Structures of Lysenin Reveal a Shared Evolutionary Origin for Pore-Forming Proteins And Its Mode of Sphingomyelin Recognition

被引：81

作者：

De Colibus, Luigi ^{[4
]}

Sonnen, Andreas F-P ^{[2
,4
]}

Morris, Keith J.

Siebert, C. Alistair ^{[4
]}

Abrusci, Patrizia ^{[1
]}

Plitzko, Juergen ^{[2
]}

Hodnik, Vesna ^{[3
]}

Leippe, Matthias ^{[5
]}

Volpi, Emanuela

Anderluh, Gregor ^{[3
,6
]}

Gilbert, Robert J. C. ^{[4
]}

机构：

[1] Univ Oxford, Sir William Dunn Sch Pathol, Oxford OX1 3RE, England

[2] Max Planck Inst Biochem, Dept Mol Struct Biol, D-82152 Martinsried, Germany

[3] Univ Ljubljana, Dept Biol, Biotech Fac, Ljubljana 1000, Slovenia

[4] Univ Oxford, Wellcome Trust Ctr Human Genet, Div Struct Biol, Oxford OX3 7BN, England

[5] Univ Kiel, Inst Zool, Dept Zoophysiol, D-24098 Kiel, Germany

[6] Natl Inst Chem, Ljubljana 1000, Slovenia

来源：

STRUCTURE | 2012年 / 20卷 / 09期

基金：

英国生物技术与生命科学研究理事会; 英国惠康基金;

关键词：

CRYSTAL-STRUCTURE; MAXIMUM-LIKELIHOOD; TOXIN; RESOLUTION; REFINEMENT; SOFTWARE; LEUKEMIA;

D O I：

10.1016/j.str.2012.06.011

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Pore-forming proteins insert from solution into membranes to create lesions, undergoing a structural rearrangement often accompanied by oligomerization. Lysenin, a pore-forming toxin from the earthworm Eisenia fetida, specifically interacts with sphingomyelin (SM) and may confer innate immunity against parasites by attacking their membranes to form pores. SM has important roles in cell membranes and lysenin is a popular SM-labeling reagent. The structure of lysenin suggests common ancestry with other pore-forming proteins from a diverse set of eukaryotes and prokaryotes. The complex with SM shows the mode of its recognition by a protein in which both the phosphocholine headgroup and one acyl tail are specifically bound. Lipid interaction studies and assays using viable target cells confirm the functional reliance of lysenin on this form of SM recognition.

引用

页码：1498 / 1507

页数：10

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