Eudicot plant-specific sphingolipids determine host selectivity of microbial NLP cytolysins
Eudicot plant-specific sphingolipids determine host selectivity of microbial NLP cytolysins
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DOI：
10.1126/science.aan6874
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发表时间：
2017-12-15
期刊：
影响因子：
56.9
通讯作者：
Nuernberger, Thorsten
中科院分区：
文献类型：
--
作者：
Lenarcic, Tea;Albert, Isabell;Nuernberger, Thorsten
坏死蛋白和乙烯诱导肽 1 样 (NLP) 蛋白构成了植物病原细菌、真菌和卵菌产生的蛋白超家族。许多 NLP 是细胞毒素，可促进双子叶植物的微生物感染，但不会促进单子叶植物的微生物感染。在这里，我们报告糖基肌醇磷酸神经酰胺 (GIPC) 鞘脂作为 NLP 毒素受体。 GIPC 组成改变的植物突变体对 NLP 毒素具有更强的抵抗力。结合研究和 X 射线晶体学表明，NLP 与 GIPC 的末端单体己糖部分形成复合物，导致毒素内的构象变化。单子叶植物对 NLP 溶细胞素不敏感的原因可能是 GIPC 头基的长度和 NLP 糖结合位点的结构。我们揭示了 NLP 溶细胞素作用的早期步骤，这些步骤决定了植物进化枝特异性毒素的选择性。
Necrosis and ethylene-inducing peptide 1-like (NLP) proteins constitute a superfamily of proteins produced by plant pathogenic bacteria, fungi, and oomycetes. Many NLPs are cytotoxins that facilitate microbial infection of eudicot, but not of monocot plants. Here, we report glycosylinositol phosphorylceramide (GIPC) sphingolipids as NLP toxin receptors. Plant mutants with altered GIPC composition were more resistant to NLP toxins. Binding studies and x-ray crystallography showed that NLPs form complexes with terminal monomeric hexose moieties of GIPCs that result in conformational changes within the toxin. Insensitivity to NLP cytolysins of monocot plants may be explained by the length of the GIPC head group and the architecture of the NLP sugar-binding site. We unveil early steps in NLP cytolysin action that determine plant clade-specific toxin selectivity.