Mycoplasma arthritidis-derived superantigen (MAM) displays DNase activity

FEMS Immunol Med Microbiol. 2007 Mar;49(2):266-71. doi: 10.1111/j.1574-695X.2006.00189.x.

Abstract

Bacterial superantigens are potent stimulators of the immune system. In this study, we expressed recombinant superantigens, which were then affinity purified and used for growth curves and DNase activity assays. Overexpression of Mycoplasma arthritidis-derived superantigen in Escherichia coli reduced bacterial growth. This is unique, as staphylococcal enterotoxin A and toxic shock syndrome toxin-1, expressed in the same vector system, showed no growth impairment. The observed growth inhibition was caused by the DNase activity of recombinant M. arthritidis-derived superantigen, thus describing the first superantigen showing enzymatic activity, which may be a result of the separate evolution of this toxin.

MeSH terms

  • Antigens, Bacterial / genetics
  • Antigens, Bacterial / isolation & purification
  • Antigens, Bacterial / metabolism*
  • Antigens, Bacterial / toxicity
  • Bacterial Toxins / genetics
  • DNA / metabolism*
  • DNA, Bacterial / metabolism*
  • Deoxyribonucleases / genetics
  • Deoxyribonucleases / isolation & purification
  • Deoxyribonucleases / metabolism*
  • Deoxyribonucleases / toxicity
  • Enterotoxins / genetics
  • Escherichia coli / genetics
  • Escherichia coli / growth & development
  • Gene Expression
  • Mycoplasma arthritidis / enzymology*
  • Mycoplasma arthritidis / immunology*
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Recombinant Proteins / toxicity
  • Staphylococcaceae
  • Superantigens / genetics
  • Superantigens / isolation & purification
  • Superantigens / metabolism*
  • Superantigens / toxicity

Substances

  • Antigens, Bacterial
  • Bacterial Toxins
  • DNA, Bacterial
  • Enterotoxins
  • Mycoplasma arthritidis mitogen
  • Recombinant Proteins
  • Superantigens
  • enterotoxin F, Staphylococcal
  • enterotoxin A, Staphylococcal
  • DNA
  • Deoxyribonucleases