Attachment of human noroviruses to histo blood group antigens (HBGAs) is thought to be essential for infection, although how this binding event promotes infection is unknown. Recent studies have shown that 60% of all GII.4 epidemic strains may undergo a spontaneous post-translational modification (PTM) in an amino acid located adjacent to the binding pocket for HBGAs. This transformation proceeds with an estimated half-life of 1–2 days under physiological conditions, dramatically affecting HBGA recognition. The surface-exposed position of this PTM and its sequence conservation suggests a relevant role in immune escape and host-cell recognition. As a first step towards the understanding of the biological implications of this PTM at atomic resolution, we report the complete assignment of methyl resonances of a MIL^ProSV^ProSA methyl-labeled sample of a 72 kDa protruding domain from a GII.4 Saga human norovirus strain. Assignments were obtained from methyl–methyl NOESY experiments combined with site-directed mutagenesis and automated assignment. This data provides the basis for a detailed characterization of the PTM-driven modulation of immune recognition in human norovirus on a molecular level.

中文翻译：

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从人诺如病毒GII.4 Saga完全突出突出域的Ala，Ile，LeuProS，Met和ValProS甲基。

尽管这种结合事件如何促进感染尚不明确，但人类诺如病毒在组织血型抗原（HBGA）上的附着被认为是必不可少的。最近的研究表明，所有GII.4流行株中有60％可能在与HBGA结合袋相邻的氨基酸中进行自发的翻译后修饰（PTM）。在生理条件下，这种转化的估计半衰期为1-2天，从而极大地影响了HBGA的识别。该PTM的表面暴露位置及其序列保守性提示免疫逃逸和宿主细胞识别中的相关作用。作为了解此PTM在原子分辨率下的生物学意义的第一步，我们报告了MIL ^ProS甲基共振的完整分配V ^ProS来自GII.4 Saga人诺如病毒株的72 kDa突出结构域的甲基标记样品。分配是从甲基-甲基NOESY实验结合定点诱变和自动分配获得的。该数据为在分子水平上详细表征人诺如病毒中PTM驱动的免疫识别调节提供了基础。