Analyze Diet
The Journal of experimental medicine1947; 85(6); 591-606; doi: 10.1084/jem.85.6.591

A Study of the Inhibition of Streptococcal Proteinase by Sera of Normal and Immune Animals and of Patients Infected with Group A Hemolytic Streptococci.

Abstract: Antiproteinase sera were prepared by immunizing horses with filtrates from a selected strain of group A streptococcus. This strain, which produced high titred proteinase but no erythrogenic toxin, was selected from forty-two strains of group A streptococci which produced varying amounts of proteinase. A few strains belonging to groups B, C, and G were also tested; they were all proteinase-negative. Methods are described for titrating streptococcal proteinase in crude culture filtrates and for measuring the antiproteinase activity of serum. The antiproteinase titres of sera from immunized horses ranged from 125 units to 1,000 units per cc. in contrast to the low titres of normal horse sera, only 5 per cent of which had titres as high as 10 to 30 units per cc. The available evidence suggests that the antiproteinase activity of immune sera is dependent on the action of specific antibody for streptococcal proteinase. Patients infected with group A streptococci do not develop high anti-proteinase titres. There appears to be no correlation between the occurrence of rheumatic fever and the antiproteinase titre of the patient's serum.
Publication Date: 1947-05-31 PubMed ID: 19871638PubMed Central: PMC2135681DOI: 10.1084/jem.85.6.591Google Scholar: Lookup
The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
  • Journal Article

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research involves investigation of the inhibition of the streptococcal proteinase enzyme by the sera of healthy and immune animals, as well as patients infected with group A hemolytic streptococci bacteria. It was discovered that the sera’s antiproteinase activity is linked to the action of specific antibodies against the streptococcal proteinase. Also, no correlation between occurrence of rheumatic fever and the antiproteinase titre of the patient’s serum was found.

Research Methodology and Results

  • The study conducted involved preparing antiproteinase sera by immunizing horses with filtrates derived from a specific strain of group A streptococcus. This strain was chosen from 42 different strains for its distinctive characteristic of producing a high amount of proteinase but no erythrogenic toxin.
  • In addition to this, a handful of strains from groups B, C, and G were tested. However, these groups were found to be devoid of any proteinase activity.
  • A methodology was set and described for titrating streptococcal proteinase in crude culture filtrates and for estimating the antiproteinase activity of serum.
  • The investigation found that the antiproteinase titers of the immunized horse sera ranged from 125 units to 1,000 units per cubic centimeter. Regular horse sera, on the other hand, displayed comparatively low titers, with just 5% having titers as high as 10 to 30 units per cubic centimeter.
  • The evidence that was collected suggests that antiproteinase activity in immune sera depends on the reaction of a specific antibody against streptococcal proteinase.

Relation to Rheumatic Fever

  • Additionally, the study investigated the relationship between antiproteinase titers and the incidence of rheumatic fever in patients infected with Group A streptococci.
  • It was observed that patients with this infection did not show high antiproteinase titers.
  • Moreover, no correlation was found between the existence of rheumatic fever and the antiproteinase titre aspect ratio of the patient’s serum.

In conclusion, this research demonstrates the inhibitory action of antiproteinase sera on streptococcal proteinase, with potential implications for understanding the body’s immune response to Group A streptococcal infections.

Cite This Article

APA
Todd EW. (1947). A Study of the Inhibition of Streptococcal Proteinase by Sera of Normal and Immune Animals and of Patients Infected with Group A Hemolytic Streptococci. J Exp Med, 85(6), 591-606. https://doi.org/10.1084/jem.85.6.591

Publication

ISSN: 0022-1007
NlmUniqueID: 2985109R
Country: United States
Language: English
Volume: 85
Issue: 6
Pages: 591-606

Researcher Affiliations

Todd, E W
  • Belmont Laboratories (London County Council), Sutton, Surrey, The Serum Institute, (Wellcome Foundation), Carshalton, Surrey, England, and the Hospital of The Rockefeller Institute for Medical Research, New York.

MeSH Terms

  • Aged
  • Animals
  • Antibodies
  • Bacterial Proteins
  • Cysteine Endopeptidases
  • Endopeptidases
  • Exotoxins
  • Horses
  • Humans
  • Immune Sera
  • Streptococcal Infections
  • Streptococcus
  • Streptococcus pyogenes

References

This article includes 5 references
  1. Elliott SD. A PROTEOLYTIC ENZYME PRODUCED BY GROUP A STREPTOCOCCI WITH SPECIAL REFERENCE TO ITS EFFECT ON THE TYPE-SPECIFIC M ANTIGEN.. J Exp Med 1945 Jun 1;81(6):573-92.
    pubmed: 19871477doi: 10.1084/jem.81.6.573google scholar: lookup
  2. Seegal BC, Seegal D. A Lytic Action of Certain Strains of Hemolytic Streptococci on Fresh Sterile Kidney and Other Tissues.. J Bacteriol 1936 Dec;32(6):621-9.
    pubmed: 16559978doi: 10.1128/jb.32.6.621-629.1936google scholar: lookup
  3. Macfarlane MG, Knight BC. The biochemistry of bacterial toxins: The lecithinase activity of Cl. welchii toxins.. Biochem J 1941 Sep;35(8-9):884-902.
    pubmed: 16747456doi: 10.1042/bj0350884google scholar: lookup
  4. Holman WL. The Value of a Cooked Meat Medium for Routine and Special Bacteriology.. J Bacteriol 1919 Mar;4(2):149-55.
    pubmed: 16558829doi: 10.1128/jb.4.2.149-155.1919google scholar: lookup
  5. Frobisher M. TISSUE-DIGESTING ENZYME (HISTASE) OF STREPTOCOCCI.. J Exp Med 1926 Nov 30;44(6):777-86.
    pubmed: 19869222doi: 10.1084/jem.44.6.777google scholar: lookup

Citations

This article has been cited 5 times.
  1. ROTHBARD S, TODD EW. Production of proteinase by hemolytic streptococci in various clinical conditions. J Exp Med 1948 Apr 1;87(4):283-94.
    doi: 10.1084/jem.87.4.283pubmed: 18904214google scholar: lookup
  2. KELLNER A, ROBERTSON T. Myocardial necrosis produced in animals by means of crystalline streptococcal proteinase. J Exp Med 1954 May 1;99(5):495-503.
    doi: 10.1084/jem.99.5.495pubmed: 13163324google scholar: lookup
  3. Lukomski S, Montgomery CA, Rurangirwa J, Geske RS, Barrish JP, Adams GJ, Musser JM. Extracellular cysteine protease produced by Streptococcus pyogenes participates in the pathogenesis of invasive skin infection and dissemination in mice. Infect Immun 1999 Apr;67(4):1779-88.
  4. Lukomski S, Burns EH Jr, Wyde PR, Podbielski A, Rurangirwa J, Moore-Poveda DK, Musser JM. Genetic inactivation of an extracellular cysteine protease (SpeB) expressed by Streptococcus pyogenes decreases resistance to phagocytosis and dissemination to organs. Infect Immun 1998 Feb;66(2):771-6.
    doi: 10.1128/IAI.66.2.771-776.1998pubmed: 9453640google scholar: lookup
  5. Gubba S, Low DE, Musser JM. Expression and characterization of group A Streptococcus extracellular cysteine protease recombinant mutant proteins and documentation of seroconversion during human invasive disease episodes. Infect Immun 1998 Feb;66(2):765-70.
    doi: 10.1128/IAI.66.2.765-770.1998pubmed: 9453639google scholar: lookup