Structural evidence for the evolution of pyrogenic toxin superantigens.

Mitchell, D T; Levitt, D G; Schlievert, P M; Ohlendorf, D H

Mitchell, D T; Levitt, D G; Schlievert, P M; Ohlendorf, D H.

Afiliación

Mitchell DT; Department of Biochemistry, University of Minnesota Medical School, 6-155 Jackson Hall, 321 Church St. SE, Minneapolis, MN 55455, USA.

J Mol Evol ; 51(6): 520-31, 2000 Dec.

Article en En | MEDLINE | ID: mdl-11116326

RESUMEN

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 AB(5) heat-labile enterotoxins, cholera toxin, pertussis toxin, and verotoxin. The strong structural homology between the pyrogenic toxins and other bacterial proteins suggests that the PTSAgs evolved through the recombination of two smaller beta-strand motifs.

Asunto(s)

Toxinas Bacterianas/genética; Evolución Molecular; Staphylococcus aureus/genética; Streptococcus pyogenes/genética; Superantígenos/genética; Secuencias de Aminoácidos; Secuencia de Aminoácidos; Toxinas Bacterianas/química; Enterotoxinas/química; Enterotoxinas/genética; Datos de Secuencia Molecular; Conformación Proteica; Homología de Secuencia de Aminoácido; Staphylococcus aureus/inmunología; Streptococcus pyogenes/inmunología; Superantígenos/química

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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Staphylococcus aureus / Streptococcus pyogenes / Toxinas Bacterianas / Superantígenos / Evolución Molecular Idioma: En Revista: J Mol Evol Año: 2000 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Alemania

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