Group B streptococcal neuraminidase is actually a hyaluronidase.
The extracellular group B streptococcal enzyme described in numerous reports as a neuraminidase is really a hyaluronidase. Over the past 25 years, the enzyme was routinely assayed with bovine submaxillary mucin as the substrate and by the thiobarbituric acid procedure to measure released sialic acid. Characterization of the actual compound released by the enzyme revealed it to be an alpha,beta-unsaturated derivative of hyalobiuronic acid that was derived from hyaluronic acid contaminating the mucin preparation. Previous reports describing an association of elevated levels of extracellular neuraminidase with virulent strains of group B streptococci must be reevaluated with the recognition that the enzyme is really a hyaluronidase.
Pritchard
D G
DG
School of Medicine Joint Departments, University of Alabama, Birmingham35294.
Lin
B
B
D000595:Amino Acid Sequence; D006821:Hyaluronoglucosaminidase / Q000032:analysis* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D009439:Neuraminidase / Q000032:analysis* / Q000302:isolation & purification; D013292:Streptococcus agalactiae / Q000201:enzymology* / Q000472:pathogenicity; D013379:Substrate Specificity; D014774:Virulence
D009439:Neuraminidase; D006821:Hyaluronoglucosaminidase