scholarly journals Cell wall deficiency as an escape mechanism from phage infection

Open Biology ◽  
2021 ◽  
Vol 11 (9) ◽  
pp. 210199
Author(s):  
Véronique Ongenae ◽  
Ariane Briegel ◽  
Dennis Claessen
Keyword(s):  
Cell Wall ◽  
Phage Therapy ◽  
Cell Envelope ◽  
Environmental Stresses ◽  
Phage Infection ◽  
Abortive Infection ◽  
Escape Mechanism ◽  
A Cell ◽  
Restriction Modification ◽  
Unwanted Consequence

The cell wall plays a central role in protecting bacteria from some environmental stresses, but not against all. In fact, in some cases, an elaborate cell envelope may even render the cell more vulnerable. For example, it contains molecules or complexes that bacteriophages recognize as the first step of host invasion, such as proteins and sugars, or cell appendages such as pili or flagella. In order to counteract phages, bacteria have evolved multiple escape mechanisms, such as restriction-modification, abortive infection, CRISPR/Cas systems or phage inhibitors. In this perspective review, we present the hypothesis that bacteria may have additional means to escape phage attack. Some bacteria are known to be able to shed their cell wall in response to environmental stresses, yielding cells that transiently lack a cell wall. In this wall-less state, the bacteria may be temporarily protected against phages, since they lack the essential entities that are necessary for phage binding and infection. Given that cell wall deficiency can be triggered by clinically administered antibiotics, phage escape could be an unwanted consequence that limits the use of phage therapy for treating stubborn infections.

scholarly journals L-form bacteria, cell walls and the origins of life

Open Biology ◽  
2013 ◽  
Vol 3 (1) ◽  
pp. 120143 ◽  
Author(s):  
Jeff Errington
Keyword(s):  
Cell Wall ◽  
Cell Envelope ◽  
Evolutionary Development ◽  
Last Common Ancestor ◽  
Bacterial Cells ◽  
A Cell ◽  
Evolutionary Radiations ◽  
Key Steps ◽  
Bacterial Domain

The peptidoglycan wall is a defining feature of bacterial cells and was probably already present in their last common ancestor. L-forms are bacterial variants that lack a cell wall and divide by a variety of processes involving membrane blebbing, tubulation, vesiculation and fission. Their unusual mode of proliferation provides a model for primitive cells and is reminiscent of recently developed in vitro vesicle reproduction processes. Invention of the cell wall may have underpinned the explosion of bacterial life on the Earth. Later innovations in cell envelope structure, particularly the emergence of the outer membrane of Gram-negative bacteria, possibly in an early endospore former, seem to have spurned further major evolutionary radiations. Comparative studies of bacterial cell envelope structure may help to resolve the early key steps in evolutionary development of the bacterial domain of life.

scholarly journals Mutations in the Lipopolysaccharide Biosynthesis Pathway Interfere with Crescentin-Mediated Cell Curvature in Caulobacter crescentus

2010 ◽  
Vol 192 (13) ◽  
pp. 3368-3378 ◽  
Author(s):  
Matthew T. Cabeen ◽  
Michelle A. Murolo ◽  
Ariane Briegel ◽  
N. Khai Bui ◽  
Waldemar Vollmer ◽  
...  
Keyword(s):  
Cell Wall ◽  
Caulobacter Crescentus ◽  
Cell Envelope ◽  
Cellular Systems ◽  
Biosynthesis Pathway ◽  
Cell Morphogenesis ◽  
Division Site ◽  
Growth Properties ◽  
A Cell ◽  
Cellular Components

ABSTRACT Bacterial cell morphogenesis requires coordination among multiple cellular systems, including the bacterial cytoskeleton and the cell wall. In the vibrioid bacterium Caulobacter crescentus, the intermediate filament-like protein crescentin forms a cell envelope-associated cytoskeletal structure that controls cell wall growth to generate cell curvature. We undertook a genetic screen to find other cellular components important for cell curvature. Here we report that deletion of a gene (wbqL) involved in the lipopolysaccharide (LPS) biosynthesis pathway abolishes cell curvature. Loss of WbqL function leads to the accumulation of an aberrant O-polysaccharide species and to the release of the S layer in the culture medium. Epistasis and microscopy experiments show that neither S-layer nor O-polysaccharide production is required for curved cell morphology per se but that production of the altered O-polysaccharide species abolishes cell curvature by apparently interfering with the ability of the crescentin structure to associate with the cell envelope. Our data suggest that perturbations in a cellular pathway that is itself fully dispensable for cell curvature can cause a disruption of cell morphogenesis, highlighting the delicate harmony among unrelated cellular systems. Using the wbqL mutant, we also show that the normal assembly and growth properties of the crescentin structure are independent of its association with the cell envelope. However, this envelope association is important for facilitating the local disruption of the stable crescentin structure at the division site during cytokinesis.

scholarly journals Cell-Associated Pheromone Peptide (cCF10) Production and Pheromone Inhibition in Enterococcus faecalis

2000 ◽  
Vol 182 (17) ◽  
pp. 4926-4933 ◽  
Author(s):  
B. A. (Leonard) Buttaro ◽  
M. H. Antiporta ◽  
G. M. Dunny
Keyword(s):  
Cell Wall ◽  
Protease Inhibitor ◽  
Enterococcus Faecalis ◽  
Cell Envelope ◽  
Conjugative Plasmid ◽  
Cell Fractionation ◽  
Cell Wall Fraction ◽  
Donor Cells ◽  
Pheromone Activity ◽  
A Cell

ABSTRACT In Enterococcus faecalis, the peptide cCF10 acts as a pheromone, inducing transfer of the conjugative plasmid pCF10 from plasmid-containing donor cells to plasmid-free recipient cells. In these studies, it was found that a substantial amount of cCF10 associates with the envelope of the producing cell. Pheromone activity was detected in both wall and membrane fractions, with the highest activity associated with the wall. Experiments examining the effects of protease inhibitor treatments either prior to or following cell fractionation suggested the presence of a cell envelope-associated pro-cCF10 that can be processed to mature cCF10 by a maturase or protease. A pCF10-encoded membrane protein, PrgY, was shown to prevent self-induction of donor cells by reducing the level of pheromone activity in the cell wall fraction.

scholarly journals A cell wall damage response mediated by a sensor kinase/response regulator pair enables beta-lactam tolerance

2015 ◽  
Vol 113 (2) ◽  
pp. 404-409 ◽  
Author(s):  
Tobias Dörr ◽  
Laura Alvarez ◽  
Fernanda Delgado ◽  
Brigid M. Davis ◽  
Felipe Cava ◽  
...  
Keyword(s):  
Cell Wall ◽  
Response Regulator ◽  
Cell Envelope ◽  
Normal Growth ◽  
Cell Diameter ◽  
Cell Wall Synthesis ◽  
Beta Lactam ◽  
Cell Wall Damage ◽  
A Cell

The bacterial cell wall is critical for maintenance of cell shape and survival. Following exposure to antibiotics that target enzymes required for cell wall synthesis, bacteria typically lyse. Although several cell envelope stress response systems have been well described, there is little knowledge of systems that modulate cell wall synthesis in response to cell wall damage, particularly in Gram-negative bacteria. Here we describe WigK/WigR, a histidine kinase/response regulator pair that enablesVibrio cholerae, the cholera pathogen, to survive exposure to antibiotics targeting cell wall synthesis in vitro and during infection. Unlike wild-typeV. cholerae, mutants lackingwigRfail to recover following exposure to cell-wall–acting antibiotics, and they exhibit a drastically increased cell diameter in the absence of such antibiotics. Conversely, overexpression ofwigRleads to cell slimming. Overexpression of activated WigR also results in increased expression of the full set of cell wall synthesis genes and to elevated cell wall content. WigKR-dependent expression of cell wall synthesis genes is induced by various cell-wall–acting antibiotics as well as by overexpression of an endogenous cell wall hydrolase. Thus, WigKR appears to monitor cell wall integrity and to enhance the capacity for increased cell wall production in response to damage. Taken together, these findings implicate WigKR as a regulator of cell wall synthesis that controls cell wall homeostasis in response to antibiotics and likely during normal growth as well.

The outer layer of the cell envelope of Halobacterium halobium

1969 ◽  
Vol 47 (1) ◽  
pp. 71-74 ◽  
Author(s):  
Carolyn L. Marshall ◽  
A. J. Wicken ◽  
A. D. Brown
Keyword(s):  
Cell Wall ◽  
Chemical Analysis ◽  
Outer Layer ◽  
Bacterial Cell ◽  
Cell Walls ◽  
Cell Envelope ◽  
Halobacterium Halobium ◽  
A Cell ◽  
Bacterial Cell Walls

The outer layer of the cell envelope of Halobacterium halobium was isolated after suspending the envelope in either 1 M NaCl or 0.02 M MgCl2. Chemical analysis of the isolated, solubilized outer layer showed it to consist of protein or glycoprotein with about 3% RNA. No free or bound lipid was detected. No cytochromes were present in the outer layer. Components commonly associated with bacterial cell walls were absent.Chemical composition together with the marked instability of the outer layer in a slight ion deficit are not consistent with a function of this layer as a "cell wall" of the organism.

scholarly journals Streptococcus thermophilus Cell Wall-Anchored Proteinase: Release, Purification, and Biochemical and Genetic Characterization

2000 ◽  
Vol 66 (11) ◽  
pp. 4772-4778 ◽  
Author(s):  
María Dolores Fernandez-Espla ◽  
Peggy Garault ◽  
Véronique Monnet ◽  
Françoise Rul
Keyword(s):  
Cell Wall ◽  
Lactic Acid ◽  
Lactic Acid Bacteria ◽  
Cell Envelope ◽  
Serine Proteinase ◽  
Streptococcus Thermophilus ◽  
Alumina Powder ◽  
A Cell ◽  
Cell Envelopes

ABSTRACT Streptococcus thermophilus CNRZ 385 expresses a cell envelope proteinase (PrtS), which is characterized in the present work, both at the biochemical and genetic levels. Since PrtS is resistant to most classical methods of extraction from the cell envelopes, we developed a three-step process based on loosening of the cell wall by cultivation of the cells in the presence of glycine (20 mM), mechanical disruption (with alumina powder), and enzymatic treatment (lysozyme). The pure enzyme is a serine proteinase highly activated by Ca2+ ions. Its activity was optimal at 37°C and pH 7.5 with acetyl-Ala-Ala-Pro-Phe-paranitroanilide as substrate. The study of the hydrolysis of the chromogenic and casein substrates indicated that PrtS presented an intermediate specificity between the most divergent types of cell envelope proteinases from lactococci, known as the PI and PIII types. This result was confirmed by the sequence determination of the regions involved in substrate specificity, which were a mix between those of PI and PIII types, and also had unique residues. Sequence analysis of the PrtS encoding gene revealed that PrtS is a member of the subtilase family. It is a multidomain protein which is maturated and tightly anchored to the cell wall via a mechanism involving an LPXTG motif. PrtS bears similarities to cell envelope proteinases from pyogenic streptococci (C5a peptidase and cell surface proteinase) and lactic acid bacteria (PrtP, PrtH, and PrtB). The highest homologies were found with streptococcal proteinases which lack, as PrtS, one domain (the B domain) present in cell envelope proteinases from all other lactic acid bacteria.

Cell-Wall-Bound Proteinase of Lactobacillus delbrueckii subsp. lactis ACA-DC 178: Characterization and Specificity for β-Casein

1999 ◽  
Vol 65 (5) ◽  
pp. 2035-2040 ◽  
Author(s):  
E. Tsakalidou ◽  
R. Anastasiou ◽  
I. Vandenberghe ◽  
J. van Beeumen ◽  
G. Kalantzopoulos
Keyword(s):  
Cell Wall ◽  
Substrate Specificity ◽  
Cell Envelope ◽  
Lactobacillus Delbrueckii ◽  
Phenylmethylsulfonyl Fluoride ◽  
A Cell ◽  
Lactobacillus Delbrueckii Subsp

ABSTRACT Lactobacillus delbrueckii subsp. lactisACA-DC 178, which was isolated from Greek Kasseri cheese, produces a cell-wall-bound proteinase. The proteinase was removed from the cell envelope by washing the cells with a Ca2+-free buffer. The crude proteinase extract shows its highest activity at pH 6.0 and 40°C. It is inhibited by phenylmethylsulfonyl fluoride, showing that the enzyme is a serine-type proteinase. Considering the substrate specificity, the enzyme is similar to the lactococcal PI-type proteinases, since it hydrolyzes β-casein mainly and α- and κ-caseins to a much lesser extent. The cell-wall-bound proteinase from L. delbrueckii subsp. lactisACA-DC 178 liberates four main peptides from β-casein, which have been identified.

scholarly journals Enzymes and Mechanisms Employed by Tailed Bacteriophages to Breach the Bacterial Cell Barriers

Viruses ◽  
2018 ◽  
Vol 10 (8) ◽  
pp. 396 ◽  
Author(s):  
Sofia Fernandes ◽  
Carlos São-José
Keyword(s):  
Cell Wall ◽  
Host Cell ◽  
Bacterial Cell ◽  
Cell Envelope ◽  
Genetic Material ◽  
Cell Types ◽  
Virus Multiplication ◽  
Virus Particles ◽  
Bacterial Cell Envelope ◽  
A Cell

Monoderm bacteria possess a cell envelope made of a cytoplasmic membrane and a cell wall, whereas diderm bacteria have and extra lipid layer, the outer membrane, covering the cell wall. Both cell types can also produce extracellular protective coats composed of polymeric substances like, for example, polysaccharidic capsules. Many of these structures form a tight physical barrier impenetrable by phage virus particles. Tailed phages evolved strategies/functions to overcome the different layers of the bacterial cell envelope, first to deliver the genetic material to the host cell cytoplasm for virus multiplication, and then to release the virion offspring at the end of the reproductive cycle. There is however a major difference between these two crucial steps of the phage infection cycle: virus entry cannot compromise cell viability, whereas effective virion progeny release requires host cell lysis. Here we present an overview of the viral structures, key protein players and mechanisms underlying phage DNA entry to bacteria, and then escape of the newly-formed virus particles from infected hosts. Understanding the biological context and mode of action of the phage-derived enzymes that compromise the bacterial cell envelope may provide valuable information for their application as antimicrobials.

scholarly journals Reversible bacteriophage resistance by shedding the bacterial cell wall

2021 ◽  
Author(s):  
Veronique Ongenae ◽  
Adam Sidi Mabrouk ◽  
Marjolein Crooijmans ◽  
Daniel Rozen ◽  
Ariane Briegel ◽  
...  
Keyword(s):  
Cell Wall ◽  
Bacterial Cell ◽  
Bacterial Population ◽  
Phage Therapy ◽  
Complete Conversion ◽  
Unknown Mechanism ◽  
Complete Eradication ◽  
Major Threat ◽  
Defense Systems ◽  
A Cell

Phages are highly abundant in the environment and a major threat for bacteria. Therefore, bacteria have evolved sophisticated defense systems to withstand phage attacks. Here, we describe a previously unknown mechanism by which mono- and diderm bacteria survive infection with diverse lytic phages. Phage exposure leads to a rapid and near complete conversion of walled cells to a cell wall-deficient state, which remain viable in osmoprotective conditions and can revert to the walled state. While shedding the cell wall dramatically reduces the number of progeny phages produced by the host, it does not always preclude phage infection. Altogether, these results show that the formation of cell wall-deficient cells prevents complete eradication of the bacterial population and suggest that cell wall-deficiency may limit the efficacy of phage therapy, especially in highly osmotic environments or when used together with antibiotics that target the cell wall.

scholarly journals An Antibiotic-Inducible Cell Wall-Associated Protein That Protects Bacillus subtilis from Autolysis

2007 ◽  
Vol 189 (13) ◽  
pp. 4671-4680 ◽  
Author(s):  
Letal I. Salzberg ◽  
John D. Helmann
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis ◽  
Cell Envelope ◽  
Sequence Similarity ◽  
Envelope Stress ◽  
Class B ◽  
Dependent Cell ◽  
A Cell ◽  
Close Relatives ◽  
Minimal Region

ABSTRACT In Bacillus subtilis, antibiotics that impair cell wall synthesis induce a characteristic stress response including the σW and σM regulons and the previously uncharacterized yoeB gene. Here we demonstrate that YoeB is a cell wall-associated protein with weak sequence similarity to a noncatalytic domain of class B penicillin-binding proteins. A yoeB-null mutant exhibits an increased rate of autolysis in response to cell wall-targeting antibiotics or nutrient depletion. This phenotype does not appear to be correlated with gross alterations in peptidoglycan structure or levels of autolysins. Promoter dissection experiments define a minimal region necessary for antibiotic-mediated induction of yoeB, and this region is highly conserved preceding yoeB homologs in close relatives of B. subtilis. These results support a model in which induction of YoeB in response to cell envelope stress decreases the activity of autolysins and thereby reduces the rate of antibiotic-dependent cell death.

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