Rodero Marta, Romero Sara, Valcárcel Ángela, González-Fernández Juan, Olmeda A Sonia, Valcárcel Félix, Daschner Alvaro, Cuéllar Carmen
Departamento de Microbiología y Parasitología, Facultad de Farmacia, Universidad Complutense de Madrid, 28040 Madrid, Spain.
UCD Veterinary Sciences Centre, University College Dublin, Belfield, D04 V1W8 Dublin, Ireland.
Pathogens. 2025 Aug 7;14(8):789. doi: 10.3390/pathogens14080789.
This study investigates the potential of sp. as a novel source of α-Gal (Galα1-3Galβ1-4GlcNAc-R) epitopes capable of inducing allergic sensitization in humans. While α-Gal is classically associated with delayed IgE-mediated hypersensitivity following tick bites, emerging evidence suggests that parasitic helminths such as sp. may also express α-Gal-containing glycoconjugates, offering an alternative sensitization pathway. Protein extracts from sp. third-stage larvae and mammalian tissues (beef, pork) were analyzed by SDS-PAGE and Western blot using a monoclonal anti-α-Gal antibody (clone M86), and α-Gal epitopes were detected by ELISA. Sera from urticaria patients, stratified by sp. sensitization status, were evaluated for anti-α-Gal IgG, IgE, and IgG4 antibodies. Inhibition assays assessed cross-reactivity. Results confirmed the presence of α-Gal epitopes on sp. proteins, with prominent bands at ~250 kDa and 65 kDa. Urticaria patients sensitized to sp. exhibited significantly elevated anti-α-Gal antibody levels compared to controls. Inhibition ELISA demonstrated substantial reduction in antibody binding with sp. extracts, indicating shared antigenic determinants with mammalian α-Gal. These findings establish sp. as a source of α-Gal-containing glycoproteins capable of eliciting specific antibody responses in humans, highlighting a potential parasitic route for α-Gal sensitization.
本研究调查了[某种寄生虫名称]作为一种新型α-半乳糖(Galα1-3Galβ1-4GlcNAc-R)表位来源的潜力,该表位能够在人类中诱导过敏致敏。虽然α-半乳糖传统上与蜱叮咬后延迟的IgE介导的超敏反应相关,但新出现的证据表明,诸如[某种寄生虫名称]等寄生蠕虫也可能表达含α-半乳糖的糖缀合物,提供了一种替代的致敏途径。使用单克隆抗α-半乳糖抗体(克隆M86)通过SDS-PAGE和蛋白质印迹分析了[某种寄生虫名称]第三期幼虫和哺乳动物组织(牛肉、猪肉)的蛋白质提取物,并通过ELISA检测α-半乳糖表位。对根据[某种寄生虫名称]致敏状态分层的荨麻疹患者血清进行抗α-半乳糖IgG、IgE和IgG4抗体评估。抑制试验评估交叉反应性。结果证实[某种寄生虫名称]蛋白质上存在α-半乳糖表位,在约250 kDa和65 kDa处有明显条带。与对照组相比,对[某种寄生虫名称]致敏的荨麻疹患者的抗α-半乳糖抗体水平显著升高。抑制ELISA表明与[某种寄生虫名称]提取物的抗体结合大幅减少,表明与哺乳动物α-半乳糖存在共同的抗原决定簇。这些发现确定[某种寄生虫名称]为一种含α-半乳糖糖蛋白的来源,能够在人类中引发特异性抗体反应,突出了α-半乳糖致敏的潜在寄生途径。