TY - JOUR
T1 - Structural evidence for the evolution of pyrogenic toxin superantigens
AU - Mitchell, David T.
AU - Levitt, David G
AU - Schlievert, Patrick M.
AU - Ohlendorf, Douglas H
N1 - Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 2000
Y1 - 2000
N2 - Pathogenic bacteria have evolved a wide variety of toxins to invade and attack host organisms. In particular, strains of the bacteria Staphylococcus aureus and Streptococcus pyogenes produce a family of pyrogenic toxin superantigens (PTSAgs) that can cause illness, e.g., toxic shock syndrome, or synergize with a number of other immune system disorders. The PTSAgs are all similar in size and have a conserved two-domain tertiary fold despite minimal amino acid sequence identity. The tertiary structure of PTSAg domain 1 is similar to the immunoglobulin binding motif of streptococcal proteins G and L. PTSAg domain 2 resembles members of the oligosaccharide/oligonucleotide binding fold family that includes the B subunits of the AB5 heat-labile enterotoxins, cholera toxin, pertussis toxin, and vetotoxin. The strong structural homology between the pyrogenic toxins and other bacterial proteins suggests that the PTSAgs evolved through the recombination of two smaller β-strand motifs.
AB - Pathogenic bacteria have evolved a wide variety of toxins to invade and attack host organisms. In particular, strains of the bacteria Staphylococcus aureus and Streptococcus pyogenes produce a family of pyrogenic toxin superantigens (PTSAgs) that can cause illness, e.g., toxic shock syndrome, or synergize with a number of other immune system disorders. The PTSAgs are all similar in size and have a conserved two-domain tertiary fold despite minimal amino acid sequence identity. The tertiary structure of PTSAg domain 1 is similar to the immunoglobulin binding motif of streptococcal proteins G and L. PTSAg domain 2 resembles members of the oligosaccharide/oligonucleotide binding fold family that includes the B subunits of the AB5 heat-labile enterotoxins, cholera toxin, pertussis toxin, and vetotoxin. The strong structural homology between the pyrogenic toxins and other bacterial proteins suggests that the PTSAgs evolved through the recombination of two smaller β-strand motifs.
KW - Enterotoxins
KW - MHC class II
KW - Protein conformation
KW - Staphylococcus aureus
KW - T-cell receptor
KW - Toxic shock syndrome toxin-1
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U2 - 10.1007/s002390010116
DO - 10.1007/s002390010116
M3 - Article
C2 - 11116326
AN - SCOPUS:0034541702
SN - 0022-2844
VL - 51
SP - 520
EP - 531
JO - Journal of Molecular Evolution
JF - Journal of Molecular Evolution
IS - 6
ER -