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

1945 ◽  
Vol 81 (6) ◽  
pp. 573-592 ◽  
Author(s):  
Stuart D. Elliott

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.

1952 ◽  
Vol 96 (6) ◽  
pp. 555-568 ◽  
Author(s):  
Maclyn McCarty

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.


1993 ◽  
Vol 9 (6) ◽  
pp. 1213-1222 ◽  
Author(s):  
Tambryn VanHeyningen ◽  
George Fogg ◽  
Debra Yates ◽  
Emanuel Hanski ◽  
Michael Caparon

2019 ◽  
Vol 167 (3) ◽  
pp. 367-370 ◽  
Author(s):  
Т. А. Danilova ◽  
G. А. Danilina ◽  
А. А Аdzhieva ◽  
A. G. Minko

1981 ◽  
Vol 25 (4) ◽  
pp. 403-405
Author(s):  
Norio Okazaki ◽  
Riichiro Akema ◽  
Yasushi Miyamoto
Keyword(s):  

Microbiology ◽  
2007 ◽  
Vol 153 (11) ◽  
pp. 3800-3808 ◽  
Author(s):  
Helena M. Linge ◽  
Inka Sastalla ◽  
D. Patric Nitsche-Schmitz ◽  
Arne Egesten ◽  
Inga-Maria Frick

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