SPECIALIZED STRUCTURE IN THE REGION OF THE FLAGELLA TUFT IN SPIRILLUM SERPENS

1963 ◽  
Vol 9 (3) ◽  
pp. 393-401 ◽  
Author(s):  
R. G. E. Murray ◽  
A. Birch-Andersen

Sections of Vestopal embeddings stained with uranyl acetate show that the flagella originate within the plasma membrane of Spirillum serpens. The tuft or bundle of flagella originate as a knob just inside the plasma membrane and pass through the membranes individually but in a defined area. Immediately surrounding this area, and extending over the rest of the end of the cell, a fine polar membrane lies parallel to and about 200 Å inside a somewhat accentuated plasma membrane and the two are linked by delicate bars. Over this region the outer portion of the cell wall loses its usual waviness; under this region the ribosomes in the cytoplasm do not approach as closely as they do to the peripheral plasma membrane, and this retreat is even more extensive in the central portion beneath the area of insertion. The central portion is generally free of membranous organelles and of nucleoplasms; mesosomes or membranous intrusions are commonly found outside the outer border of the polar membrane. The degree of extension of the flagella bases and connection with the described structures remain unknown.

1940 ◽  
Vol 60 (3) ◽  
pp. 245-259 ◽  
Author(s):  
D. Bhatia

Ditylum Brightwelli, a marine plankton diatom, shows very peculiar osmotic relations which have recently been investigated by Gross (1939). The cells (fig. 1) consist of a central mass of protoplasm containing the nucleus and connected by a few protoplasmic strands with the peripheral plasma membrane in which are embedded numerous chromatophores. The remainder of the space inside the cell is filled with cell sap. As in other diatoms, the protoplast is enclosed by a siliceous cell wall. Gross found that Ditylum plasmolyses rapidly in isotonic and hypotonic NaCl and sugar solutions, being reduced in a few seconds to a small spherical body about one-third to one-twentieth of its original volume, similar in all respects to a resting spore. In a solution of NaCl + CaCl2, and in unbuffered artificial sea-water, plasmolysis occurs in all cells, but the process is considerably delayed and completed only after several hours. In artificial sea-water, the pH of which is adjusted to about 8, the cells remain unchanged.


2014 ◽  
Vol 13 (12) ◽  
pp. 1484-1493 ◽  
Author(s):  
Julie M. Wolf ◽  
Javier Espadas-Moreno ◽  
Jose L. Luque-Garcia ◽  
Arturo Casadevall

ABSTRACTCryptococcus neoformansproduces extracellular vesicles containing a variety of cargo, including virulence factors. To become extracellular, these vesicles not only must be released from the plasma membrane but also must pass through the dense matrix of the cell wall. The greatest unknown in the area of fungal vesicles is the mechanism by which these vesicles are released to the extracellular space given the presence of the fungal cell wall. Here we used electron microscopy techniques to image the interactions of vesicles with the cell wall. Our goal was to define the ultrastructural morphology of the process to gain insights into the mechanisms involved. We describe single and multiple vesicle-leaving events, which we hypothesized were due to plasma membrane and multivesicular body vesicle origins, respectively. We further utilized melanized cells to “trap” vesicles and visualize those passing through the cell wall. Vesicle size differed depending on whether vesicles left the cytoplasm in single versus multiple release events. Furthermore, we analyzed different vesicle populations for vesicle dimensions and protein composition. Proteomic analysis tripled the number of proteins known to be associated with vesicles. Despite separation of vesicles into batches differing in size, we did not identify major differences in protein composition. In summary, our results indicate that vesicles are generated by more than one mechanism, that vesicles exit the cell by traversing the cell wall, and that vesicle populations exist as a continuum with regard to size and protein composition.


Author(s):  
Manfred E. Bayer

Bacterial viruses adsorb specifically to receptors on the host cell surface. Although the chemical composition of some of the cell wall receptors for bacteriophages of the T-series has been described and the number of receptor sites has been estimated to be 150 to 300 per E. coli cell, the localization of the sites on the bacterial wall has been unknown.When logarithmically growing cells of E. coli are transferred into a medium containing 20% sucrose, the cells plasmolize: the protoplast shrinks and becomes separated from the somewhat rigid cell wall. When these cells are fixed in 8% Formaldehyde, post-fixed in OsO4/uranyl acetate, embedded in Vestopal W, then cut in an ultramicrotome and observed with the electron microscope, the separation of protoplast and wall becomes clearly visible, (Fig. 1, 2). At a number of locations however, the protoplasmic membrane adheres to the wall even under the considerable pull of the shrinking protoplast. Thus numerous connecting bridges are maintained between protoplast and cell wall. Estimations of the total number of such wall/membrane associations yield a number of about 300 per cell.


Author(s):  
B.K. Ghosh

Periplasm of bacteria is the space outside the permeability barrier of plasma membrane but enclosed by the cell wall. The contents of this special milieu exterior could be regulated by the plasma membrane from the internal, and by the cell wall from the external environment of the cell. Unlike the gram-negative organism, the presence of this space in gram-positive bacteria is still controversial because it cannot be clearly demonstrated. We have shown the importance of some periplasmic bodies in the secretion of penicillinase from Bacillus licheniformis.In negatively stained specimens prepared by a modified technique (Figs. 1 and 2), periplasmic space (PS) contained two kinds of structures: (i) fibrils (F, 100 Å) running perpendicular to the cell wall from the protoplast and (ii) an array of vesicles of various sizes (V), which seem to have evaginated from the protoplast.


Author(s):  
Murray Stewart ◽  
T.J. Beveridge ◽  
D. Sprott

The archaebacterium Methanospirillum hungatii has a sheath as part of its cell wall which is composed mainly of protein. Treatment with dithiothreitol or NaOH released the intact sheaths and electron micrographs of this material negatively stained with uranyl acetate showed flattened hollow tubes, about 0.5 μm diameter and several microns long, in which the patterns from the top and bottom were superimposed. Single layers, derived from broken tubes, were also seen and were more simply analysed. Figure 1 shows the general appearance of a single layer. There was a faint axial periodicity at 28.5 A, which was stronger at irregular multiples of 28.5 A (3 and 4 times were most common), and fine striations were also seen at about 3° to the tube axis. Low angle electron diffraction patterns (not shown) and optical diffraction patterns (Fig. 2) from these layers showed a complex meridian (as a result of the irregular nature of the repeat along the tube axis) which showed a clear maximum at 28.5 A, consistent with the basic subunit spacing.


Author(s):  
Richard W. Burry ◽  
Diane M. Hayes

Electron microscopic (EM) immunocytochemistry localization of the neuron specific protein p65 could show which organelles contain this antigen. Antibodies (Ab) labeled with horseradish peroxidase (HRP) followed by chromogen development show a broad diffuse label distribution within cells and restricting identification of organelles. Particulate label (e.g. 10 nm colloidal gold) is highly desirable but not practical because penetration into cells requires destroying the plasma membrane. We report pre-embedding immunocytochemistry with a particulate marker, 1 nm gold, that will pass through membranes treated with saponin, a mild detergent.Cell cultures of the rat cerebellum were fixed in buffered 4% paraformaldehyde and 0.1% glutaraldehyde (Glut.). The buffer for all incubations and rinses was phosphate buffered saline with: 1% calf serum, 0.2% saponin, 0.1% gelatin, 50 mM glycine 1 mg/ml bovine serum albumin, and (not in the HRP labeled cultures) 0.02% sodium azide. The monoclonal #48 to p65 was used with three label systems: HRP, 1 nm avidin gold with IntenSE M development, and 1 nm avidin gold with Danscher development.


1993 ◽  
Vol 3 (5) ◽  
pp. 637-646 ◽  
Author(s):  
Jian-Kang Zhu ◽  
Jun Shi ◽  
Utpal Singh ◽  
Sarah E. Wyatt ◽  
Ray A. Bressan ◽  
...  

2021 ◽  
Author(s):  
Pengbo Liang ◽  
Clara Schmitz ◽  
Beatrice Lace ◽  
Franck Anicet Ditengou ◽  
Chao Su ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document