Scholarlink

<p>Schistosomes are parasitic worms responsible for devastating chronic disease including intestinal and urogenital pathologies. In-depth studies of the <i>Schistosoma mansoni</i> glycome have revealed complex, immunogenic and life stage-specific glycans, that are crucial in host-parasite interactions. Despite causing the majority of schistosome infections and specific associated pathology, the glycosylation of <i>S. haematobium</i> remains largely unstudied. Here, we characterize the glycan repertoire of <i>S. haematobium</i> using mass spectrometry-based approaches. We report substantial differences to <i>S. mansoni</i> glycans, most notably in the core structure, fucosylation patterns and glucuronic acid modifications of glycosphingolipid (GSL) glycans. Furthermore, IgG from <i>S. haematobium</i>-infected individuals preferentially bind the acidic GSL glycans compared to IgG from <i>S. mansoni</i>-infected individuals. Our results demonstrate that <i>S. haematobium</i> and <i>S. mansoni</i> are differentially glycosylated and that <i>S. haematobium</i> glycans are involved in parasite-host immunobiology. The specific, immunogenic <i>S. haematobium</i> glycans constitute targets for use in epidemiological studies and potential species-specific diagnostics.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Major human schistosome species express different glycans with immunological and diagnostic implications

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年3月23日

查看全文
  • Laudine M. C. Petralia,
  • Angela van Diepen,
  • Tao Zhang,
  • Anna O. Kildemoes,
  • Tom Veldhuizen,
  • D. Linh Nguyen,
  • Cornelis H. Smit,
  • Peter G. Kremsner,
  • Manfred Wuhrer,
  • Jeremy M. Foster,
  • Cornelis H. Hokke

摘要

Schistosomes are parasitic worms responsible for devastating chronic disease including intestinal and urogenital pathologies. In-depth studies of the Schistosoma mansoni glycome have revealed complex, immunogenic and life stage-specific glycans, that are crucial in host-parasite interactions. Despite causing the majority of schistosome infections and specific associated pathology, the glycosylation of S. haematobium remains largely unstudied. Here, we characterize the glycan repertoire of S. haematobium using mass spectrometry-based approaches. We report substantial differences to S. mansoni glycans, most notably in the core structure, fucosylation patterns and glucuronic acid modifications of glycosphingolipid (GSL) glycans. Furthermore, IgG from S. haematobium-infected individuals preferentially bind the acidic GSL glycans compared to IgG from S. mansoni-infected individuals. Our results demonstrate that S. haematobium and S. mansoni are differentially glycosylated and that S. haematobium glycans are involved in parasite-host immunobiology. The specific, immunogenic S. haematobium glycans constitute targets for use in epidemiological studies and potential species-specific diagnostics.