Structure and biological activities of beta toxin from Staphylococcus aureus

Medora Huseby, Ke Shi, C. Kent Brown, Jeff Digre, Fikre Mengistu, Seok Seo Keun, Gregory A. Bohach, Patrick M. Schlievert, Douglas H. Ohlendorf, Cathleen A. Earhart

Research output: Contribution to journalArticlepeer-review

83 Scopus citations

Abstract

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-Å 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.

Original languageEnglish (US)
Pages (from-to)8719-8726
Number of pages8
JournalJournal of bacteriology
Volume189
Issue number23
DOIs
StatePublished - Dec 2007

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