THE LYSIS OF GROUP A HEMOLYTIC STREPTOCOCCI BY EXTRACELLULAR ENZYMES OF STREPTOMYCES ALBUS

The lysis of group A hemolytic streptococci by extracellular enzymes of Streptomyces albus has been studied. The most favorable material for fractionation of the lytic enzymes was obtained by surface growth on shallow layers of liquid medium containing an acid hydrolysate of casein, glucose, and salts. The results of fractionation experiments show that the potent proetolytic enzyme of Streptomyces albus is not able to lyse group A streptococci, and that the initiation of lysis is dependent upon the action of a second, non-proteolytic enzyme. The nature of the non-proteolytic enzyme has not been determined. It does not appear to be a ribonuclease or a lysozyme-like enzyme.

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THE LYSIS OF GROUP A HEMOLYTIC STREPTOCOCCI BY EXTRACELLULAR ENZYMES OF STREPTOMYCES ALBUS

Journal of Experimental Medicine ◽

10.1084/jem.96.6.569 ◽

1952 ◽

Vol 96 (6) ◽

pp. 569-580 ◽

Cited By ~ 63

Author(s):

Maclyn McCarty

Keyword(s):

Cell Wall ◽

Extracellular Enzymes ◽

Group A Streptococci ◽

Carbohydrate Component ◽

Streptococcal Cell Wall ◽

Intact Cells ◽

Enzymatic Lysis ◽

Streptomyces Albus ◽

Group A ◽

Isolated Cell

Cell wall preparations of uniform chemical constitution have been obtained from several strains of group A streptococci. The isolated cell walls are dissolved by the same fractions of the Streptomyces albus enzymes that are effective in the lysis of intact cells, and it is likely that enzymatic lysis of group A streptococci is effected by an attack on the cell wall. The streptococcal cell wall, as prepared in this study, consists of approximately two-thirds carbohydrate and one-third protein. Small amounts of other components may be present. The carbohydrate component, which is composed primarily of N-acetyl-glucosamine and rhamnose, is the group-specific C carbohydrate. The evidence indicates that one of the streptomyces enzymes is directed toward the carbohydrate component of the cell wall.

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A PROTEOLYTIC ENZYME PRODUCED BY GROUP A STREPTOCOCCI WITH SPECIAL REFERENCE TO ITS EFFECT ON THE TYPE-SPECIFIC M ANTIGEN

Journal of Experimental Medicine ◽

10.1084/jem.81.6.573 ◽

1945 ◽

Vol 81 (6) ◽

pp. 573-592 ◽

Cited By ~ 121

Author(s):

Stuart D. Elliott

Keyword(s):

Proteolytic Enzyme ◽

Potassium Cyanide ◽

Maximal Activity ◽

Serial Passage ◽

Iodoacetic Acid ◽

Broth Culture ◽

Mouse Serum ◽

Group A Streptococci ◽

Extracellular Proteolytic Enzyme ◽

Group A

1. Group A streptococci sometimes produce in broth culture an extracellular proteolytic enzyme. 2. Under suitable cultural conditions the enzyme has been demonstrated in representative cultures of most of the Griffith types. Its production by a given strain may be suppressed by serial passage through mice and the variant so produced has been found to maintain this change in character on subculture in artificial media. 3. Under certain conditions, the enzyme attacks the type-specific M antigens of all the group A streptococci so far tested, with the exception of that of type 28. The enzyme exhibits its maximal activity at 37°C.: Extracts made from enzyme-producing cultures which have been grown at this temperature lack the M antigen; enzyme-producing strains may sometimes be induced to yield M substance in extracts by culturing the streptococci at 22° C. Cultures which, when grown at 37° C. yield M substance in extracts, do not produce the enzyme. 4. Human and rabbit fibrin are attacked and streptococcal fibrinolysin is also inactivated by the enzyme. Other susceptible substrates include casein, milk, gelatin, and benzoyl-l-arginineamide but not l-leucylglycylglycine. 5. The general properties of the enzyme resemble those of papain and some of the cathepsins: It is active under the reducing conditions produced in broth cultures by the presence of living bacteria; it is also activated by substances which reduce disulfide to sulfhydryl groups, e.g. potassium cyanide, cysteine, glutathione, and thioglycollic acid, but it is not activated by ascorbic acid. The enzyme is inactivated by iodoacetic acid and also by normal rabbit or mouse serum.

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THE LYSIS OF CELL WALLS OF GROUP A STREPTOCOCCI BY STREPTOMYCES ALBUS ENZYME TREATED WITH DIISOPROPYL FLUOROPHOSPHATE

Journal of Experimental Medicine ◽

10.1084/jem.121.5.771 ◽

1965 ◽

Vol 121 (5) ◽

pp. 771-792 ◽

Cited By ~ 6

Author(s):

Willard C. Schmidt

Keyword(s):

Cell Walls ◽

Protein A ◽

Cell Wall Polysaccharide ◽

Group A Streptococci ◽

Streptococcal Cell Wall ◽

Diisopropyl Fluorophosphate ◽

Streptomyces Albus ◽

Close Relationship ◽

Group A ◽

A Cell

Diisopropyl fluorophosphate (DFP) effectively inhibited proteolytic activity in preparations of partially purified Streptomyces albus enzyme used to lyse cell walls of Group A streptococci. Lysis of non-trypsinized Group A cell walls with DFP-treated S. albus enzyme released a soluble protein fraction containing antigenic type-specific M protein, a carbohydrate fraction consisting of Group A and a small amount of A-variant polysaccharides, and a dialyzable fraction. The similarities of the products of DFP-treated S. albus enzyme lysis of streptococcal cell walls to those released by phage muralytic enzyme furnish additional evidence of the close relationship of these wall lysins. In view of small differences in electrophoretic mobility, immunodiffusion, and chemical composition, it is suggested that Group A streptococcal cell wall polysaccharide dissolved by DFP-S. albus enzyme consists of a spectrum of molecules having the same immunological determinants but differing in content of conjugated mucopeptide.

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