬细胞的吞噬作用。
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