Staphylococcal enterotoxin B (SEB) and
toxic shock syndrome toxin-1 are the super
antigens responsible for diseases such as
staphylococcal food poisoning and
toxic shock syndrome. At low serum concentrations, SEB can trigger
toxic shock, profound
hypotension and multi organ failure and hence is recognized as biowarfare molecule. In this study, a multidomain fusion
protein (r-TE) was generated with specificity for SEB and
toxic shock syndrome toxin (Tsst-1). The fusion gene comprising the conserved regions of seb and the tsst genes was
codon-optimized for expression in Escherichia coli and encoded a 26 kDa recombinant multidomain chimeric
protein (r-TE). Hyperimmune antiserum raised against r-TE specifically reacted with SEB (~28 kDa) and
Tsst-1 (~22 kDa) components during Western blot analysis and by plate ELISA in confirmed toxin producing strains of S. aureus. The antigenicity of the SEB component of the r-TE
protein was also confirmed using TECRA kit. The described procedure of creating a single
protein molecule carrying components of two different toxins whilst still retaining the original
antigenic determinants of individual toxins proved highly advantageous in the development of rapid, reliable and cost effective immunoassays and may also have the potential to serve as candidate molecule for
vaccine studies.