Biological toxicity of cellulose nanocrystals (CNCs) against the luxCDABE-based bioluminescent bioreporter Escherichia coli 652T7

The results obtained from toxicity assessment of quantum dots (QDs) can be used to establish guidelines for the application of QDs in bioimaging. This paper focused on the design of a novel method to evaluate the toxicity of CdTe QDs using engineeringEscherichia colias a model. The toxicity of mercaptoacetic acid (MPA), glutathione (GSH), and L-cysteine (Cys) capped CdTe QDs was analyzed according to the heterologous protein expression in BL21/DE3, engineeringEscherichia coliextensively used for protein expression. The results showed that the MPA-CdTe QDs had more serious toxicity than the other two kinds of CdTe QDs. The microscopic images and SEM micrographs further proved that both the proliferation and the protein expression of engineeringEscherichia coliwere inhibited after treatment with MPA-CdTe QDs. The proposed method is important to evaluate biological toxicity of both QDs and other nanoparticles.

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Biological Activity of Thyme White Essential Oil Stabilized by Cellulose Nanocrystals

Biomolecules ◽

10.3390/biom9120799 ◽

2019 ◽

Vol 9 (12) ◽

pp. 799 ◽

Cited By ~ 7

Author(s):

Jonghyun Shin ◽

Kyunga Na ◽

Sungchul Shin ◽

Seon-Mi Seo ◽

Hye Jung Youn ◽

...

Keyword(s):

Escherichia Coli ◽

Essential Oil ◽

Cellulose Nanocrystals ◽

Sulfonic Acid ◽

Inhibitory Concentration ◽

Minimum Bactericidal Concentration ◽

Emulsion Stability ◽

Pickering Emulsion ◽

Fluorescent Labelling ◽

And Staphylococcus Aureus

Cellulose nanocrystals (CNCs) are produced by sulfonic acid hydrolysis and used for the formation of Pickering emulsion (PE) with thyme white essential oil (EO). Highly volatile and hydrophobic thyme white is encapsulated in PE by the amphiphilicity of CNCs. Encapsulation of EO in a CNC shell is determined by confocal microscopy with distinct fluorescent labelling. The amount of CNC affects the size distribution of PE, and the emulsion stability is confirmed by rheological property. The antimicrobial activity of the emulsion is evaluated against Escherichia coli and Staphylococcus aureus by minimal inhibitory concentration and minimum bactericidal concentration. The larvicidal activity is also investigated against Aedes albopictus by dispersing the emulsion in water.

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The impact of cellulose nanocrystals on the aggregation and initial adhesion to a solid surface of Escherichia coli K12: Role of solution chemistry

Colloids and Surfaces B Biointerfaces ◽

10.1016/j.colsurfb.2015.09.042 ◽

2015 ◽

Vol 136 ◽

pp. 570-576 ◽

Cited By ~ 3

Author(s):

Xiaohui Sun ◽

Yanxi Shao ◽

Yaman Boluk ◽

Yang Liu

Keyword(s):

Escherichia Coli ◽

Solid Surface ◽

Cellulose Nanocrystals ◽

Solution Chemistry ◽

Escherichia Coli K12 ◽

Initial Adhesion ◽

The Impact

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Novel spider web trap approach based on chitosan/cellulose nanocrystals/glycerol membrane for the detection of Escherichia coli O157:H7 on food surfaces

International Journal of Biological Macromolecules ◽

10.1016/j.ijbiomac.2019.09.225 ◽

2020 ◽

Vol 146 ◽

pp. 1009-1014 ◽

Cited By ~ 7

Author(s):

Amina Baraketi ◽

Sabato D'Auria ◽

Shiv Shankar ◽

Carole Fraschini ◽

Stephane Salmieri ◽

...

Keyword(s):

Escherichia Coli ◽

Cellulose Nanocrystals ◽

Escherichia Coli O157 ◽

Spider Web

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Structural organization of escherichia coli ribosomes as determined by immuno electron microscopy

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100081693 ◽

1978 ◽

Vol 36 (2) ◽

pp. 166-167 ◽

Cited By ~ 1

Author(s):

G. Stöffler ◽

R.W. Bald ◽

J. Dieckhoff ◽

H. Eckhard ◽

R. Lührmann ◽

...

Keyword(s):

Electron Microscopy ◽

Escherichia Coli ◽

Ribosomal Proteins ◽

Structural Organization ◽

Three Dimensional ◽

Ribosomal Subunit ◽

Spatial Arrangement ◽

Small Subunit ◽

Antibody Binding ◽

Immuno Electron Microscopy

A central step towards an understanding of the structure and function of the Escherichia coli ribosome, a large multicomponent assembly, is the elucidation of the spatial arrangement of its 54 proteins and its three rRNA molecules. The structural organization of ribosomal components has been investigated by a number of experimental approaches. Specific antibodies directed against each of the 54 ribosomal proteins of Escherichia coli have been performed to examine antibody-subunit complexes by electron microscopy. The position of the bound antibody, specific for a particular protein, can be determined; it indicates the location of the corresponding protein on the ribosomal surface.The three-dimensional distribution of each of the 21 small subunit proteins on the ribosomal surface has been determined by immuno electron microscopy: the 21 proteins have been found exposed with altogether 43 antibody binding sites. Each one of 12 proteins showed antibody binding at remote positions on the subunit surface, indicating highly extended conformations of the proteins concerned within the 30S ribosomal subunit; the remaining proteins are, however, not necessarily globular in shape (Fig. 1).

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Sites of Adsorption of the Bacteriophages T3 and T5 on the Wall of Escherichia Coli B.

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100060490 ◽

1967 ◽

Vol 25 ◽

pp. 96-97

Author(s):

Manfred E. Bayer

Keyword(s):

Escherichia Coli ◽

Cell Wall ◽

Electron Microscope ◽

Uranyl Acetate ◽

E Coli ◽

Receptor Sites ◽

Rigid Cell Wall ◽

Host Cell Surface ◽

Bacterial Viruses ◽

Escherichia Coli B

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.

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Infection of Escherichia coli with bacteriophages

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100063767 ◽

1969 ◽

Vol 27 ◽

pp. 370-371

Author(s):

Manfred E. Bayer

Keyword(s):

Escherichia Coli ◽

Nucleic Acid ◽

Cell Surface ◽

Virus Type ◽

Infection Process ◽

Adsorption Site ◽

The Other ◽

Specific Receptors ◽

Bacterial Receptors

The first step in the infection of a bacterium by a virus consists of a collision between cell and bacteriophage. The presence of virus-specific receptors on the cell surface will trigger a number of events leading eventually to release of the phage nucleic acid. The execution of the various "steps" in the infection process varies from one virus-type to the other, depending on the anatomy of the virus. Small viruses like ØX 174 and MS2 adsorb directly with their capsid to the bacterial receptors, while other phages possess attachment organelles of varying complexity. In bacteriophages T3 (Fig. 1) and T7 the small conical processes of their heads point toward the adsorption site; a welldefined baseplate is attached to the head of P22; heads without baseplates are not infective.

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The Nature of the Intramembrane Particle

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s1431927600003020 ◽

1980 ◽

Vol 38 ◽

pp. 688-691

Author(s):

A.J. Verkleij

Keyword(s):

Escherichia Coli ◽

Tight Junction ◽

Gap Junction ◽

The Other ◽

Fracture Face ◽

Band 3 Protein ◽

Satisfactory Explanation ◽

Freeze Fracturing ◽

Intramembrane Particle ◽

Luminal Membrane

Freeze-fracturing splits membranes into two helves, thus allowing an examination of the membrane interior. The 5-10 rm particles visible on both monolayers are widely assumed to be proteinaceous in nature. Most membranes do not reveal impressions complementary to particles on the opposite fracture face, if the membranes are fractured under conditions without etching. Even if it is considered that shadowing, contamination or fracturing itself might obscure complementary pits', there is no satisfactory explanation why under similar physical circimstances matching halves of other membranes can be visualized. A prominent example of uncomplementarity is found in the erythrocyte manbrane. It is wall established that band 3 protein and possibly glycophorin represents these nonccmplanentary particles. On the other hand a number of membrane types show pits opposite the particles. Scme well known examples are the ";gap junction',"; tight junction, the luminal membrane of the bladder epithelial cells and the outer membrane of Escherichia coli.

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