Journal
JOURNAL OF BACTERIOLOGY
Volume 189, Issue 23, Pages 8719-8726Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.00741-07
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Funding
- NCRR NIH HHS [P20 RR15587, P20 RR016454, P20 RR015587] Funding Source: Medline
- NHLBI NIH HHS [R01 HL036611, R01 HL36611] Funding Source: Medline
- NIAID NIH HHS [R01 AI057585, R01 AI57585] Funding Source: Medline
- NIDCR NIH HHS [T32 DE007288, 5T32-DE007288-11] Funding Source: Medline
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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.
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