Lysis of Grouped and Ungrouped Streptococci by Lysozyme

Coleman, Sylvia E.; Rijn, I van de; Bleiweis, Arnold S.

doi:10.1128/iai.2.5.563-569.1970

Cited by 49 publications

(25 citation statements)

References 14 publications

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“…An additional control experiment was performed to determine if hen egg lysozyme injected in vivo could effect PG-APS-induced arthritis. Hen egg lysozyme is a basic protein with muramidase activity, but it is unable to degrade group A streptococcal cell wall in vitro (22)(23)(24). Rats were injected intraperitoneally with an arthropathic dose of PG-APS and randomly divided into two groups.…”

Section: Treatment Of Arthritis In Rats With Mutanolysinmentioning

confidence: 99%

Treatment of experimental erosive arthritis in rats by injection of the muralytic enzyme mutanolysin.

Janusz¹,

Chetty²,

Eisenberg³

et al. 1984

The Journal of Experimental Medicine

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A single intravenous injection into rats of 0.4 mg of the muralytic enzyme mutanolysin, given as long as 3 d after an arthropathic dose of peptidoglycan-polysaccharide polymers derived from group A streptococci (PG-APS), resulted in a complete resolution of acute arthritis and the prevention of chronic joint disease. When administration of mutanolysin was delayed until 14 d after the injection of PG-APS, a great reduction in the severity of chronic inflammation was still observed. Quantitation of the amount of PG-APS present in the limbs, spleen, and liver by a solid phase enzyme-linked immunoassay indicated that the tissues of mutanolysin-treated rats contained as much PG-APS as tissues of PBS-treated control rats. In addition, rats treated with mutanolysin immediately after receiving an intraperitoneal injection of PG-APS developed a transient limb edema similar to that seen in rats after the injection of PG-APS digested to a small fragment size in vitro with mutanolysin. We hypothesize that mutanolysin acts in vivo by degrading PG-APS to small fragments that persist but are no longer arthropathic.

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Section: Treatment Of Arthritis In Rats With Mutanolysinmentioning

confidence: 99%

Treatment of experimental erosive arthritis in rats by injection of the muralytic enzyme mutanolysin.

Janusz¹,

Chetty²,

Eisenberg³

et al. 1984

The Journal of Experimental Medicine

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“…Based on these observations, it has been suggested that the quantity and digestibility of endocytosed material may control acid hydrolase production (29). PPG stimulated acid hydrolase production greatly, but it is not digestible by macrophages (9,11,34). Group A streptococcal cell walls can be digested partially by N-acetyl-/3-D-glucosaminidase, an enzyme found in certain soil bacteria (10).…”

Section: A Component Of Group a Streptococcal Cell Walls Induces Chromentioning

confidence: 99%

Changes in Cellular Enzyme Levels and Extracellular Release of Lysosomal Acid Hydrolases in Macrophages Exposed to Group a Streptococcal Cell Wall Substance

Davies

Page

Allison

1974

The Journal of Experimental Medicine

139

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Infection by group A streptococci may lead to chronic inflammatory lesions of the myocardium, heart valves, joints, and skin. The pathogenesis of these lesions remains uncertain (1), and several experimental animal models have been used to study chronic inflammation induced by group A streptococci and their extracellular products (2). Cell wall preparations containing only type-specific polysaccharide and peptidoglycan (PPG) 1 have the capacity to induce chronic-recurring granulomatous lesions in the skin of rabbits (3), lesions resembling those of rheumatic fever in the hearts of mice (4) and rabbits (5), and severe polyarthritis in rats (6). Available evidence indicates that PPG induces inflammatory lesions by direct interaction with infiltrating leukocytes, rather than by an immunopathologic mechanism (7). In experimental lesions, PPG becomes associated with macrophages (3), and it appears that these cells lack .the ability to digest the material (5, 8-11). These observations have led us to investigate the effects of PPG on mouse peritoneal macrophages maintained in culture. We have found that PPG, at concentrations which do not appear to be cytotoxic, induces marked morphologic and biochemical changes in these cells. They undergo a three-to fourfold increase in size, and there is a significant elevation in the levels of acid hydrolases and other cellular enzymes. Furthermore, there is a selective release of the hydrolases into the extracellular environment with no detectable loss of cell viability. Materials and MethodsMaterials.--Bovine pancreatic ribonuclease (type I-A), twice crystallized pancreatic trypsin (type III), phenolphthalein glucuronic acid 0.01 M, pH 7.0; o-nitrophenyl-/3-1)-galactopyranoside, leucine-2-naphthylamide, ¢z-naphthyl acid phosphate and glycogen type II (from

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“…Its pH optimum of 3.4 is lower than that of lysozynir and its pattern of heat lability as a function of pH is opposite to that of lysozyme ( 1 1 ) . While the enzyme, like lysozyrne, liberates reducing groups and is thcrefore a glycosidase, its ability to partly degrade streptococcal cell walls prepared by glass-head breakage and enzyme digestion contrasts sharply lvith the inability of lysozyme to do so (6,8).…”

Section: Discussionmentioning

confidence: 99%

“…I n this paper ive report partial purification of this enzyme and some of its properties. I n particular, we have studied the effect of this enzyme on streptococcal cell walls, and have found that it could partially degrade certain cell-tzall preparations that resist attack hy hen egg white lysozynie (6,8 ) . Unlike lysozyme, hacteriolytic action of the enzyme includes release of the group-specific carbohydrate rendering it potentially useful for studies on streptococcal cell wall structure.…”

Section: Index Abstractmentioning

confidence: 99%

Partial Purification and Characterization of a Bacteriolytic Enzyme Secreted by *Tetrahymena**

Vick

Gallis

Wheat

et al. 1979

The Journal of Protozoology

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Tetrahymena pyriformis strain HSM secretes large quantities of acid hydrolases into the culture medium. An enzyme secreted by the ciliate and capable of degrading walls of streptococci was identified and purified to a considerable degree. The pH optimum of this enzyme was 3--4, and it was eluted after cytochrome c from Sephadex G-75 columns. Unlike lysozyme, the enzyme was thermolabile at pH 2.9, but relatively thermostable at pH 8.1. It degraded 14C-labeled cell walls of streptococci releasing reducing groups. Cell walls prepared from different strains of streptococci differed in susceptibility to this enzyme, the most sensitive strain tested being of group A, type T12. It was shown in immunologic studies that this hydrolase released the group-specific carbohydrate from the walls. Secretions of Tetrahymena from early stationary-phase cultures had more bacteriolytic activity than those from cells from late stationary-phase cultures. Further, cells from cultures grown in glucose-supplemented medium secreted less of the enzyme than ciliates of comparable age grown in unsupplemented proteose-peptone. The newly isolated bacteriolytic enzyme, presumably of lysosomal origin, may be helpful in characterizing streptococcal cell walls.

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Lysis of Grouped and Ungrouped Streptococci by Lysozyme

Cited by 49 publications

References 14 publications

Treatment of experimental erosive arthritis in rats by injection of the muralytic enzyme mutanolysin.

Treatment of experimental erosive arthritis in rats by injection of the muralytic enzyme mutanolysin.

Changes in Cellular Enzyme Levels and Extracellular Release of Lysosomal Acid Hydrolases in Macrophages Exposed to Group a Streptococcal Cell Wall Substance

Partial Purification and Characterization of a Bacteriolytic Enzyme Secreted by *Tetrahymena**

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Lysis of Grouped and Ungrouped Streptococci by Lysozyme

Cited by 49 publications

References 14 publications

Treatment of experimental erosive arthritis in rats by injection of the muralytic enzyme mutanolysin.

Treatment of experimental erosive arthritis in rats by injection of the muralytic enzyme mutanolysin.

Changes in Cellular Enzyme Levels and Extracellular Release of Lysosomal Acid Hydrolases in Macrophages Exposed to Group a Streptococcal Cell Wall Substance

Partial Purification and Characterization of a Bacteriolytic Enzyme Secreted by Tetrahymena*

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Partial Purification and Characterization of a Bacteriolytic Enzyme Secreted by *Tetrahymena**