Journal of Microbiology

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Molecular mechanism of Escherichia coli H10407 induced diarrhoea and its control through immunomodulatory action of bioactives from Simarouba amara (Aubl.): Hegde Veena , Sandesh K. Gowda , Rajeshwara N. Achur , Nayaka Boramuthi Thippeswamy; J. Microbiol. 2021;59(4):435-447. Published online February 25, 2021; DOI: https://doi.org/10.1007/s12275-021-0423-2

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Enterotoxigenic Escherichia coli (ETEC) infection is a major cause of death in children under the age of five in developing countries. ETEC (O78:H11:CFA/I:LT+:ST+) mechanism has been studied in detail with either heat labile (LT) or heat stable (ST) toxins using in vitro and in vivo models. However, there is no adequate information on ETEC pathogenesis producing both the toxins (LT, ST) in BALB/c mice model. In this study, female mice have been employed to understand ETEC H10407 infection induced changes in physiology, biochemical and immunological patterns up to seven days post-infection and the antidiarrhoeal effect of Simarouba amara (Aubl.) bark aqueous extract (SAAE) has also been looked into. The results indicate that BALB/c is sensitive to ETEC infection resulting in altered jejunum and ileum histomorphology. Withal, ETEC influenced cAMP, PGE2, and NO production resulting in fluid accumulation with varied Na+, K+, Cl-, and Ca2+ levels. Meanwhile, ETEC subverted expression of IL-1β, intestine alkaline phosphatase (IAP), and myeloperoxidase (MPO) in jejunum and ileum. Our data also indicate the severity of pathogenesis reduction which might be due to attainment of equilibrium after reaching optimum rate of infection. Nevertheless, degree of pathogenesis was highly significant (p < 0.01) in all the studied parameters. Besides that, SAAE was successful in reducing the infectious diarrhoea by inhibiting ETEC H10407 in intestine (jejunum and ileum), and shedding in feces. SAAE decreased cAMP, PGE2, and fluid accumulation effectively and boosted the functional activity of immune system in jejunum and ileum IAP, MPO, IL-1β, and nitric oxide.

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Relaxed Cleavage Specificity of Hyperactive Variants of Escherichia coli RNase E on RNA I
Dayeong Bae, Hana Hyeon, Eunkyoung Shin, Ji-Hyun Yeom, Kangseok Lee
Journal of Microbiology.2023; 61(2): 211. CrossRef
A systematic antidiarrhoeal evaluation of a vegetable root Begonia roxburghii and its marker flavonoids against nonpathogenic and pathogenic diarrhoea
Rupali S. Prasad, Nikhil Y. Yenorkar, Suhas R. Dhaswadikar, Saurabh K. Sinha, Nitish Rai, Pravesh Sharma, Onkar Kulkarni, Neeraj Kumar, Mahaveer Dhobi, Damiki Laloo, Shailendra S. Gurav, Prakash R. Itankar, Satyendra K. Prasad
Food Bioscience.2023; 53: 102672. CrossRef

Leucobacter coleopterorum sp. nov., Leucobacter insecticola sp. nov., and Leucobacter viscericola sp. nov., isolated from the intestine of the diving beetles, Cybister brevis and Cybister lewisianus, and emended description of the genus Leucobacter: Dong-Wook Hyun , Hojun Sung , Pil Soo Kim , Ji-Hyun Yun , Jin-Woo Bae; J. Microbiol. 2021;59(4):360-368. Published online January 26, 2021; DOI: https://doi.org/10.1007/s12275-021-0472-6

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Abstract

Three novel bacterial strains, HDW9AT, HDW9BT, and HDW9CT, isolated from the intestine of the diving beetles Cybister lewisianus and Cybister brevis, were characterized as three novel species using a polyphasic approach. The isolates were Gram-staining-positive, strictly aerobic, non-motile, and rod-shaped. They grew optimally at 30°C (pH 7) in the presence of 0.5% (wt/vol) NaCl. Phylogenetic analysis based on the 16S rRNA gene sequences revealed that they belong to the genus Leucobacter and are closely related to L. denitrificans M1T8B10T (98.4–98.7% sequence similarity). Average nucleotide identity (ANI) values among the isolates were 76.4–84.1%. ANI values for the isolates and the closest taxonomic species, L. denitrificans KACC 14055T, were 72.3–73.1%. The isolates showed ANI values of < 76.5% with all analyzable Leucobacter strains in the EzBioCloud database. The genomic DNA G + C content of the isolates was 60.3–62.5%. The polar lipid components were phosphatidylglycerol, diphosphatidylglycerol, and other unidentified glycolipids, phospholipids, and lipids. The major cellular fatty acids were anteiso- C15:0, iso-C16:0, and anteiso-C17:0. MK-10 was the major respiratory quinone, and MK-7 and MK-11 were the minor respiratory quinones. The whole-cell sugar components of the isolates were ribose, glucose, galactose, and mannose. The isolates harbored L-2,4-diaminobutyric acid, L-serine, L-lysine, L-aspartic acid, glycine, and D-glutamic acid within the cell wall peptidoglycan. Based on phylogenetic, phenotypic, chemotaxonomic, and genotypic analyses, strains HDW9AT, HDW9BT, and HDW9CT represent three novel species within the genus Leucobacter. We propose the name Leucobacter coleopterorum sp. nov. for strain HDW9AT (= KACC 21331T = KCTC 49317T = JCM 33667T), the name Leucobacter insecticola sp. nov. for strain HDW9BT (= KACC 21332T = KCTC 49318T = JCM 33668T), and the name Leucobacter viscericola sp. nov. for strain HDW9CT (= KACC 21333T = KCTC 49319T = JCM 33669T).

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Biogenic Silver Nanoparticles Produced by Soil Rare Actinomycetes and Their Significant Effect on Aspergillus-derived mycotoxins
Mohamed N. Abd El-Ghany, Salwa A. Hamdi, Shereen M. Korany, Reham M. Elbaz, Ahmed N. Emam, Mohamed G. Farahat
Microorganisms.2023; 11(4): 1006. CrossRef
Leucobacter tenebrionis sp. nov., isolated from the gut of Tenebrio molitor
Yu Ying, Bo Yuan, Tingting Liu, Xiaoshuan Bai, Haifeng Zhao
International Journal of Systematic and Evolutionary Microbiology .2023;[Epub] CrossRef
Leucobacter allii sp. nov. and Leucobacter rhizosphaerae sp. nov., isolated from rhizospheres of onion and garlic, respectively
Seunghwan Kim, Tomomi Asano, Hanako Naito, Moriyuki Hamada, Hang-Yeon Weon, Soon-Wo Kwon, Jun Heo
International Journal of Systematic and Evolutionary Microbiology .2023;[Epub] CrossRef
Leucobacter chinensis sp. nov., with plant growth-promoting potential isolated from field soil after seven-years continuous maize cropping
Jie Zhu, Juan Che, Xin Jiang, Mingchao Ma, Dawei Guan, Li Li, Fengming Cao, Baisuo Zhao, Yaowei Kang, Ji Zhao, Delong Kong, Yiqing Zhou, Zhiyong Ruan, Jun Li
International Journal of Systematic and Evolutionary Microbiology .2022;[Epub] CrossRef
Changes of gut microbiota in colorectal cancer patients with Pentatrichomonas hominis infection
Hongbo Zhang, Yanhui Yu, Jianhua Li, Pengtao Gong, Xiaocen Wang, Xin Li, Yidan Cheng, Xiuyan Yu, Nan Zhang, Xichen Zhang
Frontiers in Cellular and Infection Microbiology.2022;[Epub] CrossRef
Lysobacter ciconiae sp. nov., and Lysobacter avium sp. nov., isolated from the faeces of an Oriental stork
So-Yeon Lee, Pil Soo Kim, Hojun Sung, Dong-Wook Hyun, Jin-Woo Bae
Journal of Microbiology.2022; 60(5): 469. CrossRef
Valid publication of new names and new combinations effectively published outside the IJSEM. Validation List no. 203
Aharon Oren, George M. Garrity
International Journal of Systematic and Evolutionary Microbiology .2022;[Epub] CrossRef
Leucobacter soli sp. nov., from soil amended with humic acid
Peter Kämpfer, John A. McInroy, Dominique Clermont, Meina Neumann-Schaal, Alexis Criscuolo, Hans-Jürgen Busse, Stefanie P. Glaeser
International Journal of Systematic and Evolutionary Microbiology .2021;[Epub] CrossRef
Fate of Functional Bacterial and Eukaryotic Community Regulated by Earthworms during Vermicomposting of Dewatered Sludge, Studies Based on the 16S rDNA and 18S rDNA Sequencing of Active Cells
Jun Yang, Kui Huang, Lansheng Peng, Jianhui Li, Aozhan Liu
International Journal of Environmental Research and Public Health.2021; 18(18): 9713. CrossRef

The antibacterial activity of E. coli bacteriophage lysin lysep3 is enhanced by fusing the Bacillus amyloliquefaciens bacteriophage endolysin binding domain D8 to the C-terminal region: Shuang Wang , Jingmin Gu , Meng Lv , Zhimin Guo , Guangmou Yan , Ling Yu , Chongtao Du , Xin Feng , Wenyu Han , Changjiang Sun , Liancheng Lei; J. Microbiol. 2017;55(5):403-408. Published online January 26, 2017; DOI: https://doi.org/10.1007/s12275-017-6431-6

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Abstract

Bacteriophage endolysin is one of the most promising anti-biotic substitutes, but in Gram-negative bacteria, the outer membrane prevents the lysin from hydrolyzing peptidogly-cans and blocks the development of lysin applications. The prime strategy for new antibiotic substitutes is allowing lysin to access the peptidoglycan from outside of the bacteria by reformation of the lysin. In this study, the novel Escherichia coli (E. coli) phage lyase lysep3, which lacks outside-in cata-lytic ability, was fused with the N-terminal region of the Bacillus amyloliquefaciens lysin including its cell wall bind-ing domain D8 through the best manner of protein fusion based on the predicted tertiary structure of lysep3-D8 to ob-tain an engineered lysin that can lyse bacteria from the out-side. Our results showed that lysep3-D8 could lyse both Gram- negative and Gram-positive bacteria, whereas lysep3 and D8 have no impact on bacterial growth. The MIC of lysep3-D8 on E. coli CVCC1418 is 60 μg/ml; lysep3-D8 can inhibit the growth of bacteria up to 12 h at this concentration. The bac-tericidal spectrum of lysep3-D8 is broad, as it can lyse of all of 14 E. coli strains, 3 P. aeruginosa strains, 1 Acinetobacter baumannii strain, and 1 Streptococcus strain. Lysep3-D8 has sufficient bactericidal effects on the 14 E. coli strains tested at the concentration of 100 μg/ml. The cell wall binding do-main of the engineered lysin can destroy the integrity of the outer membrane of bacteria, thus allowing the catalytic do-main to reach its target, peptidoglycan, to lyse the bacteria. Lysep3-D8 can be used as a preservative in fodder to benefit the health of animals. The method we used here proved to be a successful exploration of the reformation of phage lysin.

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New-Generation Antibacterial Agent—Cellulose-Binding Thermostable TP84_Endolysin
Małgorzata Ponikowska, Joanna Żebrowska, Piotr M. Skowron
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Characterization of Pseudomonas aeruginosa bacteriophages and control hemorrhagic pneumonia on a mice model
Yanjie Zhang, Ruiqing Wang, Qingxia Hu, Ni Lv, Likun Zhang, Zengqi Yang, Yefei Zhou, Xinglong Wang
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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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Abstract: 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.

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