Supramolecular self-assemblies for bacterial cell agglutination driven by directional charge-transfer interactions

2018 ◽  
Vol 54 (23) ◽  
pp. 2922-2925 ◽  
Author(s):  
Dan Wu ◽  
Jie Shen ◽  
Hongzhen Bai ◽  
Guocan Yu
Keyword(s):  
Charge Transfer ◽  
Bacterial Cell ◽  
Cell Agglutination ◽  
E Coli ◽  
A Cell ◽  
Multivalent Interactions ◽  
Supramolecular Amphiphiles

Two supramolecular amphiphiles are fabricated through directional charge-transfer interactions, which self-assemble into nanofibers and nanoribbons. Due to the existence of galactose on their surface, these self-assemblies act as a cell glue to agglutinate E. coli, benefiting from multivalent interactions.

Fe(iii)-complex mediated bacterial cell surface immobilization of eGFP and enzymes

2021 ◽  
Author(s):  
Lilin Feng ◽  
Liang Gao ◽  
Daniel F. Sauer ◽  
Yu Ji ◽  
Haiyang Cui ◽  
...  
Keyword(s):  
Cell Surface ◽  
Bacterial Cell ◽  
Surface Immobilization ◽  
E Coli ◽  
Bacterial Cell Surface ◽  
Reversible Method

A facile and reversible method to immobilize His6-tagged proteins on the E. coli cell surface through the formation of an Fe(iii)-complex.

Redox responsive supramolecular amphiphiles based on reversible charge transfer interactions

2009 ◽  
pp. 5380 ◽  
Author(s):  
Chao Wang ◽  
Yinsheng Guo ◽  
Yapei Wang ◽  
Huaping Xu ◽  
Xi Zhang
Keyword(s):  
Charge Transfer ◽  
Redox Responsive ◽  
Supramolecular Amphiphiles

Multivalent Nanofibers of a Controlled Length: Regulation of Bacterial Cell Agglutination

2012 ◽  
Vol 134 (36) ◽  
pp. 14722-14725 ◽  
Author(s):  
Dong-Woo Lee ◽  
Taehoon Kim ◽  
Il-Soo Park ◽  
Zhegang Huang ◽  
Myongsoo Lee
Keyword(s):  
Bacterial Cell ◽  
Cell Agglutination ◽  
Length Regulation

scholarly journals Of the Morphogenes that Make a Ring, A Rod and a Sphere in Escherichia Coli

2007 ◽  
Vol 90 (2-3) ◽  
pp. 59-72 ◽  
Author(s):  
Medhatm Khattar ◽  
Issmat I. Kassem ◽  
Ziad W. El-Hajj
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
Bacterial Cell ◽  
Bacterial Cell Division ◽  
Antibacterial Compounds ◽  
E Coli ◽  
The Past ◽  
New Knowledge ◽  
Fundamental Process ◽  
Simple Question

In 1993, William Donachie wrote “The success of molecular genetics in the study of bacterial cell division has been so great that we find ourselves, armed with much greater knowledge of detail, confronted once again with the same naive questions that we set to answer in the first place”1. Indeed, attempts to answer the apparently simple question of how a bacterial cell divides have led to a wealth of new knowledge, in particular over the past decade and a half. And while some questions have been answered to a great extent since the early reports of isolation of division mutants of Escherichia coli2,3, some key pieces of the puzzle remain elusive. In addition to it being a fundamental process in bacteria that merits investigation in its own right, studying the process of cell division offers an abundance of new targets for the development of new antibacterial compounds that act directly against key division proteins and other components of the cytoskeleton, which are encoded by the morphogenes of E. coli4. This review aims to present the reader with a snapshot summary of the key players in E. coli morphogenesis with emphasis on cell division and the rod to sphere transition.

scholarly journals High-resolution crystal structures of Escherichia coli FtsZ bound to GDP and GTP

2020 ◽  
Vol 76 (2) ◽  
pp. 94-102 ◽  
Author(s):  
Maria A. Schumacher ◽  
Tomoo Ohashi ◽  
Lauren Corbin ◽  
Harold P. Erickson
Keyword(s):  
Escherichia Coli ◽  
Staphylococcus Aureus ◽  
Cell Division ◽  
High Resolution ◽  
Crystal Structures ◽  
Bacterial Cell ◽  
Model System ◽  
E Coli ◽  
Z Ring ◽  
Main Model

Bacterial cytokinesis is mediated by the Z-ring, which is formed by the prokaryotic tubulin homolog FtsZ. Recent data indicate that the Z-ring is composed of small patches of FtsZ protofilaments that travel around the bacterial cell by treadmilling. Treadmilling involves a switch from a relaxed (R) state, favored for monomers, to a tense (T) conformation, which is favored upon association into filaments. The R conformation has been observed in numerous monomeric FtsZ crystal structures and the T conformation in Staphylococcus aureus FtsZ crystallized as assembled filaments. However, while Escherichia coli has served as a main model system for the study of the Z-ring and the associated divisome, a structure has not yet been reported for E. coli FtsZ. To address this gap, structures were determined of the E. coli FtsZ mutant FtsZ(L178E) with GDP and GTP bound to 1.35 and 1.40 Å resolution, respectively. The E. coli FtsZ(L178E) structures both crystallized as straight filaments with subunits in the R conformation. These high-resolution structures can be employed to facilitate experimental cell-division studies and their interpretation in E. coli.

scholarly journals Cell-Free Protein Synthesis by Diversifying Bacterial Transcription Machinery

BioTech ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 24
Author(s):  
Marina Snapyan ◽  
Sylvain Robin ◽  
Garabet Yeretssian ◽  
Michèle Lecocq ◽  
Frédéric Marc ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Genomic Sequence ◽  
Synthetic Activity ◽  
Translation System ◽  
Free System ◽  
Transcription Terminator ◽  
Cell Free System ◽  
E Coli ◽  
Bacterial Transcription ◽  
A Cell

We have evaluated several approaches to increase protein synthesis in a cell-free coupled bacterial transcription and translation system. A strong pargC promoter, originally isolated from a moderate thermophilic bacterium Geobacillus stearothermophilus, was used to improve the performance of a cell-free system in extracts of Escherichia coli BL21 (DE3). A stimulating effect on protein synthesis was detected with extracts prepared from recombinant cells, in which the E. coli RNA polymerase subunits α, β, β’ and ω are simultaneously coexpressed. Appending a 3′ UTR genomic sequence and a T7 transcription terminator to the protein-coding region also improves the synthetic activity of some genes from linear DNA. The E. coli BL21 (DE3) rna::Tn10 mutant deficient in a periplasmic RNase I was constructed. The mutant cell-free extract increases by up to four-fold the expression of bacterial and human genes mediated from both bacterial pargC and phage pT7 promoters. By contrast, the RNase E deficiency does not affect the cell-free expression of the same genes. The regulatory proteins of the extremophilic bacterium Thermotoga, synthesized in a cell-free system, can provide the binding capacity to target DNA regions. The advantageous characteristics of cell-free systems described open attractive opportunities for high-throughput screening assays.

scholarly journals Evaluating the abilities of diverse nitroaromatic prodrug metabolites to exit a model Gram negative vector for bacterial-directed enzyme-prodrug therapy

2020 ◽  
Author(s):  
JVE Chan-Hyams ◽  
JN Copp ◽  
JB Smaill ◽  
AV Patterson ◽  
David Ackerley
Keyword(s):  
Human Cell ◽  
Bacterial Cell ◽  
Bystander Effect ◽  
Cell Transfer ◽  
Bacterial Strains ◽  
Enzyme Prodrug Therapy ◽  
E Coli ◽  
Human Cell Cultures ◽  
Cell To Cell Transfer ◽  
Nitro Reduction

© 2018 Elsevier Inc. Gene-directed enzyme-prodrug therapy (GDEPT) employs tumour-tropic vectors including viruses and bacteria to deliver a genetically-encoded prodrug-converting enzyme to the tumour environment, thereby sensitising the tumour to the prodrug. Nitroreductases, able to activate a range of promising nitroaromatic prodrugs to genotoxic metabolites, are of great interest for GDEPT. The bystander effect (cell-to-cell transfer of activated prodrug metabolites) has been quantified for some nitroaromatic prodrugs in mixed multilayer human cell cultures, however while these provide a good model for viral DEPT (VDEPT) they do not inform on the ability of these prodrug metabolites to exit bacterial vectors (relevant to bacterial-DEPT (BDEPT)). To investigate this we grew two Escherichia coli strains in co-culture; an activator strain expressing the nitroreductase E. coli NfsA and a recipient strain containing an SOS-GFP DNA damage responsive gene construct. In this system, induction of GFP by reduced prodrug metabolites can only occur following their transfer from the activator to the recipient cells. We used this to investigate five clinically relevant prodrugs: metronidazole, CB1954, nitro-CBI-DEI, and two dinitrobenzamide mustard prodrug analogues, PR-104A and SN27686. Consistent with the bystander efficiencies previously measured in human cell multilayers, reduced metronidazole exhibited little bacterial cell-to-cell transfer, whereas nitro-CBI-DEI was passed very efficiently from activator to recipient cells post-reduction. However, in contrast with observations in human cell multilayers, the nitrogen mustard prodrug metabolites were not effectively passed between the two bacterial strains, whereas reduced CB1954 was transferred efficiently. Using nitroreductase enzymes that exhibit different biases for the 2- versus 4-nitro substituents of CB1954, we further showed that the 2-nitro reduction products exhibit substantially higher levels of bacterial cell-to-cell transfer than the 4-nitro reduction products, consistent with their relative bystander efficiencies in human cell culture. Overall, our data suggest that prodrugs may differ in their suitability for VDEPT versus BDEPT applications and emphasise the importance of evaluating an enzyme-prodrug partnership in an appropriate context for the intended vector.

scholarly journals Bacterial Cell Inactivation Using a Single-Frequency Batch-Type Ultrasound Device

2021 ◽  
Vol 6 (1) ◽  
pp. 65-80
Author(s):  
Poetro Sambegoro ◽  
Maya Fitriyanti ◽  
Bentang Arief Budiman ◽  
Kamarisima Kamarisima ◽  
Sekar Wangi Arraudah Baliwangi ◽  
...  
Keyword(s):  
Bacterial Cell ◽  
Treatment Time ◽  
Low Cost ◽  
Single Frequency ◽  
Bacterial Cells ◽  
Cell Inactivation ◽  
E Coli ◽  
Commercial System ◽  
Ultrasound Device ◽  
Frequency Ultrasound

Ultrasound technology employs cavitation to generate high-pressure soundwaves to disrupt bacterial cells. This study reveals the effectiveness of a single frequency ultrasound device for bacterial cell inactivation. A low-cost ultrasound device having a single frequency, i.e. 22 kHz for lab-scale application, was developed first, and the prototype was mechanically designed and analyzed using the finite-element method to assure the targeted natural frequency could be achieved. The prototype was then tested inactivating bacterial cells, Escherichia coli (E. coli) and Bacillus subtilis (B. subtilis), in a simple medium and a food system, and the results were then compared to a commercial system. A treatment time of up to 15 minutes was able to reduce E. coli and B. subtilis cells by 3.3 log and 2.8 log, respectively, and these results were similar to those of the commercial system. The effectiveness of bacterial cell inactivation using the developed single-frequency ultrasound device is then discussed. The findings are useful for designing low-cost ultrasound devices for application in the food industry.

scholarly journals An analysis of lectin-initiated cell agglutination in a series of CHO subclones which respond morphologically to growth in dibutyryl cyclic AMP.

1976 ◽  
Vol 70 (1) ◽  
pp. 204-216 ◽  
Author(s):  
J van Veen ◽  
R M Roberts ◽  
K D Noonan
Keyword(s):  
Surface Membrane ◽  
Con A ◽  
Cell Agglutination ◽  
Lectin Receptors ◽  
Lectin Receptor ◽  
Free Mobility ◽  
Receptor Sites ◽  
Protein And Rna Synthesis ◽  
A Cell ◽  
Membrane Components

We have investigated the molecular basis of the agglutinability of CHO subclones which respond differentially in terms of morphology and surface architecture in the presence of dB-cAMP in the medium. We have demonstrated that the agglutinability of these subclones with both wheat germ agglutinin (WGA) and concanavalin A (Con A) probably depends on the free lateral mobility of the lectin receptor sites in the plane of the membrane. The nonagglutinable surface architecture seems to depend on the presence in the membrane of a protease-labile peptide(s), which appears to be distinct from the lectin receptors, as well as on continuous protein and RNA synthesis. This dependence on continuous transcription and translation may be related to the maintenance of the protease-labile peptide(s) in such a state as to restrict mobility of the lectin receptors. The surface architecture defined as nonagglutinable also depends on the state of polymerization of the intracellular microtubules and microfilaments. It is suggested that these microskeletal elements serve to anchor the lectin receptors in such a manner as to restrict their mobility and thereby reduce the relative agglutinability of a cell line. We suggest that control of the free mobility of both the Con A and WGA receptor sites is dependent on two constraints, one applied by protease-labile ("surface") membrane components and the other by components of the intracellular microskeletal system.

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