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*
Division of Molecular Medicine and
School of Biological Sciences, University of Auckland, Auckland, New Zealand
Recently, we described the identification of novel streptococcal
superantigens (SAgs) by mining the Streptococcus
pyogenes M1 genome database at Oklahoma University.
Here, we report the cloning, expression, and functional analysis of
streptococcal pyrogenic exotoxin (SPE)-J and another novel SAg (SPE-I).
SPE-I is most closely related to SPE-H and staphylococcal enterotoxin
I, whereas SPE-J is most closely related to SPE-C. Recombinant forms of
SPE-I and SPE-J were mitogenic for PBL, both reaching half maximum
responses at 0.1 pg/ml. Evidence from binding studies and cell
aggregation assays using a human B-lymphoblastoid cell line (LG-2)
suggests that both toxins exclusively bind to the polymorphic MHC class
II 
-chain in a zinc-dependent mode but not to the generic MHC class
II 
-chain. The results from analysis by light scattering indicate
that SPE-J exists as a dimer in solution above concentrations of 4.0
mg/ml. Moreover, SPE-J induced a rapid homotypic aggregation of
LG-2 cells, suggesting that this toxin might cross-link MHC class II
molecules on the cell surface by building tetramers of the type
HLA-DR–SPE-J–SPE-J–HLA-DR. SPE-I preferably stimulates T cells
bearing the V18.1 TCR, which is not targeted by any other known SAg.
SPE-J almost exclusively stimulates V2.1 T cells, a V that is
targeted by several other streptococcal SAgs, suggesting a specific
role for this T cell subpopulation in immune defense. Despite a primary
sequence diversity of 51%, SPE-J is functionally indistinguishable
from SPE-C and might play a role in streptococcal disease, which has
previously been addressed to SPE-C.
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