Structure and Biological Activities of Beta Toxin from Staphylococcus aureus-Reference-Cited by-同舟云学术

Structure and Biological Activities of Beta Toxin from Staphylococcus aureus

Published:2007-12 Issue:23 Volume:189 Page:8719-8726
ISSN:0021-9193
Container-title:Journal of Bacteriology
language:en
Short-container-title:J Bacteriol

Author:

Huseby Medora¹,Shi Ke¹,Brown C. Kent¹,Digre Jeff¹,Mengistu Fikre¹,Seo Keun Seok²,Bohach Gregory A.²,Schlievert Patrick M.³,Ohlendorf Douglas H.¹,Earhart Cathleen A.¹

Affiliation:

1. Department of Biochemistry, Molecular Biology and Biophysics

2. Department of Microbiology, Molecular Biology and Biochemistry, University of Idaho, Moscow, Idaho

3. Department of Microbiology, University of Minnesota, Minneapolis, Minnesota

Abstract

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.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/JB.00741-07

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