Staphylococcus saprophyticus hemagglutinin is a 160-kilodalton surface polypeptide.

AUTOR(ES)

Gatermann, S

RESUMO

Many strains of Staphylococcus saprophyticus cause direct hemagglutination of sheep erythrocytes. For a high proportion of clinical isolates, a surface protein (Ssp) that is apparently not involved in this property has been described. In this study, S. saprophyticus CCM883, a hemagglutinating but Ssp-negative strain, was used for the identification, purification, and characterization of a 160-kDa surface polypeptide that appears to be the major component of the hemagglutinin. Expression of the protein required the addition to the growth medium of EDTA in micromolar quantities, suggesting an inhibitory role for some unidentified metal ion. The protein was purified by means of Sephacryl S-300 chromatography, and antisera were raised in rabbits. Antibody against this protein inhibited the hemagglutination of two other, unrelated strains and was used to demonstrate, by electron microscopy, the presence of the protein on the surface of the cells. In a confirmatory experiment, the purified antigen was incubated with erythrocytes and binding was detected by the Western immunoblot technique with the antibody to the 160-kDa polypeptide. These experiments indicate that this surface protein is the hemagglutinin of S. saprophyticus.

Documentos Relacionados

• A 160-kilodalton epithelial cell surface glycoprotein recognized by plant lectins that inhibit the adherence of Actinomyces naeslundii.
• Staphylococcus saprophyticus hemagglutinin binds fibronectin.
• The hemagglutinin of Staphylococcus saprophyticus is a major adhesin for uroepithelial cells.
• Identification of the gene family encoding the 160-kilodalton Trypanosoma cruzi complement regulatory protein.
• Multiple Signal Input and Output Domains of the 160-Kilodalton Nuclear Receptor Coactivator Proteins