scholarly journals ELECTRON MICROSCOPIC STUDIES ON STREPTOCOCCI

1973 ◽  
Vol 138 (1) ◽  
pp. 245-258 ◽  
Author(s):  
John Swanson ◽  
Emil C. Gotschlich
Keyword(s):  
Cell Wall ◽  
Horseradish Peroxidase ◽  
Electron Microscopic ◽  
Streptococcal Cell Wall ◽  
Outermost Surface ◽  
Laminar Distribution ◽  
Specific Polysaccharide ◽  
Microscopic Studies ◽  
Group A ◽  
Protein Cell

The location of Group A carbohydrate in the streptococcal cell wall has been studied by several ultrastructural techniques. The findings, based largely on use of ferritin- and horseradish peroxidase-conjugated antibodies, are interpreted as demonstrating a discrete laminar distribution of the group-specific polysaccharide. This carbohydrate layer is located on the outermost surface of the cell wall in organisms lacking protein cell wall antigens.

scholarly journals ELECTRON MICROSCOPIC STUDIES ON STREPTOCOCCI

1969 ◽  
Vol 130 (5) ◽  
pp. 1063-1091 ◽  
Author(s):  
John Swanson ◽  
Konrad C. Hsu ◽  
Emil C. Gotschlich
Keyword(s):  
Cell Wall ◽  
Nitrous Acid ◽  
Intact Cell ◽  
M Protein ◽  
Acid Extraction ◽  
Electron Microscopic ◽  
Streptococcal Cell Wall ◽  
Before And After ◽  
Specific Polysaccharide ◽  
Microscopic Studies

The presence of M antigens on group A streptococci is associated with hairlike fimbriae that cover the surface of the streptococcal cell wall and are demonstrable by electron microscopy. These fimbriae also may be associated with R antigen. Like M protein, the surface fimbriae are destroyed by trypsin treatment and reappear when "trypsinized" streptococci are reincubated in fresh, trypsin-free broth. Ferritin-conjugated, type-specific antibodies localize on homologous M+ cells in a pattern suggestive of several M antigenic sites along the length of individual surface fimbria. The M-associated fimbriae remain on the residual cell wall after removal of the bulk of group-specific polysaccharide through nitrous acid extraction. This suggests attachment of the fimbriae to the mucopeptide and minor polysaccharide components remaining in the nitrous acid-extracted wall. The pattern of localization of ferritin-conjugated antibodies on homologous streptococci before and after trypsin exposure and upon reincubation of the trypsinized cells in fresh medium suggests the following hypothesis: M antigen is secreted by the cell, is partially excreted through the otherwise intact cell wall, and is bound by the wall so that M protein occupies a peripheral, exposed position on the surfaces of the streptococcal cell wall.

Electron Microscopic Studies on Streptococci

1970 ◽  
Vol 28 ◽  
pp. 194-195
Author(s):  
JOHN SWANSON M.D.
Keyword(s):  
Cell Walls ◽  
Teichoic Acid ◽  
Chemical Components ◽  
Group A Streptococci ◽  
Electron Microscopic ◽  
Histochemical Methods ◽  
Specific Polysaccharide ◽  
Microscopic Studies ◽  
Group A ◽  
Comparative Examination

Group A streptococci contain a variety of chemical components in their cell walls. The major components are mucopeptide, group-specific polysaccharide, protein constituents (M,T, and R), and teichoic acid. Investigations have been carried out to determine the location of each of these classes of chemical components. The techniques used include simple, comparative examination of selected strains that lack or possess a particular component, electron histochemical methods, immunoferritin methods, and extraction or removal of a particular component.

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.

Electron microscopic studies on the formation of vesicular bodies during cell wall degradation and regeneration in yeast

1977 ◽  
Vol 17 (4) ◽  
pp. 293-297
Author(s):  
V. V. Dmitriev ◽  
A. B. Tsiomenko ◽  
E. N. Ratner ◽  
V. K. Akimenko ◽  
B. A. Fikhte
Keyword(s):  
Cell Wall ◽  
Cell Wall Degradation ◽  
Electron Microscopic ◽  
Microscopic Studies

scholarly journals Streptococcal cell walls and synovial cell activation. Stimulation of synovial fibroblast plasminogen activator activity by monocytes treated with group A streptococcal cell wall sonicates and muramyl dipeptide.

1982 ◽  
Vol 155 (6) ◽  
pp. 1702-1718 ◽  
Author(s):  
J A Hamilton ◽  
J B Zabriskie ◽  
L B Lachman ◽  
Y S Chen
Keyword(s):  
Cell Wall ◽  
Plasminogen Activator ◽  
Synovial Fibroblast ◽  
Cell Activation ◽  
Interleukin 2 ◽  
Muramyl Dipeptide ◽  
Cellular Interactions ◽  
Human Monocytes ◽  
Streptococcal Cell Wall ◽  
Group A

Group A streptococcal peptidoglycan has previously been shown to be arthritogenic in rats and has been implicated as a structure present in a class of possible etiologic agents for rheumatoid arthritis. The present study reports that conditioned medium from human monocytes, after interaction with cell wall sonicates of four group A streptococcal strains, stimulates the plasminogen activator (PA) activity of nonrheumatoid synovial fibroblasts. Low concentrations of N-acetylmuramyl-L-alanyl-D isoglutamine (muramyl dipeptide) can also generate this synovial activator (SA) activity from human monocytes. Preliminary biochemical data suggest that the SA activity is distinct from interferon-gamma, interleukin 1, and interleukin 2. These results indicate that agents that are arthritogenic in rats can modulate human synovial fibroblast functions via monocytes. The findings are proposed to have possible significance for an understanding of the cellular interactions involved in the formation and function of the rheumatoid pannus, because PA has been invoked as possibly being generally important for the processes of cell migration, tissue remodeling, and inflammation.

scholarly journals Streptococcal cell wall arthritis. Passive transfer of disease with a T cell line and crossreactivity of streptococcal cell wall antigens with Mycobacterium tuberculosis.

1989 ◽  
Vol 170 (2) ◽  
pp. 369-382 ◽  
Author(s):  
S Q DeJoy ◽  
K M Ferguson ◽  
T M Sapp ◽  
J B Zabriskie ◽  
A L Oronsky ◽  
...  
Keyword(s):  
Cell Wall ◽  
T Cell ◽  
Cell Lines ◽  
Cell Walls ◽  
Chronic Phase ◽  
Streptococcal Cell Wall ◽  
Group A ◽  
Primary Lymph Node ◽  
T Cell Lines ◽  
Streptococcal Cell Wall Arthritis

Primary lymph node cells derived from streptococcal cell wall arthritic rats or those derived from adjuvant arthritic rats proliferated in response to cell wall antigens derived from either streptococcal cell walls or those from M. tuberculosis. In addition, two T cell lines have been isolated from lymph nodes of rats during the chronic phase of streptococcal cell wall arthritis. These T cell lines transfered clinical disease to naive syngeneic irradiated recipients, and they proliferated in the presence of cell wall antigens derived from streptococci or antigens derived from Mycobacterium but failed to proliferate in the presence of the 65-kD antigen (containing the sequence TFGLQLELT) derived from Mycobacterium. These observations indicate that T cells play a crucial role in the pathogenesis of streptococcal cell wall arthritis and suggest that antigenic crossreactivity exists between cell walls of group A streptococci and antigens derived from Mycobacterium. The 65-kD Mycobacterium protein is not involved in the observed antigenic crossreactivity.

Electron microscopic studies on the formation of vesicular bodies during cell wall degradation and regeneration in yeast

1977 ◽  
Vol 17 (4) ◽  
pp. 293-297 ◽  
Author(s):  
V. V. Dmitriev ◽  
A. B. Tsiomenko ◽  
E. N. Ratner ◽  
V. K. Akimenko ◽  
B. A. Fikhte
Keyword(s):  
Cell Wall ◽  
Cell Wall Degradation ◽  
Electron Microscopic ◽  
Microscopic Studies

scholarly journals Streptococcal M protein extracted by nonionic detergent. I. Properties of the antiphagocytic and type-specific molecules.

1976 ◽  
Vol 144 (1) ◽  
pp. 32-53 ◽  
Author(s):  
V A Fischetti ◽  
E C Gotschlich ◽  
G Siviglia ◽  
J B Zabriskie
Keyword(s):  
Cell Wall ◽  
M Protein ◽  
Multiple Form ◽  
Streptococcal Cell Wall ◽  
Streptococcal M Protein ◽  
Physical Chemical ◽  
Immunological Tests ◽  
Multiple Protein ◽  
Nonionic Detergent ◽  
Group A

Group A streptococcal M protein was extracted with nonionic detergent and subjected to a number of physical, chemical, and immunological tests. M protein thus extracted was composed of multiple protein bands, ranging from 35,000 down to 6,000 daltons, all having type-specific precipitating activity. The anti-phagocytic proteins, however, were limited to three molecular species having mol wt of 28,000, 31,000, and 35,000 daltons, and could be separated from those proteins that had only type specificity. Physical studies indicated that these proteins existed as individual asymmetrical molecules which were not aggregated. By radiolabeling M protein on living streptococci, it was determined that these protein bands were found on the streptococcal cell wall in this multiple form. Also, by pulse chase experiments supported by chemical and immunological data, evidence was obtained strongly suggesting that the smaller, type-specific molecules are used to assemble the larger, antiphagocytic proteins.

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 Conjugated avidin binds to mast cell granules.

1985 ◽  
Vol 33 (1) ◽  
pp. 27-32 ◽  
Author(s):  
M D Tharp ◽  
L L Seelig ◽  
R E Tigelaar ◽  
P R Bergstresser
Keyword(s):  
Mast Cell ◽  
Mast Cells ◽  
Horseradish Peroxidase ◽  
Staining Technique ◽  
Cellular Structures ◽  
Clinical Tool ◽  
Electron Microscopic ◽  
Simple Method ◽  
Human Mast Cells ◽  
Microscopic Studies

The glycoprotein, avidin, conjugated either to the enzyme horseradish peroxidase, or to the fluorochrome dyes, fluorescein or rhodamine, identifies the granules of mast cells in both tissues and cell suspensions. In the absence of prior fixation, mast cells were not identified with conjugated avidin; however, granules released from these cells were stained with this labeled glycoprotein. The specificity of avidin for mast cells was confirmed by the absence of conjugated avidin-positive cells in the skin of mice (S1/S1d) deficient in mature dermal mast cells. Electron microscopic studies confirmed that avidin binds specifically to individual mast cell granules rather than to other cellular structures. Rodent and human mast cells were readily stained with avidin conjugated to horseradish peroxidase or to either of the fluorochrome dyes. The conjugated avidin staining technique is a reliable and simple method for identifying rodent and human mast cells, one that is useful as both an investigative and a clinical tool.

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