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Genetic insights into novel lysis suppression by phage CSP1 in Escherichia coli
Moosung Kim, Sangryeol Ryu
J. Microbiol. 2025;63(4):e2501013.   Published online April 29, 2025
DOI: https://doi.org/10.71150/jm.2501013
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AbstractAbstract PDFSupplementary Material

Lysis inhibition (LIN) in bacteriophage is a strategy to maximize progeny production. A clear plaque-forming mutant, CSP1C, was isolated from the turbid plaque-forming CSP1 phage. CSP1C exhibited an adsorption rate and replication dynamics similar to CSP1. Approximately 90% of the phages were adsorbed to the host cell within 12 min, and both phages had a latent period of 25 min. Burst sizes were 171.42 ± 31.75 plaque-forming units (PFU) per infected cell for CSP1 and 168.94 ± 51.67 PFU per infected cell for CSP1C. Both phages caused comparable reductions in viable E. coli cell counts at a low multiplicity of infection (MOI). However, CSP1 infection did not reduce turbidity, suggesting a form of LIN distinct from the well-characterized LIN of T4 phage. Genomic analysis revealed that a 4,672-base pairs (bp) DNA region, encompassing part of the tail fiber gene, CSP1_020, along with three hypothetical genes, CSP1_021, CSP1_022, and part of CSP1_023, was deleted from CSP1 to make CSP1C. Complementation analysis in CSP1C identified CSP1_020, CSP1_021, and CSP1_022 as a minimal gene set required for the lysis suppression in CSP1. Co-expression of these genes in E. coli with holin (CSP1_092) and endolysin (CSP1_091) resulted in lysis suppression. Lysis suppression was abolished by disrupting the proton motive force (PMF), supporting their potential role as antiholin. Additionally, CSP1_021 directly interacts with holin, suggesting that it may function as an antiholin. These findings identify new genetic factors involved in lysis suppression in CSP1, providing broader insights into phage strategies for modulating host cell lysis.

Journal Article
Identification of a novel phospholipase D gene and effects of carbon sources on its expression in Bacillus cereus ZY12
Yu Zhao , Yinfeng Xu , Fang Yu , Chunzhi Zhang
J. Microbiol. 2018;56(4):264-271.   Published online April 2, 2018
DOI: https://doi.org/10.1007/s12275-018-7529-1
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  • 4 Crossref
AbstractAbstract
In the present study, a new strain, Bacillus cereus ZY12, producing phospholipase D (PLD) was identified. The expression of PLD in this strain was found to be induced by its substrate, phosphatidylcholine (PC), and completely silenced by other carbon sources, such as glucose, fructose, and maltose, which are generally used in microbial growth cultures, thus presenting a unique expression pattern different from other PLD-producing microorganisms. This study is the first to report on the ability of B. cereus to produce PLD, and successfully clone its PLD-coding gene and identify its function, extending the knowledge on PLD distribution and evolution in microorganisms.

Citations

Citations to this article as recorded by  
  • Efficient Extracellular Production of Phospholipase D in Escherichia coli via Genetic and Process Engineering Modification
    Huan Liu, Yang Yang, Tianyi Wang, Yuchen Ning, Li Deng, Fang Wang
    Synthetic Biology and Engineering.2025; 3(2): 10006.     CrossRef
  • Structural insights into PA3488-mediated inactivation of Pseudomonas aeruginosa PldA
    Xiaoyun Yang, Zongqiang Li, Liang Zhao, Zhun She, Zengqiang Gao, Sen-Fang Sui, Yuhui Dong, Yanhua Li
    Nature Communications.2022;[Epub]     CrossRef
  • Construction of a Super-Folder Fluorescent Protein-Guided Secretory Expression System for the Production of Phospholipase D in Bacillus subtilis
    Haiyang Zhang, Xuehan Li, Qi Liu, Jianan Sun, Francesco Secundo, Xiangzhao Mao
    Journal of Agricultural and Food Chemistry.2021; 69(24): 6842.     CrossRef
  • Microbial phospholipase D: Identification, modification and application
    Zhenxia Zhang, Ming Chen, Wei Xu, Wenli Zhang, Tao Zhang, Cuie Guang, Wanmeng Mu
    Trends in Food Science & Technology.2020; 96: 145.     CrossRef
Review
REVIEW] Phage Lysis: Three Steps, Three Choices, One Outcome
Ryl Young
J. Microbiol. 2014;52(3):243-258.   Published online March 1, 2014
DOI: https://doi.org/10.1007/s12275-014-4087-z
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  • 284 Scopus
AbstractAbstract
The lysis of bacterial hosts by double-strand DNA bacteriophages, once thought to reflect merely the accumulation of sufficient lysozyme activity during the infection cycle, has been revealed to recently been revealed to be a carefully regulated and temporally scheduled process. For phages of Gramnegative hosts, there are three steps, corresponding to subversion of each of the three layers of the cell envelope: inner membrane, peptidoglycan, and outer membrane. The pathway is controlled at the level of the cytoplasmic membrane. In canonical lysis, a phage encoded protein, the holin, accumulates harmlessly in the cytoplasmic membrane until triggering at an allele-specific time to form micron-scale holes. This allows the soluble endolysin to escape from the cytoplasm to degrade the peptidoglycan. Recently a parallel pathway has been elucidated in which a different type of holin, the pinholin, which, instead of triggering to form large holes, triggers to form small, heptameric channels that serve to depolarize the membrane. Pinholins are associated with SAR endolysins, which accumulate in the periplasm as inactive, membrane-tethered enzymes. Pinholin triggering collapses the proton motive force, allowing the SAR endolysins to refold to an active form and attack the peptidoglycan. Surprisingly, a third step, the disruption of the outer membrane is also required. This is usually achieved by a spanin complex, consisting of a small outer membrane lipoprotein and an integral cytoplasmic membrane protein, designated as o-spanin and i-spanin, respectively. Without spanin function, lysis is blocked and progeny virions are trapped in dead spherical cells, suggesting that the outer membrane has considerable tensile strength. In addition to two-component spanins, there are some single-component spanins, or u-spanins, that have an N-terminal outer-membrane lipoprotein signal and a C-terminal transmembrane domain. A possible mechanism for spanin function to disrupt the outer membrane is to catalyze fusion of the inner and outer membranes.
Journal Article
Effect of Mycelial Extract of Clavicorona pyxidata on Acetylcholinesterase and β-Secretase Activity in vitro
Tae-Hee Lee , Young-Il Park , Yeong-Hwan Han
J. Microbiol. 2006;44(5):502-507.
DOI: https://doi.org/2448 [pii]
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AbstractAbstract
In a previous study, an extract of Clavicorona pyxidata DGUM 29005 mycelia demonstrated an inhibitory effect against enzyme-associated perceptual disorders. We have attempted to determine whether this mycelial extract is also capable of inhibiting the activities of acetylcholinesterase (AChE) and β-secretase (BACE) activity. Butanol, ethanol, and water extracts of C. pyxidata DGUM 29005 mycelia were shown to inhibit AChE activity by 99.3%, 93.7%, and 91.7%, respectively. The inhibitory value of the butanol extract was more profound than that of tacrine (95.4%). The ethanol extract also exerted an inhibitory effect against BACE activity; this fraction may harbor the potential for development into a pharmocotherapeutic modality for the treatment of Alzheimer''s disease (AD) patients. Rat pheochromocytoma PC12 cells in culture were not determined to be susceptible to the cytotoxic activity evidenced by the mycelial extract. The ethanol extract inhibited endogenous AChE activity in PC12 cellular homogenates, with an IC50 of 67.5 μg/ml, after incubation with intact cells, and also inhibited BACE activity in a dose-dependent fashion. These results suggest that the C. pyxidata mycelial extract has the potential to enhance cholinergic function and, therefore, may perform a function in the amelioration of the cholinergic deficit observed in cases of AD, as well as other types of age-associated memory impairment.
Bioluminescent Assay of Phospholipase C Using A Luminescent Marine Mutant Bacterium Vibrio harveyi M-17
Ki Woong Cho , SangJun Mo , Hyi-Seung Lee , Jung-Rae Rho , Jongheon Shin
J. Microbiol. 2000;38(3):150-155.
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AbstractAbstract
A bioluminescent assay method for detecting the activity of phospholipase C (PLC; phosphatidyl choline cholinephosphohydrolase, EC 3.1.4.3) was developed using bioluminescent marine bacteria. Phospholipase C from Bacillus cereus and sn-1,2-dimyristoyl phosphatidyl choline (DMPC) as a substrate were used in the demonstration, and the produced sn-1,2-dimyristoyl glycerol was further hydrolyzed with lipase from Candida cylidracea. The hydrolyzed myristic acid was quantified using a dark mutant of Vibrio harveyi (designated as M-17). The in vivo light intensity of which was stimulated specifically up to one thousand fold in the presence of myristic acid. The rates of the hydrolysis of the DMPC substrate by the phospholipase measured by the luminescence method were linear with time and the amount of enzyme added. Activity measurement conditions (at 25 C, pH 6.5, 10 min fixed time assay) were established to detect as little as 0.1 mUnit of phospholipase C and 5 nM of myristic acid production.

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