Cell Wall Lytic Enzymes And Their Role In Bacteriophages Infection

Use of chemical pesticides has been shown to have many negative side effects, such as insecticide resistance and resurgence, an outbreak of secondary pests and diseases, the disappearance of parasitoid and predator species as well as residual effects on food crops and on the environment. Over the past 60 years, both the number of agricultural toxins in the environment and incidence rates of toxin-related diseases has increased dramatically. The most effective way to combat this problem is through the use of natural predators. One of the best examples of this is the use of host-specific bacteriophages to control bacterial diseases. The mechanism of infection is a very interesting one. To break through the bacterial cell wall the bacteriophages must produce a range of lytic enzymes. This review will examine and discuss studies of these site-specific cell wall lytic enzymes and their roles in the infection of bacteriophages.

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Searching for the Evolutionary Design of the Pneumococcal Cell Wall Lytic Enzymes

Bacterial Growth and Lysis ◽

10.1007/978-1-4757-9359-8_30 ◽

1993 ◽

pp. 253-259

Author(s):

Rubens López ◽

José L. García ◽

Eduardo Díaz ◽

Jesús M. Sanz ◽

José M. Sánchez-Puelles ◽

...

Keyword(s):

Cell Wall ◽

Evolutionary Design ◽

Lytic Enzymes ◽

Cell Wall Lytic Enzymes

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Structural analysis and biological significance of the cell wall lytic enzymes of Streptococcus pneumoniae and its bacteriophage

FEMS Microbiology Letters ◽

10.1016/0378-1097(92)90243-h ◽

1992 ◽

Vol 100 (1-3) ◽

pp. 439-447 ◽

Cited By ~ 1

Author(s):

R López

Keyword(s):

Cell Wall ◽

Streptococcus Pneumoniae ◽

Structural Analysis ◽

Biological Significance ◽

Lytic Enzymes ◽

Cell Wall Lytic Enzymes

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Roles of LysM and LytM domains in resuscitation-promoting factor (Rpf) activity and Rpf-mediated peptidoglycan cleavage and dormant spore reactivation

Journal of Biological Chemistry ◽

10.1074/jbc.ra120.013994 ◽

2020 ◽

Vol 295 (27) ◽

pp. 9171-9182 ◽

Cited By ~ 2

Author(s):

Danielle L. Sexton ◽

Francesca A. Herlihey ◽

Ashley S. Brott ◽

David A. Crisante ◽

Evan Shepherdson ◽

...

Keyword(s):

Cell Wall ◽

Spore Germination ◽

Lytic Enzymes ◽

Lytic Transglycosylases ◽

Signaling Function ◽

Dormant Spore ◽

The Subject ◽

Resuscitation Promoting Factors ◽

Insight Into ◽

Cell Wall Lytic Enzymes

Bacterial dormancy can take many forms, including formation of Bacillus endospores, Streptomyces exospores, and metabolically latent Mycobacterium cells. In the actinobacteria, including the streptomycetes and mycobacteria, the rapid resuscitation from a dormant state requires the activities of a family of cell-wall lytic enzymes called resuscitation-promoting factors (Rpfs). Whether Rpf activity promotes resuscitation by generating peptidoglycan fragments (muropeptides) that function as signaling molecules for spore germination or by simply remodeling the dormant cell wall has been the subject of much debate. Here, to address this question, we used mutagenesis and peptidoglycan binding and cleavage assays to first gain broader insight into the biochemical function of diverse Rpf enzymes. We show that their LysM and LytM domains enhance Rpf enzyme activity; their LytM domain and, in some cases their LysM domain, also promoted peptidoglycan binding. We further demonstrate that the Rpfs function as endo-acting lytic transglycosylases, cleaving within the peptidoglycan backbone. We also found that unlike in other systems, Rpf activity in the streptomycetes is not correlated with peptidoglycan-responsive Ser/Thr kinases for cell signaling, and the germination of rpf mutant strains could not be stimulated by the addition of known germinants. Collectively, these results suggest that in Streptomyces, Rpfs have a structural rather than signaling function during spore germination, and that in the actinobacteria, any signaling function associated with spore resuscitation requires the activity of additional yet to be identified enzymes.

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CWLy-SVM: A support vector machine-based tool for identifying cell wall lytic enzymes

Computational Biology and Chemistry ◽

10.1016/j.compbiolchem.2020.107304 ◽

2020 ◽

Vol 87 ◽

pp. 107304 ◽

Cited By ~ 5

Author(s):

Chaolu Meng ◽

Fei Guo ◽

Quan Zou

Keyword(s):

Support Vector Machine ◽

Cell Wall ◽

Support Vector ◽

Lytic Enzymes ◽

Cell Wall Lytic Enzymes

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Lysis ofPediococcusandBrevibacteriumCells by Cell-Wall Lytic Enzymes, L3, L11, ALE and Lysozyme

Agricultural and Biological Chemistry ◽

10.1080/00021369.1966.10858739 ◽

1966 ◽

Vol 30 (11) ◽

pp. 1097-1101

Author(s):

Kenji Sakaguchi ◽

Shozo Kotani ◽

Hidekazu Suginaka ◽

Yoshiyuki Hirachi ◽

Shuzo Kashiba ◽

...

Keyword(s):

Cell Wall ◽

Lytic Enzymes ◽

Cell Wall Lytic Enzymes

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Random Mutagenesis Identifies Novel Genes Involved in the Secretion of Antimicrobial, Cell Wall-Lytic Enzymes by Lactococcus lactis

Applied and Environmental Microbiology ◽

10.1128/aem.00767-08 ◽

2008 ◽

Vol 74 (24) ◽

pp. 7490-7496 ◽

Cited By ~ 4

Author(s):

Yu Pei Tan ◽

Philip M. Giffard ◽

Daniel G. Barry ◽

Wilhelmina M. Huston ◽

Mark S. Turner

Keyword(s):

Cell Wall ◽

Lactococcus Lactis ◽

Transmembrane Protein ◽

Random Mutagenesis ◽

Lytic Enzyme ◽

Control Strain ◽

Lytic Enzymes ◽

Positive Bacterium ◽

Peptidoglycan Biosynthesis ◽

Cell Wall Lytic Enzymes

ABSTRACT Lactococcus lactis is a gram-positive bacterium that is widely used in the food industry and is therefore desirable as a candidate for the production and secretion of recombinant proteins. Previously, we generated a L. lactis strain that expressed and secreted the antimicrobial cell wall-lytic enzyme lysostaphin. To identify lactococcal gene products that affect the production of lysostaphin, we isolated and characterized mutants generated by random transposon mutagenesis that had altered lysostaphin activity. Out of 35,000 mutants screened, only one with no lysostaphin activity was identified, and it was found to contain an insertion in the lysostaphin expression cassette. Ten mutants with higher lysostaphin activity contained insertions in only four different genes, which encode an uncharacterized putative transmembrane protein (llmg_0609) (three mutants), an enzyme catalyzing the first step in peptidoglycan biosynthesis (murA2) (five mutants), a putative regulator of peptidoglycan modification (trmA) (one mutant), and an uncharacterized enzyme possibly involved in ubiquinone biosynthesis (llmg_2148) (one mutant). These mutants were found to secrete larger amounts of lysostaphin than the control strain (MG1363[lss]), and the greatest increase in secretion was 9.8- to 16.1-fold, for the llmg_0609 mutants. The lysostaphin-oversecreting llmg_0609, murA2, and trmA mutants were also found to secrete larger amounts of another cell wall-lytic enzyme (the Listeria monocytogenes bacteriophage endolysin Ply511) than the control strain, indicating that the phenotype is not limited to lysostaphin.

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