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. 1980 Oct;144(1):164–171. doi: 10.1128/jb.144.1.164-171.1980

Purification and partial characterization of neuraminidase from type III group B streptococci.

T W Milligan, S J Mattingly, D C Straus
PMCID: PMC294612  PMID: 6998945

Abstract

Extracellular neuraminidase from a type III fresh clinical isolate of a group B streptococcus was purified by a combination of salt fractionation, affinity chromatography of Affi-Gel blue, ion-exchange chromatography on diethylaminoethylcellulose, and gel filtration on Sephacryl S-200. These procedures yielded enzyme which was purified approximately 1,000-fold compared with the enzyme found in the original supernatant fluid. This type III streptococcal neuraminidase had a molecular weight of approximately 125,000 as estimated by filtration on Sephacryl S-200 and approximately 106,000 when analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. In contrast to the majority of other bacterial neuraminidases, the type III group B streptococcal enzyme had no effect on colominic acid or N-acetylneuramin-lactose; however, it was quite active on bovine submaxillary mucin.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Anthony B. F., Okada D. M. The emergence of group B streptococci in infections of the newborn infant. Annu Rev Med. 1977;28:355–369. doi: 10.1146/annurev.me.28.020177.002035. [DOI] [PubMed] [Google Scholar]
  2. Baker C. J., Barrett F. F. Group B streptococcal infections in infants. The importance of the various serotypes. JAMA. 1974 Nov 25;230(8):1158–1160. [PubMed] [Google Scholar]
  3. Baker C. J., Kasper D. L. Identification of sialic acid in polysaccharide antigens in group B Streptococcus. Infect Immun. 1976 Jan;13(1):284–288. doi: 10.1128/iai.13.1.284-288.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Balke E., Drzeniek R. Untersuchungen über die Clostridium perfringens-Neuraminidase. Z Naturforsch B. 1969 May;24(5):599–603. [PubMed] [Google Scholar]
  5. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1016/0003-2697(76)90527-3. [DOI] [PubMed] [Google Scholar]
  6. Cassidy J. T., Jourdian G. W., Roseman S. The sialic acids. VI. Purification and properties of sialidase from Clostridium perfringens. J Biol Chem. 1965 Sep;240(9):3501–3506. [PubMed] [Google Scholar]
  7. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  8. Davis L., Baig M. M., Ayoub E. M. Properties of extracellular neuraminidase produced by group A streptococcus. Infect Immun. 1979 Jun;24(3):780–786. doi: 10.1128/iai.24.3.780-786.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Drzeniek R. Differences in splitting capacity of virus and V. cholerae neuraminidases on sialic acid type substrates. Biochem Biophys Res Commun. 1967 Mar 21;26(6):631–638. doi: 10.1016/s0006-291x(67)80118-9. [DOI] [PubMed] [Google Scholar]
  10. Drzeniek R. Viral and bacterial neuraminidases. Curr Top Microbiol Immunol. 1972;59:35–74. doi: 10.1007/978-3-642-65444-2_2. [DOI] [PubMed] [Google Scholar]
  11. FARR R. S. A quantitative immunochemical measure of the primary interaction between I BSA and antibody. J Infect Dis. 1958 Nov-Dec;103(3):239–262. doi: 10.1093/infdis/103.3.239. [DOI] [PubMed] [Google Scholar]
  12. Flashner M., Wang P., Hurley J. B., Tanenbaum S. W. Properties of an inducible extracellular neuraminidase from an Arthrobacter isolate. J Bacteriol. 1977 Mar;129(3):1457–1465. doi: 10.1128/jb.129.3.1457-1465.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. GOTTSCHALK A., GRAHAM E. R. 6-alpha-D-Sialyl-N-acetyl-galactosamine: the neuraminidase-susceptible prosthetic group of bovine salivary mucoprotein. Biochim Biophys Acta. 1959 Aug;34:380–391. doi: 10.1016/0006-3002(59)90290-2. [DOI] [PubMed] [Google Scholar]
  14. Glasgow L. R., Paulson J. C., Hill R. L. Systematic purification of five glycosidases from Streptococcus (Diplococcus) pneumoniae. J Biol Chem. 1977 Dec 10;252(23):8615–8623. [PubMed] [Google Scholar]
  15. HUGHES R. C., JEANLOZ R. W. THE EXTRACELLULAR GLYCOSIDASES OF DIPLOCOCCUS PNEUMONIAE. I. PURIFICATION AND PROPERTIES OF A NEURAMINIDASE AND A BETA-GALACTOSIDASE. ACTION ON THE ALPHA-1-ACID GLYCOPROTEIN OF HUMAN PLASMA. Biochemistry. 1964 Oct;3:1535–1543. doi: 10.1021/bi00898a025. [DOI] [PubMed] [Google Scholar]
  16. Hayano S., Tanaka A. Sialidase-like enzymes produced by group A, B, C, G, and L streptococci and by Streptococcus sanguis. J Bacteriol. 1969 Mar;97(3):1328–1333. doi: 10.1128/jb.97.3.1328-1333.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Hemming V. G., Hall R. T., Rhodes P. G., Shigeoka A. O., Hill H. R. Assessment of group B streptococcal opsonins in human and rabbit serum by neutrophil chemiluminescence. J Clin Invest. 1976 Dec;58(6):1379–1387. doi: 10.1172/JCI108593. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Jennings H. J., Rosell K. G., Kasper D. L. Structural determination and serology of the native polysaccharide antigen of type-III group B Streptococcus. Can J Biochem. 1980 Feb;58(2):112–120. doi: 10.1139/o80-016. [DOI] [PubMed] [Google Scholar]
  19. Kane J. A., Karakawa W. W. Existence of multiple immunodeterminants in the type-specific capsular substance of group B type Ia streptococci. Infect Immun. 1978 Mar;19(3):983–991. doi: 10.1128/iai.19.3.983-991.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Kasper D. L., Baker C. J., Baltimore R. S., Crabb J. H., Schiffman G., Jennings H. J. Immunodeterminant specificity of human immunity to type III group B streptococcus. J Exp Med. 1979 Feb 1;149(2):327–339. doi: 10.1084/jem.149.2.327. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Milligan T. W., Baker C. J., Straus D. C., Mattingly S. J. Association of elevated levels of extracellular neuraminidase with clinical isolates of type III group B streptococci. Infect Immun. 1978 Sep;21(3):738–746. doi: 10.1128/iai.21.3.738-746.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Milligan T. W., Straus D. C., Mattingly S. J. Extracellular neuraminidase production by group B streptococci. Infect Immun. 1977 Oct;18(1):189–195. doi: 10.1128/iai.18.1.189-195.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Moriyama T., Barksdale L. Neuraminidase of Corynebacterium diphtheriae. J Bacteriol. 1967 Nov;94(5):1565–1581. doi: 10.1128/jb.94.5.1565-1581.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Stahl W. L., O'Toole R. D. Pneumococcal neuraminidase: purification and properties. Biochim Biophys Acta. 1972 May 12;268(2):480–487. doi: 10.1016/0005-2744(72)90343-9. [DOI] [PubMed] [Google Scholar]
  25. Tai J. Y., Gotschlich E. C., Lancefield R. C. Isolation of type-specific polysaccharide antigen from group B type Ib streptococci. J Exp Med. 1979 Jan 1;149(1):58–66. doi: 10.1084/jem.149.1.58. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Wilkinson H. W., Facklam R. R., Wortham E. C. Distribution by serological type of group B streptococci isolated from a variety of clinical material over a five-year period (with special reference to neonatal sepsis and meningitis). Infect Immun. 1973 Aug;8(2):228–235. doi: 10.1128/iai.8.2.228-235.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]

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