关键词: Binding protein Carbohydrate-mediated interaction Glycolipids Norovirus Sulfatide

来  源:   DOI:10.1093/jb/mvae051

Abstract:
Noroviruses are a prevalent cause of human viral gastroenteritis, yet the precise mechanisms underlying their infection cycle, particularly their interactions with and entry into cells, remain poorly understood. Human norovirus (HuNoV) primarily targets human small intestinal epithelial cells, within which 3-O sulfogalactosylceramide (sulfatide) ranks among the most abundant glycosphingolipids (GSLs). While sulfatide involvement in the binding and infection mechanism of several viruses has been documented, its interaction with noroviruses remains underexplored. This study investigated whether noroviruses interact with sulfatide. We found that the recombinant viral capsid protein VP1 of HuNoV (genogroups I and II) and murine norovirus (genogroup V) exhibited robust binding to sulfatide compared with other tested GSLs using ELISA, TLC binding assay, and qRT-PCR binding assay. Notably, we found that sulfatide is a novel binding target for norovirus particles. Overall, our findings reveal a previously unknown norovirus-sulfatide interaction, proposing sulfatide as a potential candidate for norovirus infection receptors.
摘要:
诺罗病毒是人类病毒性胃肠炎的流行原因,然而,它们感染周期背后的确切机制,特别是它们与细胞的相互作用和进入细胞,仍然知之甚少。人类诺如病毒(HuNoV)主要针对人类小肠上皮细胞,其中3-O磺基半乳糖基神经酰胺(硫酸盐)是最丰富的鞘糖脂(GSL)之一。虽然硫苷脂参与几种病毒的结合和感染机制已被证明,它与诺如病毒的相互作用仍未充分开发。这项研究调查了诺如病毒是否与硫苷脂相互作用。我们发现,与其他使用ELISA测试的GSL相比,HuNoV(基因组I和II)和鼠诺如病毒(基因组V)的重组病毒衣壳蛋白VP1表现出与硫苷脂的牢固结合,TLC结合测定,和qRT-PCR结合测定。值得注意的是,我们发现硫酸脂是诺如病毒颗粒的一种新的结合靶标。总的来说,我们的发现揭示了以前未知的诺如病毒-硫酸脂相互作用,建议硫苷脂作为诺如病毒感染受体的潜在候选者。
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