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Structure and biological activities of beta toxin from Staphylococcus aureus.


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-A 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.

SUBMITTER: Huseby M 

PROVIDER: S-EPMC2168928 | biostudies-literature | 2007 Dec

REPOSITORIES: biostudies-literature

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Structure and biological activities of beta toxin from Staphylococcus aureus.

Huseby Medora M   Shi Ke K   Brown C Kent CK   Digre Jeff J   Mengistu Fikre F   Seo Keun Seok KS   Bohach Gregory A GA   Schlievert Patrick M PM   Ohlendorf Douglas H DH   Earhart Cathleen A CA  

Journal of bacteriology 20070914 23


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-A 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 sphingomyel  ...[more]

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