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[The hydrophobicity of Streptococcus pyogenes as a possible marker of its virulence].

The hydrophobicity of 366 S. pyogenes cultures isolated from the pharynx of tonsillitis and scarlet fever patients and healthy children, as well as museum strain of type M29, was studied. The study revealed that the hydrophobicity of cultures isolated from scarlet fever patients exceeded that of cultures isolated from healthy carriers and tonsillitis patients. Among S. pyogenes cultures isolated in cases of prolonged carriership a considerable proportion of highly hydrophobic cultures was detected, which was probably indicative of an important role played by the hydrophobicity of streptococci in retaining them on the barrier epithelium. This was confirmed by the presence of correlation between the hydrophobicity of culture of S. pyogenes, type M29, and its adhesion to the fibronectin receptor and HEp-2 cells. For S. pyogenes of type M6, epidemic in the group of children under observation during the period of 1987-1988, the values characterizing its hydrophobicity were registered which significantly exceeded average hydrophobicity values. At the period of a rise in morbidity S. pyogenes cultures were characterized by significantly higher hydrophobicity. The variability of the hydrophobicity index and its relationship with the dissociation of cultures were established. The hydrophobicity index may be used as one of the virulence markers of S. pyogenes strains.

Carrier State↗
PubMed1986

Purification and partial characterization of the nephritis strain-associated protein from Streptococcus pyogenes, group A.

We report the isolation and purification of the nephritis strain-associated protein (NSAP) first described by Villareal et al. (8). Amino acid analysis, and determination of the first 21 amino-terminal amino acids indicated that this 46 kD protein is a streptokinase. Biochemical analysis confirmed that NSAP could act as a plasminogen activator; immunological investigations indicated that NSAP is antigenically different from streptokinase from group C streptococcus, and possibly represents a unique streptokinase. It is this uniqueness that may contribute to the role of NSAP in the pathogenesis of acute poststreptococcal glomerulonephritis.

Amino Acid Sequence↗
PubMed1993

Molecular cloning, identification, and sequence of the hyaluronan synthase gene from group A Streptococcus pyogenes.

The hyaluronan (HA) synthase of Group A Streptococci has been identified by transposon mutagenesis and deletion analysis. The genes for the HA synthase and a recently identified UDP-Glc dehydrogenase (Dougherty, B. A., and van de Rijn, I. (1993) J. Biol. Chem. 268, 7118-7124) reside on a contiguous stretch of 3.2-kilobase pair DNA that can direct HA biosynthesis in Enterococcus faecalis and Escherichia coli as well as mutant Streptococcus (DeAngelis, P. L., Papaconstantinou, J., and Weigel, P. H. (1993) J. Biol. Chem. 268, 14568-14571). The synthase contains 395 residues (calculated Mr = 45,063) and migrates on SDS-PAGE with a molecular mass of 42 kDa. E. coli K5, which synthesizes UDP-glucuronic acid for production of its endogenous capsular polysaccharide, can make HA if it contains a plasmid encoding the intact 42-kDa protein. E. coli SURE or chi 1448 cells containing the same construct, however, cannot produce HA since these strains cannot make both required sugar nucleotide precursors. The HA synthase is predicted to be an integral membrane protein with four membrane-associated helices, which is consistent with the location of the enzyme activity in Streptococci. There is significant homology between the HA synthase and the Rhizobium nodC gene product, an enzyme that synthesizes chitin-like oligomers. This is the first description at the molecular level of an enzyme shown to synthesize a glycosaminoglycan.

Amino Acid Sequence↗