Effect of Body Fluids and Macromolecular Substances on the Lysis of Group A Streptococci by Muramidases of Streptomyces albus

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

Journal of Experimental Medicine ◽

10.1084/jem.96.6.555 ◽

1952 ◽

Vol 96 (6) ◽

pp. 555-568 ◽

Cited By ~ 43

Author(s):

Maclyn McCarty

Keyword(s):

Liquid Medium ◽

Proteolytic Enzyme ◽

Extracellular Enzymes ◽

Surface Growth ◽

Group A Streptococci ◽

Lytic Enzymes ◽

Acid Hydrolysate ◽

Streptomyces Albus ◽

Group A

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 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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