scholarly journals How bacterial cell division might cheat turgor pressure - a unified mechanism of septal division in Gram-positive and Gram-negative bacteria

BioEssays ◽  
2017 ◽  
Vol 39 (8) ◽  
pp. 1700045 ◽  
Author(s):  
Harold P. Erickson
2018 ◽  
Vol 4 (5) ◽  
pp. 055002 ◽  
Author(s):  
Manfred Köller ◽  
Nadine Ziegler ◽  
Christina Sengstock ◽  
Thomas A Schildhauer ◽  
Alfred Ludwig

2010 ◽  
Vol 192 (24) ◽  
pp. 6329-6335 ◽  
Author(s):  
A. K. Fenton ◽  
M. Kanna ◽  
R. D. Woods ◽  
S.-I. Aizawa ◽  
R. E. Sockett

ABSTRACT The Bdellovibrio are miniature “living antibiotic” predatory bacteria which invade, reseal, and digest other larger Gram-negative bacteria, including pathogens. Nutrients for the replication of Bdellovibrio bacteria come entirely from the digestion of the single invaded bacterium, now called a bdelloplast, which is bound by the original prey outer membrane. Bdellovibrio bacteria are efficient digesters of prey cells, yielding on average 4 to 6 progeny from digestion of a single prey cell of a genome size similar to that of the Bdellovibrio cell itself. The developmental intrabacterial cycle of Bdellovibrio is largely unknown and has never been visualized “live.” Using the latest motorized xy stage with a very defined z-axis control and engineered periplasmically fluorescent prey allows, for the first time, accurate return and visualization without prey bleaching of developing Bdellovibrio cells using solely the inner resources of a prey cell over several hours. We show that Bdellovibrio bacteria do not follow the familiar pattern of bacterial cell division by binary fission. Instead, they septate synchronously to produce both odd and even numbers of progeny, even when two separate Bdellovibrio cells have invaded and develop within a single prey bacterium, producing two different amounts of progeny. Evolution of this novel septation pattern, allowing odd progeny yields, allows optimal use of the finite prey cell resources to produce maximal replicated, predatory bacteria. When replication is complete, Bdellovibrio cells exit the exhausted prey and are seen leaving via discrete pores rather than by breakdown of the entire outer membrane of the prey.


1952 ◽  
Vol 30 (4) ◽  
pp. 486-489 ◽  
Author(s):  
Russell E. MacDonald ◽  
Charles J. Bishop

A crystalline antibacterial substance isolated from apple leaves has been identified as phloretin. It has been shown to inhibit the growth of a number of Gram-positive and Gram-negative bacteria. The activity of the compound is bacteriostatic in nature and is shown in concentrations as low as 30 p.p.m. Its antibacterial action may be related to inhibition of the uptake of phosphorus by the bacterial cell.


Author(s):  
Stevan R. Emmett ◽  
Nicola Hill ◽  
Federico Dajas-Bailador

Antibiotics include an extensive range of agents able to kill or prevent reproduction of bacteria in the body, without being overly toxic to the patient. Traditionally derived from living organisms, most are now chemically synthesized and act to disrupt the integrity of the bacterial cell wall, or penetrate the cell and disrupt protein synthesis or nucleic acid replication. Typically, bacteria are identified according to their ap­pearance under the microscope depending on shape and response to the Gram stain test. Further identification is obtained by growth characteristics on various types of culture media, based on broth or agar, biochemical and immunological profiles. Further testing on broth or agar determines antibiotic sensitivity to guide on anti­biotic therapy in individual patients. This process can take 24– 48 hours to culture and a further 24– 48 hours to measure sensitivities. Increasingly, new technology, e.g. Matrix Assisted Laser Desorption Ionization— Time of Flight (MALDI- TOF) and nucleic acid amplification as­says, are being used to provide more rapid identification. The Gram classification, however, is still widely referred to as it differentiates bacteria by the presence or absence of the outer lipid membrane (see Figure 11.1), a fundamental characteristic that influences antibiotic management. Antimicrobial agents rely on selective action exploiting genetic differences between bacterial and eukaryotic cells. They target bacterial cell wall synthesis, bacterial protein synthesis, microbial DNA or RNA synthesis, by acting on bacterial cell metabolic pathways or by inhibiting the ac­tion of a bacterial toxin (see Table 11.1). Both Gram- positive and Gram- negative bacteria possess a rigid cell wall able to protect the bacteria from varying osmotic pressures (Figure 11.1). Peptidoglycan gives the cell wall its rigidity and is composed of a glycan chain of complex alternating carbohydrates, N- acetylglucosamide (N- ATG), and N- acetylmurcarinic acid (N- ATM), that are cross- linked by peptide (or glycine) chains. In Gram-positive bacteria, the cell wall contains multiple peptido­glycan layers, interspersed with teichoic acids, whereas Gram- negative bacteria contain only one or two peptido­glycan layers that are surrounded by an outer membrane attached by lipoproteins. The outer membrane contains porins (which regulate transport of substances into and out of the cell), lipopolysaccharides, and outer proteins in a phospholipid bilayer. For both Gram- negative and Gram-positive bacteria, peptidoglycan synthesis involves about 30 bacterial enzymes acting over three stages. Since the cell wall is unique to bacteria, it makes a suitable target for antibiotic therapy.


Toxins ◽  
2020 ◽  
Vol 12 (12) ◽  
pp. 771
Author(s):  
Lipeng Zhong ◽  
Jiye Liu ◽  
Shiyu Teng ◽  
Zhixiong Xie

The abuse of antibiotics and the consequent increase of drug-resistant bacteria constitute a serious threat to human health, and new antibiotics are urgently needed. Research shows that antimicrobial peptides produced by natural organisms are potential substitutes for antibiotics. Based on Deinagkistrodonacutus (known as five-pacer viper) genome bioinformatics analysis, we discovered a new cathelicidin antibacterial peptide which was called FP-CATH. Circular dichromatic analysis showed a typical helical structure. FP-CATH showed broad-spectrum antibacterial activity. It has antibacterial activity to Gram-negative bacteria and Gram-positive bacteria including methicillin-resistant Staphylococcus aureus (MRSA). The results of transmission electron microscopy (TEM) and scanning electron microscopy (SEM) showed that FP-CATH could cause the change of bacterial cell integrity, having a destructive effect on Gram-negative bacteria and inducing Gram-positive bacterial surface formation of vesicular structure. FP-CATH could bind to LPS and showed strong binding ability to bacterial DNA. In vivo, FP-CATH can improve the survival rate of nematodes in bacterial invasion experiments, and has a certain protective effect on nematodes. To sum up, FP-CATH is likely to play a role in multiple mechanisms of antibacterial action by impacting bacterial cell integrity and binding to bacterial biomolecules. It is hoped that the study of FP-CATH antibacterial mechanisms will prove useful for development of novel antibiotics.


mBio ◽  
2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Tanneke den Blaauwen ◽  
Joen Luirink

ABSTRACT Assembly of the division machinery in Gram-negative and Gram-positive bacteria occurs in two time-dependent steps. First, the FtsZ proto-ring localizes at midcell including some FtsN molecules. Subsequently, the proteins that catalyze and regulate septal peptidoglycan (PG) synthesis are recruited including among others, the FtsBLQ-PB1B-FtsW-PBP3 complex. Further accumulation of FtsN finally allows initiation of cell division. It was known that FtsA and FtsQLB somehow prevented this initiation. Recently, A. Boes, S. Olatunji, E. Breukink, and M. Terrak (mBio 10:e01912-18, 2019, https://doi.org/10.1128/mBio.01912-18) reported that this is caused by inhibition of the activity of the PG synthases by FtsBLQ, which has to be outcompeted by accumulation of the PBP1b activating FtsN. This supports a central structural as well as regulatory role for the FtsBLQ protein complex that is conserved only in prokaryotes, making it an attractive target for antibiotic development.


2019 ◽  
Author(s):  
Lam T. Nguyen ◽  
Catherine M. Oikonomou ◽  
Grant J. Jensen

ABSTRACTTo divide, bacteria must constrict their membranes against significant force from turgor pressure. A tubulin homo-log, FtsZ, is thought to drive constriction, but how FtsZ filaments might generate constrictive force in the absence of motor proteins is not well understood. There are two predominant models in the field. In one, filaments overlap to form complete rings around the circumference of the cell; as filaments slide against each other to maximize lateral contact, the rings constrict. In the other, filaments exert force on the membrane by a GTP-hydrolysis-induced switch in conformation from straight to bent. Here we developed software, ZCONSTRICT, for quantitative 3D simulations of Gram-negative bacterial cell division to test these two models and identify critical conditions required for them to work. We find that the avidity of lateral interactions quickly halts the sliding of filaments, so a mechanism such as depolymerization or treadmilling is required to sustain constriction by filament sliding. For filament bending, we find that a mechanism such as the presence of a rigid linker is required to constrain bending within the division plane and maintain the distance observed in vivo between the filaments and the membrane. We also explored the recent observation of constriction associated with a single FtsZ filament and found that it can be explained by the filament bending model if there is a rigid connection between the filament and the cell wall. Together, our work sheds light on the physical principles underlying bacterial cell division and informs future experiments to elucidate the mechanism of FtsZ.


2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Lam T. Nguyen ◽  
Catherine M. Oikonomou ◽  
H. Jane Ding ◽  
Mohammed Kaplan ◽  
Qing Yao ◽  
...  

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