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在条纹鲈()组织中表达的一种“原”型半乳糖凝集素会释放到表皮黏液中,并与细菌和黏液聚糖结合。

A "proto" type galectin expressed in striped bass () tissues is released to epidermal mucus and binds to bacterial and mucus glycans.

作者信息

Henrikson Davin E, Ahmed Hafiz, Tasumi Satoshi, Gokara Mahesh, Feng Chiguang, Abernathy Kelsey, Iqbal Muddassar, Bianchet Mario A, Vasta Gerardo R

机构信息

Department of Microbiology and Immunology, University of Maryland School of Medicine, University of Maryland Baltimore (UMB), Baltimore, MD, United States.

Institute of Marine and Environmental Technology, Columbus Center, Baltimore, MD, United States.

出版信息

Front Cell Infect Microbiol. 2025 May 14;15:1572734. doi: 10.3389/fcimb.2025.1572734. eCollection 2025.

Abstract

Like all aquatic vertebrates and invertebrates, teleost fish are subject to the constant pressure of bacterial, fungal, and parasitic organisms present in the environmental interface that can potentially cause disease. Numerous defense molecules, including galectins, have been isolated from the skin and gut tissues of several marine and freshwater fish species. To provide new insights into the potential role(s) of galectins in the teleost fish innate immune system, we carried out studies on the striped bass (), a keystone fish species in Chesapeake Bay. We purified from epidermal skin mucus, and skin and muscle tissue, a 15-kDa galectin that we designated Msgal1-L1 ( galectin1-like protein 1). Both the transcript sequence and gene organization of Msgal1-L1 suggested a close relationship to the zebrafish galectin Drgal1-L2 and other proto type galectins from vertebrates, including the mammalian galectin-1. Glycan microarray analysis of Msgal1-L1 revealed a binding preference for Galβ1,4GlcNAc, and a homology structural model identified the amino acids involved in ligand recognition, both observations consistent with proto type galectins. Immunohistological examination localized Msgal1-L1 to epithelial and macrophage-/fibroblast-like cells in mucosal tissues, including skin and gill. The preliminary localization of Msgal1-L1 in free macrophage-like cells in epidermal mucus was corroborated by immunofluorescence analysis of macrophages isolated from head kidney. Msgal1-L1 binds in a carbohydrate-specific manner to O-glycosylated components of epidermal mucus. Msgal1-L1 agglutinated environmental bacterial species and strains, some of which are recognized fish pathogens, such as and spp. A microbial microarray analysis revealed that it preferentially binds to bacterial exopolysaccharides (e.g., and spp.) as well as various lipopolysaccharide O-antigen serotypes of spp. A preliminary solid-phase assay showed that Msgal1-L1 strongly bound sp., but very weakly to , an endemic pathogen of striped bass in Chesapeake Bay. Taken together, this evidence suggests that Msgal1-L1 may function in defense recognition against environmental bacteria by agglutinating and/or cross-linking them to mucus oligosaccharides to immobilize them within the epidermal mucus film and prevent their access to the fish epithelial cell surface. would evade this defense mechanism to reach and infect the fish skin epithelial layer.

摘要

与所有水生脊椎动物和无脊椎动物一样,硬骨鱼受到环境界面中存在的细菌、真菌和寄生虫的持续压力,这些生物可能会引发疾病。人们已经从几种海洋和淡水鱼类的皮肤和肠道组织中分离出了许多防御分子,包括半乳糖凝集素。为了深入了解半乳糖凝集素在硬骨鱼先天免疫系统中的潜在作用,我们以条纹鲈(切萨皮克湾的一种关键鱼类)为研究对象展开了研究。我们从表皮黏液、皮肤和肌肉组织中纯化出一种15 kDa的半乳糖凝集素,将其命名为Msgal1-L1(半乳糖凝集素1样蛋白1)。Msgal1-L1的转录本序列和基因结构表明,它与斑马鱼半乳糖凝集素Drgal1-L2以及包括哺乳动物半乳糖凝集素-1在内的其他脊椎动物原型半乳糖凝集素关系密切。对Msgal1-L1的聚糖微阵列分析显示,它对Galβ1,4GlcNAc具有结合偏好,同源结构模型确定了参与配体识别的氨基酸,这两个观察结果都与原型半乳糖凝集素一致。免疫组织学检查将Msgal1-L1定位到黏膜组织(包括皮肤和鳃)中的上皮细胞以及巨噬细胞样/成纤维细胞样细胞。从头部肾脏分离出的巨噬细胞的免疫荧光分析证实了Msgal1-L1在表皮黏液中游离巨噬细胞样细胞中的初步定位。Msgal1-L1以碳水化合物特异性方式与表皮黏液的O-糖基化成分结合。Msgal1-L1凝集环境中的细菌种类和菌株,其中一些是公认的鱼类病原体,如[具体细菌名称1]和[具体细菌名称2]等。微生物微阵列分析表明,它优先结合细菌胞外多糖(如[具体细菌名称3]和[具体细菌名称4]等)以及[具体细菌名称5]的各种脂多糖O抗原血清型。初步的固相分析表明,Msgal1-L1与[具体细菌名称6]强烈结合,但与切萨皮克湾条纹鲈的地方性病原体[具体细菌名称7]结合非常弱。综上所述,这些证据表明,Msgal1-L1可能通过将环境细菌凝集和/或交联到黏液寡糖上,使其固定在表皮黏液膜内并阻止它们接触鱼上皮细胞表面,从而在抵御环境细菌的识别中发挥作用。[具体细菌名称7]会避开这种防御机制,从而到达并感染鱼的皮肤上皮层。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb45/12116657/fe8eb402334d/fcimb-15-1572734-g001.jpg

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