Hostname: page-component-8448b6f56d-sxzjt Total loading time: 0 Render date: 2024-04-19T07:57:59.006Z Has data issue: false hasContentIssue false
  • English
  • Français

The serum opacity reaction of Streptococcus pyogenes: general properties of the streptococcal factor and of the reaction in aged serum*

Published online by Cambridge University Press:  15 May 2009

M. J. Hill  and
Lewis W. Wannamaker
M. J. Hill
Affiliation:
Departments of Pediatrics and Microbiology, University of Minnesota Medical School, Minneapolis, Minnesota, U.S.A.
Lewis W. Wannamaker
Affiliation:
Departments of Pediatrics and Microbiology, University of Minnesota Medical School, Minneapolis, Minnesota, U.S.A.
Rights & Permissions [Opens in a new window]

Summary

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

The capacity of certain strains of Streptococcus pyogenes to produce opacity in aged horse serum has been studied. Cells from all stages of the growth cycle are able to produce opacity. Maximal activity is reached towards the end of the exponential phase of growth.

Examination of cell fractions obtained by mechanical breakage and differential centrifugation suggested that the cell-bound activity is predominantly associated with the membrane fraction. Extraction with sodium deoxycholate yields a soluble fraction of high activity.

There is considerable strain variation in heat stability of the serum opacity factor. Cell-bound activity is often quite resistant to heat, whereas extracted activity is less stable.

Low concentrations of divalent cations have an activating effect, whereas high concentrations inhibit the serum opacity reaction. High concentrations of uni-valent cations are without effect on the cell-free enzyme but have an activating effect on the cell-bound enzyme.

For both the cell-bound and the cell-free enzyme the pH optimum was 5·8.

Although sensitive to trypsin and pepsin, the serum opacity factor appears to be resistant to streptococcal proteinase. Its activity is destroyed by formaldehyde and by periodate but is unaffected by a number of reducing agents.

Pre-heating of the serum or the addition of iodoacetate did not affect the serum opacity reaction. The enhanced cholesterol esterification previously described with fresh serum appears to be a secondary reaction. Even when isolated by relatively gentle methods, α-lipoprotein serves as a substrate only in the presence of crystalline serum albumin.

Type
Research Article
Information
Journal of Hygiene , Volume 66 , Issue 1 , March 1968 , pp. 37 - 47
Copyright
Copyright © Cambridge University Press 1968

References

REFERENCES

Duncombe, W. G. (1963). The colourimetric micro-determination of long chain fatty acids. Biochem. J. 88, 7.CrossRefGoogle ScholarPubMed
Freimer, E. H. (1963). Studies of L-forms and protoplasts of group A streptococci. J. exp Med. 117, 377.CrossRefGoogle ScholarPubMed
Gillespie, W. A. & Alder, V. G. (1952). Production of opacity in egg yolk media by coagu-lase positive staphylococci. J. Path. Bact. 64, 187.CrossRefGoogle ScholarPubMed
Ginsburg, I., Harris, T. N. & Grossowicz, N. (1963). Oxygen stable hemolysins of group A streptococci. J. exp. Med. 118, 905.CrossRefGoogle ScholarPubMed
Gooder, H. (1961). Association of the serum opacity reaction with serological type in Str. pyogenes. J. gen. Microbiol. 25, 347.CrossRefGoogle Scholar
Griffith, F. (1934). The serological classification of Streptococcus pyogenes. J. Hyg., Camb. 34, 542.Google ScholarPubMed
Hill, M. J. (1967). Action of bile salts on bacterial cell walls. Nature, Lond. 214, 1152.CrossRefGoogle ScholarPubMed
Kingsley, G. R. & Schaffert, R. R. (1949). Determination of free and total cholesterol by direct chloroform extraction. J. biol. Chem. 180, 315.CrossRefGoogle ScholarPubMed
Köhler, W. (1963). Serum-Opazitäts-Reaktion (SOR) und die Bildung des M-antigens durch Streptococcus pyogenes. Zentbl. Bakt. ParasitKde, Abt. 1, Orig. 189, 275.Google Scholar
Korn, E. D. (1959). Serum lipoprotein lipase. Meth. biochem. Analysis 7, 145.CrossRefGoogle Scholar
Krumwiede, E. (1954). Studies on a Kpoproteinase of group A streptococci. J. exp. Med. 100, 629.CrossRefGoogle ScholarPubMed
Lowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. (1951). Protein measurement with the Folin phenol reagent. J. biol. Chem. 193, 265.CrossRefGoogle ScholarPubMed
Maxted, W. R. (1957). The active agent in nascent phage lysis of streptococci. J. gen. Microbiol. 16, 584.CrossRefGoogle ScholarPubMed
Michel, M. F. & Gooder, H. (1962). Amino acids, amino sugars and sugars present in the cell wall of some strains of Streptococcus pyogenes. J. gen. Microbiol. 29, 199.CrossRefGoogle ScholarPubMed
Rowen, R. (1961). The release of cholesterol esters from serum lipoproteins by extracts of certain group A streptococci. J. exp. Med. 114, 807.CrossRefGoogle Scholar
Rowen, R. & Martin, J. (1963). Enhancement of cholesterol esterification in serum by an extract of a group A streptococcus. Biochim. biophys. Acta 70, 396.CrossRefGoogle ScholarPubMed
Swift, H. F., Wilson, A. T. & Lancefield, R. C. (1943). Typing of group A hemolytic streptococci by M precipitin reactions in capillary pipettes. J. exp. Med. 78, 127.CrossRefGoogle Scholar
Top, F. H. Jr. & Wannamaker, L. W. (1968). The serum opacity reaction of Streptococcus pyogenes: frequency of production of streptococcal lipoproteinase by strains of different serological types and relationship to M protein production. J. Hyg., Camb. 66, 49.CrossRefGoogle ScholarPubMed
Ward, H. K. & Rudd, G. V. (1938). Studies on haemolytic streptococci from human sources: the cultural characteristics for potentially virulent strains. Aust. J. exp. Biol. med. Sci. 16, 181.CrossRefGoogle Scholar