GSTDTAP  > 地球科学
DOI10.1126/science.aan6874
Eudicot plant-specific sphingolipids determine host selectivity of microbial NLP cytolysins
Lenarcic, Tea1; Albert, Isabell2; Boehm, Hannah2; Hodnik, Vesna1,3; Pirc, Katja1; Zavec, Apolonija B.1; Podobnik, Marjetka1; Pahovnik, David4; Zagar, Ema4; Pruitt, Rory2; Greimel, Peter5,6; Yamaji-Hasegawa, Akiko5,7; Kobayashi, Toshihide5,8; Zienkiewicz, Agnieszka9,10; Goemann, Jasmin9,10; Mortimer, Jenny C.11,12; Fang, Lin11,12; Mamode-Cassim, Adiilah13; Deleu, Magali14; Lins, Laurence14; Oecking, Claudia2; Feussner, Ivo9,10; Mongrand, Sebastien13; Anderluh, Gregor1; Nuernberger, Thorsten2
2017-12-15
发表期刊SCIENCE
ISSN0036-8075
EISSN1095-9203
出版年2017
卷号358期号:6369页码:1431-+
文章类型Article
语种英语
国家Slovenia; Germany; Japan; France; USA; Belgium
英文摘要

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.


领域地球科学 ; 气候变化 ; 资源环境
收录类别SCI-E
WOS记录号WOS:000417918500041
WOS关键词NEP1-LIKE PROTEINS ; IMMUNE-RESPONSES ; ARABIDOPSIS ; TOXIN
WOS类目Multidisciplinary Sciences
WOS研究方向Science & Technology - Other Topics
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引用统计
文献类型期刊论文
条目标识符http://119.78.100.173/C666/handle/2XK7JSWQ/197562
专题地球科学
资源环境科学
气候变化
作者单位1.Natl Inst Chem, Dept Mol Biol & Nanobictechnol, Hajdrihova 19, Ljubljana TEA LENAREI, Slovenia;
2.Eberhard Karls Univ Tubingen, Ctr Plant Mol Biol, Morgenstelle 32, D-72076 Tubingen, Germany;
3.Univ Ljubljana, Dept Biol, Bictech Fac, Jamnikarjeva 101, Ljubljana 1000, Slovenia;
4.Natl Inst Chem, Dept Polymer Chem & Technol, Hajdrihova 19, Ljubljana 1000, Slovenia;
5.RIKEN, Lipid Biol Lab, Wako, Saitama 3510198, Japan;
6.Riken Inst Phys & Chem Res, Lab Cell Funct Dynam, Brain Sci Inst, Wako, Saitama 3510198, Japan;
7.Riken Inst Phys & Chem Res, Mol Membrane Neurosci, Brain Sci Inst, Wako, Saitama 3510198, Japan;
8.Univ Strasbourg, CNRS, UMR 7213, F-67401 Illkirch Graffenstaden, France;
9.Univ Gottingen, Dept Plant Biochem, Albrecht von Haller Inst Plant Sci, Gottingen, Germany;
10.Univ Gottingen, Gottingen Ctr Mol Biosci, Gottingen, Germany;
11.Joint Bioenergy Inst, Emeryville, CA 94608 USA;
12.Lawrence Berkeley Natl Lab, Biosci Div, Berkeley, CA 94720 USA;
13.Univ Bordeaux, CNRS, UMR 5200, Lab Biogenese Membranaire, 71 Ave Edouard Bourlaux, F-33883 Villenave Dornon, France;
14.Univ Liege, Lab Mol Biophys Interfaces, Gembloux, Belgium
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GB/T 7714
Lenarcic, Tea,Albert, Isabell,Boehm, Hannah,et al. Eudicot plant-specific sphingolipids determine host selectivity of microbial NLP cytolysins[J]. SCIENCE,2017,358(6369):1431-+.
APA Lenarcic, Tea.,Albert, Isabell.,Boehm, Hannah.,Hodnik, Vesna.,Pirc, Katja.,...&Nuernberger, Thorsten.(2017).Eudicot plant-specific sphingolipids determine host selectivity of microbial NLP cytolysins.SCIENCE,358(6369),1431-+.
MLA Lenarcic, Tea,et al."Eudicot plant-specific sphingolipids determine host selectivity of microbial NLP cytolysins".SCIENCE 358.6369(2017):1431-+.
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