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Structure and biological activities of beta toxin from Staphylococcus aureus

被引：133
作者：
Huseby, Medora
Shi, Ke
Brown, C. Kent
Digre, Jeff
Mengistu, Fikre
Seo, Keun Seok
Bohach, Gregory A.
Schlievert, Patrick M.
Ohlendorf, Douglas H.
Earhart, Cathleen A.
机构：
[1] Univ Minnesota, Dept Biochem Mol Biol & Biophys, Minneapolis, MN USA
[2] Univ Minnesota, Dept Microbiol, Minneapolis, MN USA
[3] Univ Idaho, Dept Microbiol Mol Biol & Biochem, Moscow, ID 83843 USA
来源：
JOURNAL OF BACTERIOLOGY | 2007年 / 189卷 / 23期
关键词：
D O I：
10.1128/JB.00741-07
中图分类号：
Q93 [微生物学];
学科分类号：
071005 [微生物学]; 100705 [微生物与生化药学];
摘要：
Beta toxin is a neutral sphingomyelinase secreted by certain strains of Staphylococcus aureus. This virulence factor lyses erythrocytes in order to evade the host immune system as well as scavenge nutrients. The structure of beta toxin was determined at 2.4-angstrom resolution using crystals that were merohedrally twinned. This structure is similar to that of the sphingomyelinases of Listeria ivanovii and Bacillus cereus. Beta toxin belongs to the DNase I folding superfamily; in addition to sphingomyelinases, the proteins most structurally related to beta toxin include human endonuclease HAP1, Escherichia coli endonuclease III, bovine pancreatic DNase I, and the endonuclease domain of TRAS1 from Bombyx mori. Our biological assays demonstrated for the first time that beta toxin kills proliferating human lymphocytes. Structure-directed active site mutations show that biological activities, including hemolysis and lymphotoxicity, are due to the sphingomyelinase activity of the enzyme.
引用
收藏
页码：8719 / 8726
页数：8
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