Literature DB >> 17873030

Structure and biological activities of beta toxin from Staphylococcus aureus.

Medora Huseby1, Ke Shi, C Kent Brown, Jeff Digre, Fikre Mengistu, Keun Seok Seo, Gregory A Bohach, Patrick M Schlievert, Douglas H Ohlendorf, Cathleen A Earhart.   

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.

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Year:  2007        PMID： 17873030      PMCID： PMC2168928          DOI： 10.1128/JB.00741-07

Source DB:  PubMed          Journal:  J Bacteriol        ISSN： 0021-9193            Impact factor:   3.490


  32 in total

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  62 in total

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2.  Structure of a mutant β toxin from Staphylococcus aureus reveals domain swapping and conformational flexibility.

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5.  Characterization of hemolysins of Staphylococcus strains isolated from human and bovine, southern Iran.

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Review 6.  The rise and rise of Staphylococcus aureus: laughing in the face of granulocytes.

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Review 8.  Inflammasome Activation Can Mediate Tissue-Specific Pathogenesis or Protection in Staphylococcus aureus Infection.

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9.  A critical role for hemolysins and bacterial lipoproteins in Staphylococcus aureus-induced activation of the Nlrp3 inflammasome.

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10.  Inactivation of staphylococcal virulence factors using a light-activated antimicrobial agent.

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