Structure and Biological Activities of Beta Toxin from Staphylococcus aureus

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

doi:10.1128/JB.00741-07

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Structure and Biological Activities of Beta Toxin from Staphylococcus aureus

Journal article

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Peer reviewed

Structure and Biological Activities of Beta Toxin from Staphylococcus aureus

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

Journal of bacteriology, Vol.189(23), pp.8719-8726

12/2007

DOI: 10.1128/JB.00741-07

PMCID: PMC2168928

PMID: 17873030

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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.

Molecular Biology of Pathogens

Details

Title: Subtitle: Structure and Biological Activities of Beta Toxin from Staphylococcus aureus
Creators: Medora Huseby - Department of Microbiology, Molecular Biology and Biochemistry, University of Idaho, Moscow, Idaho
Ke Shi - Department of Microbiology, Molecular Biology and Biochemistry, University of Idaho, Moscow, Idaho
C. Kent Brown - Department of Microbiology, Molecular Biology and Biochemistry, University of Idaho, Moscow, Idaho
Jeff Digre - Department of Microbiology, Molecular Biology and Biochemistry, University of Idaho, Moscow, Idaho
Fikre Mengistu - Department of Microbiology, Molecular Biology and Biochemistry, University of Idaho, Moscow, Idaho
Keun Seok Seo - Department of Microbiology, Molecular Biology and Biochemistry, University of Idaho, Moscow, Idaho
Gregory A Bohach - Department of Microbiology, Molecular Biology and Biochemistry, University of Idaho, Moscow, Idaho
Patrick M Schlievert - Department of Microbiology, Molecular Biology and Biochemistry, University of Idaho, Moscow, Idaho
Douglas H Ohlendorf - Department of Microbiology, Molecular Biology and Biochemistry, University of Idaho, Moscow, Idaho
Cathleen A Earhart - Department of Microbiology, Molecular Biology and Biochemistry, University of Idaho, Moscow, Idaho
Resource Type: Journal article
Publication Details: Journal of bacteriology, Vol.189(23), pp.8719-8726
DOI: 10.1128/JB.00741-07
PMID: 17873030
PMCID: PMC2168928
NLM abbreviation: J Bacteriol
ISSN: 0021-9193
eISSN: 1098-5530
Publisher: American Society for Microbiology (ASM)
Language: English
Date published: 12/2007
Academic Unit: Microbiology and Immunology; Internal Medicine
Record Identifier: 9984001216502771

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