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

1952 ◽  
Vol 96 (6) ◽  
pp. 569-580 ◽  
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.

scholarly journals STUDIES ON STREPTOCOCCAL BACTERIOPHAGES

1968 ◽  
Vol 127 (3) ◽  
pp. 489-505 ◽  
Author(s):  
Vincent A. Fischetti ◽  
John B. Zabriskie
Keyword(s):  
Cell Wall ◽  
Living Cell ◽  
Cell Walls ◽  
Group A Streptococci ◽  
Viral Inactivation ◽  
Streptococcal Cell Wall ◽  
Group A ◽  
Isolated Cell ◽  
Virulent Group ◽  
Living Group

Evidence has been presented that Group C bacteriophages differ as to their inactivating site on the streptococcal cell wall. While all three phages adsorb to isolated cell walls, only the C1 phage was inactivated by enzymatically prepared group-specific carbohydrate. None of the Group C phages were inactivated by chemically extracted group-specific carbohydrate. In contrast, all virulent Group A streptococcal bacteriophages adsorbed only to living Group A streptococci. However, Group A temperate phages were able to adsorb to isolated cell walls but not to group-specific carbohydrate. While it has not been possible to identify the specific inactivating substance for the Group A virulent phages, certain pieces of evidence indirectly implicate the group-specific carbohydrate, specifically the N-acetylglucosamine moiety. The fact that Group A virulent phages failed to adsorb to heat-killed Group A streptococcal cells suggests that additional factors produced by the living cell are needed for complete viral inactivation.

scholarly journals STUDIES OF L FORMS AND PROTOPLASTS OF GROUP A STREPTOCOCCI

1959 ◽  
Vol 110 (6) ◽  
pp. 853-874 ◽  
Author(s):  
Earl H. Freimer ◽  
Richard M. Krause ◽  
Maclyn McCarty
Keyword(s):  
Cell Wall ◽  
Cell Walls ◽  
M Protein ◽  
Group A Streptococci ◽  
Group A ◽  
Isolated Cell ◽  
Streptococcal Strain

L forms of Group A streptococci have been isolated by the use of penicillin gradient agar plates. Osmotically fragile protoplasts of Group A streptococci have been obtained by the use of Group C phage-associated lysin which lyses Group A streptococci and their isolated cell walls. Membranes surrounding these enzymatically derived protoplasts have been isolated, and chemical and immunological studies indicate that they are free of cell wall carbohydrate and M protein. The streptococcal protoplasts reproduce as colonies which are morphologically indistinguishable from streptococcal L forms. Evidence is presented to show that these two streptococcal derivatives are serologically and physiologically related to each other as well as to the parent streptococcal strain from which they were isolated.

scholarly journals ENHANCED RESISTANCE TO STREPTOCOCCAL INFECTION INDUCED IN MICE BY CELL WALL MUCOPEPTIDE

1965 ◽  
Vol 122 (5) ◽  
pp. 877-890 ◽  
Author(s):  
Jiri Rotta ◽  
Thomas J. Prendergast ◽  
Walter W. Karakawa ◽  
Charles K. Harmon ◽  
Richard M. Krause
Keyword(s):  
Cell Wall ◽  
Cell Walls ◽  
Streptococcal Infection ◽  
Group A Streptococci ◽  
Streptococcal Cell Wall ◽  
Enhanced Resistance ◽  
Group A ◽  
Late Recovery ◽  
Fever Response ◽  
Virulent Group

The streptococcal cell wall mucopeptide when injected into mice either intraperitoneally or intravenously enhances the resitance to subsequent challenge with virulent Group A streptococci. Rabbits which are injected intravenously with solubilized mucopeptide develop a fever response which has a resemblance to that achieved with endotoxin. Mice which survive 6 to 7 weeks after challenge with virulent Group A streptococci yield at autopsy search Group A streptococci serologically identical to the challenge organisms. A preparative dose of cell walls injected into mice prior to challenge diminished this late recovery of streptococci. Group A-variant streptococci were recovered from mice which survived challenge and carried the organisms for several weeks. Filterable bacterial forms, which grew on L form media, were recovered from infected mice. The serologic type of the L forms was identical to that of the challenge organisms.

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

1952 ◽  
Vol 96 (6) ◽  
pp. 555-568 ◽  
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.

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

1965 ◽  
Vol 121 (5) ◽  
pp. 771-792 ◽  
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.

scholarly journals RELATION OF RHEUMATIC-LIKE CARDIAC LESIONS OF THE MOUSE TO LOCALIZATION OF GROUP A STREPTOCOCCAL CELL WALLS

1969 ◽  
Vol 129 (1) ◽  
pp. 37-49 ◽  
Author(s):  
S. H. Ohanian ◽  
J. H. Schwab ◽  
W. J. Cromartie
Keyword(s):  
Cell Wall ◽  
Cell Walls ◽  
Wall Material ◽  
Cell Wall Material ◽  
Mediastinal Lymph Nodes ◽  
Loose Connective Tissue ◽  
Streptococcal Cell Wall ◽  
Cardiac Lesions ◽  
Group A ◽  
Isolated Cell

Mice injected intraperitoneally with isolated cell wall fragments of Group A streptococci develop a carditis similar to that previously observed in mice injected with crude extracts of this organism. Neither the soluble cytoplasmic components of Group A streptococcal cells nor the nonfragmented cell walls produced carditis in this experimental model. Fluorescein and 125I-labeled antibodies specific for Group A streptococcal cell wall antigens were used to demonstrate that, for 5 wk after injection, cell wall material is localized around the sites of active lesions in the heart. In addition, the cell wall antigen accumulates in the liver, spleen, mediastinal lymph nodes, and the adjacent loose connective tissue, where it persists for at least 10 wk.

scholarly journals STUDIES ON BACTERIOPHAGES OF HEMOLYTIC STREPTOCOCCI

1957 ◽  
Vol 106 (3) ◽  
pp. 365-384 ◽  
Author(s):  
Richard M. Krause
Keyword(s):  
Cell Wall ◽  
Hyaluronic Acid ◽  
Cell Walls ◽  
Receptor Site ◽  
Surface Proteins ◽  
Phage Antibody ◽  
Group A ◽  
Phage Receptor ◽  
Hyaluronic Acid Capsule ◽  
Isolated Cell

The host ranges of bacteriophages for group A, types 1, 6, 12, and 25 and group C streptococci have been determined. The findings indicate that the susceptibility to these phages is primarily a group-specific phenomenon, although it is modified by several factors such as the hyaluronic acid capsule, lysogeny, and possibly the presence of surface proteins. Phage antibody studies indicate that while the group A phages are antigenically related, they are distinct from the group C phage. This is in agreement with the observation that group A phages are not specific for their homologous streptococcal types. The purified group C carbohydrate inactivates group C phage but not the group A phages, thus suggesting that the carbohydrate, a component of the cell wall, may serve as the phage receptor site. It has not been possible to inactivate the group A phages with group A carbohydrate. Phage lysis of groups A and C streptococci is accompanied by fragmentation of the cell wall since the C carbohydrate has been identified serologically and chemically in the supernate of centrifuged lysates. The immediate lysis of groups A and C hemolytic streptococci and their isolated cell walls by an accesory heat-labile lytic factor in fresh group C lysates is also described.

Electron microscopy of the replicative events of A25 bacteriophages in group A streptococci

1972 ◽  
Vol 18 (1) ◽  
pp. 93-96 ◽  
Author(s):  
S. E. Read ◽  
R. W. Reed
Keyword(s):  
Electron Microscopy ◽  
Cell Wall ◽  
Electron Microscope ◽  
Nucleic Acid ◽  
Group A Streptococcus ◽  
Group A Streptococci ◽  
Virulent Phage ◽  
Acid Pool ◽  
Group A ◽  
A Cell

The replicative events of a virulent phage (A25) infection of a group A Streptococcus (T253) were studied using the electron microscope. The first intracellular evidence of phage replication in a cell occurred 30 min after infection with arrest of cell division and increase in the nucleic acid pool. Phage heads were evident in the nucleic acid pool of the cells 45 min after infection. Release of phages occurred by splitting of the cell wall along discrete lines. This appeared to be at sites of active wall synthesis, i.e., near the region of septum formation. Many phage components were released but relatively few complete phages indicating a relatively inefficient replicative system.

scholarly journals Ionic Relations of Cells of Ohara Australis I. Ion Exchange in the Cell Wall

1959 ◽  
Vol 12 (4) ◽  
pp. 395 ◽  
Author(s):  
J Dainty ◽  
AB Hope
Keyword(s):  
Cell Wall ◽  
Ion Exchange ◽  
Free Space ◽  
Cell Walls ◽  
Plant Cells ◽  
External Solution ◽  
Exchangeable Cations ◽  
Intact Cells ◽  
Donnan Free Space ◽  
Isolated Cell

Measurements of ion exchange were made between isolated cell walls of Ohara australis and an external solution. Comparison between intact cells and cell walls showed that nearly all the easily exchangeable cations are located in the cell wall. The wall is hown to consist of "water free space" (W.F.S.) and "Donnan free space" (D.F.S.); the concentration of in diffusible anions in the D.F.S. is about O� 6 equivjl. This finding is contrary to past suggestions that the D.F.S. is in the cytoplasm of plant cells.

scholarly journals Doubly Branched Hexasaccharide Epitope on the Cell Wall Polysaccharide of Group A Streptococci Recognized by Human and Rabbit Antisera

2005 ◽  
Vol 73 (10) ◽  
pp. 6383-6389 ◽  
Author(s):  
Francis Michon ◽  
Samuel L. Moore ◽  
John Kim ◽  
Milan S. Blake ◽  
France-Isabelle Auzanneau ◽  
...  
Keyword(s):  
Cell Wall ◽  
Rabbit Antiserum ◽  
Cell Wall Polysaccharide ◽  
Group A Streptococci ◽  
Group B Streptococci ◽  
Group A ◽  
Streptococcal Polysaccharide ◽  
Synthetic Oligosaccharides ◽  
Group B ◽  
Dominant Epitope

ABSTRACT A number of epitope specificities associated with the cell wall polysaccharide antigen of group A streptococci were identified in a polyclonal rabbit antiserum induced in rabbits by whole group A streptococci and in polyclonal convalescent human antisera from children that had recovered from streptococcal A infections. The identification was achieved by using a series of synthetic oligosaccharides, glycoconjugates, and bacterial polysaccharide inhibitors to inhibit the binding of the group A helical polysaccharide to the polyclonal antisera. The exclusively dominant epitope expressed in the convalescent human antisera was the doubly branched extended helical hexasaccharide with the structure α-l-Rhap(1→2)[β-d-GlcpNAc(1→3)]α-l-Rhap(1→3)α-l-Rhap(1→2)[β-d-GlcpNAc(1→3)]α-l-Rhap. The hexasaccharide epitope also bound with the highest immunoreactivity to the rabbit antiserum. In contrast, the human antisera did not show significant binding to the singly branched pentasaccharide with the structure α-l-Rhap(1→2)α-l-Rhap(1→3)α-l-Rhap(1→2)[β-d-GlcpNAc(1→3)]α-l-Rhap or the branched trisaccharide α-l-Rhap(1→2)[β-d-GlcpNAc(1→3)]α-l-Rhap, although both these haptens bound significantly to the same rabbit antiserum, albeit with less immunoreactivity than the hexasaccharide. Inhibition studies using streptococcal group A and B rabbit antisera and the inhibitors indicated above also suggested that the group A carbohydrate, unlike the group B streptococcal polysaccharide, does not contain the disaccharide α-l-Rhap(1→2)α-l-Rhap motif at its nonreducing chain terminus, stressing the importance of mapping the determinant specificities of these two important streptococcal subcapsular group polysaccharides to fully understand the serological relationships between group A and group B streptococci.

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