Symposium on the fine structure and replication of bacteria and their parts. 3. Bacterial cell-wall replication followed by immunofluorescence.

Cole, R M

doi:10.1128/mmbr.29.3.326-344.1965

Cited by 45 publications

(34 citation statements)

References 32 publications

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“…The apparent greater staining with FL-Con A at septal regions may be related to differences in teichoic acid content or may simply reflect the presence of a double wall. Cole has noted intense staining at division points for several rod-shaped bacteria by using fluorescein-conjugated antibodies (8).…”

Section: Discussionmentioning

confidence: 99%

Distribution of teichoic acid in the cell wall of Bacillus subtilis

Doyle¹,

McDannel²,

Helman³

et al. 1975

J Bacteriol

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Hydrolysis of the cell wall of Bacillus subtilis 168 by autolysins or lysozyme resulted in the exposure of glucosylated teichoic acid molecules as evidenced by increased precipitation of ["4C] concanavalin A. The number of concanavalin A-reactive sites increased significantly after only limited enzymatic digestion of the walls. Quantitative analyses of ["4C]concanavalin A-treated wall or wall hydrolysate complexes indicate that approximately one-half of the teichoic acid molecules are surface-exposed, whereas the remainder are probably embedded within the peptidoglycan matrix. Treatment of the cell walls with sodium dodecyl sulfate or Triton X-100 did not result in new concanavalin A-reactive sites. Partial autolysis diminished the ability of the cell walls to adsorb bacteriophage 025. Fluorescein-labeled concanavalin A bound intensely over the entire surface of growing B. subtilis 168 cells, suggesting that teichoic acid molecules are located on the total solvent-exposed surface area of the bacteria.The exact location and configuration of teichoic acids in the cell walls of gram-positive bacteria is still unknown. One important question that has remained unanswered is whether all of the cell wall teichoic acid molecules are surface exposed or whether some of the molecules are intercalated within the insoluble peptidoglycan network. Furthermore, with respect to bacilli, it is not known with certainty whether the teichoic acids are found in both hemispherical caps and rods.Several papers have appeared which deal peripherally with these problems. Burger (7) showed that by subjecting the cell walls of Bacillus subtilis 3610 and B. subtilis W-23 to lysozyme greater quantities of anti-teichoic acid antibody could be precipitated, suggesting that teichoic acids were arranged on both the surface and within the peptidoglycan matrix. Nermut (22) extracted the walls of B. megaterium M with hot formamide to remove the teichoic acid and found that the wall thickness decreased by approximately one-half. Nermut interpreted these results in terms of a two-layered cell wall structure, with the outer layer consisting of extractable teichoic acid and the inner layer consisting of nonextractable peptidoglycan. Birdsell et al. (Abstr. Annu. Meet. Am. Soc. Microbiol. 1972, G212, p. 65) found that thin sections of concanavalin A-treated B. subtilis 168 cell walls contained an outer fluffy layer and a smooth inner wall face. The fluffy, discontinu-ous outer layer was absent when the walls were treated with the concanavalin A (Con A) inhibitor methyl-alpha-D-glucopyranoside or when walls containing non-glucosylated teichoic acid were employed. These findings suggested that in B. subtilis 168 at least a portion of the teichoic acid was located on the outer, but not the inner, surface of the cell wall. Recently, Weibull (26) showed that the cell wall of aldehyde-fixed, unstained B. subtilis ATCC 6051 possessed two electron-dense layers separated by an electron-transparent layer. One interpretation of these results is that the teichoic a...

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Section: Discussionmentioning

confidence: 99%

Distribution of teichoic acid in the cell wall of Bacillus subtilis

Doyle¹,

McDannel²,

Helman³

et al. 1975

J Bacteriol

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“…Incubation of the cells in fresh, trypsin-free broth is accompanied by renewed ferritin tagging of the cell wall surfaces (Figs. [20][21][22]. After 10 rain reincubation (Figs.…”

Section: Localization Of Ferritin-conjugated Antibodies On M+ Cells Amentioning

confidence: 99%

“…In a previous electron microscopic study of streptococci (20), it was suggested that iV[ protein occurs as a "microcapsule" on the surface of the organisms. While it seems probable that the material designated as microcapsule corresponds to the surface fimbriae described in the present report, the published micrographs do not permit direct comparison.…”

Section: Appearance Of M-associated Fimbriae After Nitrous Acid Extramentioning

confidence: 99%

Electron Microscopic Studies on Streptococci

Swanson

Hsu

Gotschlich

1969

The Journal of Experimental Medicine

226

127

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Extensive chemical and immunological studies have characterized the group A streptococcal cell wall as composed of four major components: M protein (and related T and R antigens), carbohydrate, mucopeptide, and glycerol teichoic acid (1, 2). These cell wall constituents, along with an external capsule and an underlying cytoplasmic membrane, are important in determining the relationship between group A streptococci and their human hosts (3). Our aim is to define the morphology and location of each of the major components of the streptococcal cell wall. The first component we have studied is the M antigen or M protein, the topic of this report.M protein plays a role in determining virulence of streptococci, inhibits phagocytosis of the organisms by leukocytes, and stimulates production of type-specific, protective antibodies by the animal host (4). These effects, together with other properties attributable to the protein, have suggested to previous investigators that the M antigen is on the exterior of group A streptococci (1, 4). Our electron microscopic findings substantiate this concept. We have found that the presence of M antigen is associated with hair-like fimbriae on the outer surfaces of several strains of group A streptococci. It appears that multiple M antigenic sites reside along the length of the fimbriae. R antigens may be associated with the same type of fimbriae. We have also obtained data suggesting the attachment of the M-associated fimbriae to the underlying portions of the cell wall. Finally, our studies suggest that M protein is not incorporated into the cell wall simultaneous to the synthesis of other portions of the wall.

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“…The teins, have contributed to an understanding of potential elucidation of the roles of individual cell-wall macgrowth mechanistns; yet the roles of specific wall mac-rotnolecules that contribute to or participate in wall romolectiles involved have not been determined, growth will require the use of inhibitors that act specifi-Inhibitors have been of some value in studies of wall cally and in a nontoxic fashion, growth (Ray 1962, Nevins 1975, Cleland 1976 In this paper we report on the potential of using an-tibodies, raised against cell-wall protein, as inhibitors of growth. Antibodies have been successftilly employed in studies of bacterial wall metabolism (Cole 1966). More recently, in an investigation of .abscission.…”

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confidence: 99%

Wall‐protein antibodies as inhibitors of growth and of autolytic reactions of isolated cell wall

Huber

Nevins

1981

Physiologia Plantarum

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Antiserum raised against protein prepared from corn (Zea mays L. hybrid B73 X Mo17) seedling cell wall exhibits antigrowth activity and inhibits autolytic reactions of isolated cell wall. The growth of corn coleoptile segments pretreated in wall‐protein antiserum was inhibited 35% compared to tissue which had been exposed to normal serum. Since the cuticle constituted a barrier to the entry of serum protein the coleoptile surface was abraded prior to exposure to the serum. Growth inhibition observed in nonabraded sections (8 to 10%) was apparently the result of the entry of serum protein via the cut ends of the tissue. Subsections recut from the central region of antiserum‐treated, nonabraded coleoptiles responded normally in growth experiments. Antiserum brought in contact with isolated cell wall prior to its use with intact coleoptiles was less effective as a growth inhibitor, which suggested that the antibodies which impede growth responses bind to cell wall. Wall‐protein antiserum also strongly inhibited autolytic reactions of isolated cell wall. Wall treated in normal serum or buffer liberated sugars at a rate of 8.6 μg‐ (mg wall dry‐weight)−1·h−1 while antiserum‐treated wall autolyzed at a rate of 2.6 μg·mg−1·h−1 representing a 70% reduction in autolytic potential. After 24 h yields from antiserum‐treated wall were 50% lower than yields obtained from control wall. The antiserum had no effect on the molecular‐weight distribution of the autolytically‐liberated products, and direct assays of wall‐bound and solubilized endo‐ and exo‐β‐d‐glucanases involved in autolytic reactions demonstrated no significant impairment of their catalytic activity. However, the addition to antiserum‐treated wall of a wall‐protein preparation containing autolytic enzymes resulted in a significant enhancement (132%) in autolytic potential. The evidence suggests that enzyme mobility may be critical in the autolytic hydrolytsis of plant cell wall.

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Symposium on the fine structure and replication of bacteria and their parts. 3. Bacterial cell-wall replication followed by immunofluorescence.

Cited by 45 publications

References 32 publications

Distribution of teichoic acid in the cell wall of Bacillus subtilis

Distribution of teichoic acid in the cell wall of Bacillus subtilis

Electron Microscopic Studies on Streptococci

Wall‐protein antibodies as inhibitors of growth and of autolytic reactions of isolated cell wall

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