Journal of Microbiology

Journal Article

The assessment of host and bacterial proteins in sputum from active pulmonary tuberculosis: Hsin-Chih Lai , Yu-Tze Horng , Pen-Fang Yeh , Jann-Yuan Wang , Chin-Chung Shu , Jang-Jih Lu , Jen-Jyh Lee , Po-Chi Soo; J. Microbiol. 2016;54(11):761-767. Published online October 29, 2016; DOI: https://doi.org/10.1007/s12275-016-6201-x

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Pulmonary tuberculosis (TB) is caused by Mycobacterium tuberculosis. The protein composition of sputum may reflect the immune status of the lung. This study aimed to evaluate the protein profiles in spontaneous sputum samples from patients with active pulmonary TB. Sputum samples were collected from patients with pulmonary TB and healthy controls. Western blotting was used to analyze the amount of interleukin 10 (IL-10), interferon-gamma (IFN-γ), IL-25, IL- 17, perforin-1, urease, albumin, transferrin, lactoferrin, adenosine deaminase (also known as adenosine aminohydrolase, or ADA), ADA-2, granzyme B, granulysin, and caspase- 1 in sputum. Results of detection of IL-10, IFN-γ, perforin- 1, urease, ADA2, and caspase-1, showed relatively high specificity in distinguishing patients with TB from healthy controls, although sensitivities varied from 13.3% to 66.1%. By defining a positive result as the detection of any two proteins in sputum samples, combined use of transferrin and urease as markers increased sensitivity to 73.2% and specificity to 71.1%. Furthermore, we observed that the concentration of transferrin was proportional to the number of acidfast bacilli detected in sputum specimens. Detection of sputum transferrin and urease was highly associated with pulmonary TB infection. In addition, a high concentration of transferrin detected in sputum might correlate with active TB infection. This data on sputum proteins in patients with TB may aid in the development of biomarkers to assess the severity of pulmonary TB.

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From simple to complex: Protein‐based biomarker discovery in tuberculosis
Zaynab Mousavian, Gunilla Källenius, Christopher Sundling
European Journal of Immunology.2023;[Epub] CrossRef
Interleukin 8 and Pentaxin (C-Reactive Protein) as Potential New Biomarkers of Bovine Tuberculosis
Xintao Gao, Xiaoyu Guo, Ming Li, Hong Jia, Weidong Lin, Lichun Fang, Yitong Jiang, Hongfei Zhu, Zhifang Zhang, Jiabo Ding, Ting Xin, Brad Fenwick
Journal of Clinical Microbiology.2019;[Epub] CrossRef

Research Support, Non-U.S. Gov't

Morphological changes in human gastric epithelial cells induced by nuclear targeting of Helicobacter pylori urease subunit A: Jung Hwa Lee , So Hyun Jun , Jung-Min Kim , Seung Chul Baik , Je Chul Lee; J. Microbiol. 2015;53(6):406-414. Published online May 30, 2015; DOI: https://doi.org/10.1007/s12275-015-5085-5

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Abstract

Nuclear targeting of bacterial proteins and their pathological effects on host cells are an emerging pathogenic mechanism in bacteria. We have previously reported that urease subunit A (UreA) of Helicobacter pylori targets the nuclei of COS-7 cells through nuclear localization signals (NLSs). This study further investigated whether UreA of H. pylori targets the nuclei of gastric epithelial cells and then induces molecular and cellular changes in the host cells. H. pylori 26695 strain produced and secreted outer membrane vesicles (OMVs). UreA was translocated into gastric epithelial AGS cells through outer membrane vesicles (OMVs) and then targeted the nuclei of AGS cells. Nuclear targeting of rUreA did not induce host cell death, but resulted in morphological changes, such as cellular elongation, in AGS cells. In contrast, AGS cells treated with rUreAΔNLS proteins did not show this morphological change. Next generation sequencing revealed that nuclear targeting of UreA differentially regulated 102 morphogenesis- related genes, of which 67 and 35 were up-regulated and down-regulated, respectively. Our results suggest that nuclear targeting of H. pylori UreA induces both molecular and cellular changes in gastric epithelial cells.

Citations

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Effects of Exosomes Derived From Helicobacter pylori Outer Membrane Vesicle-Infected Hepatocytes on Hepatic Stellate Cell Activation and Liver Fibrosis Induction
Masoumeh Ebadi Zahmatkesh, Mariyeh Jahanbakhsh, Negin Hoseini, Saina Shegefti, Amir Peymani, Hossein Dabin, Rasoul Samimi, Shahin Bolori
Frontiers in Cellular and Infection Microbiology.2022;[Epub] CrossRef
Significance of Helicobacter pylori and Its Serological Typing in Gastric Cancer
碧玉张
Advances in Clinical Medicine.2022; 12(12): 11694. CrossRef
Rational Development of Bacterial Ureases Inhibitors
Saurabh Loharch, Łukasz Berlicki
The Chemical Record.2022;[Epub] CrossRef
Emerging therapeutic targets for gastric cancer from a host-Helicobacter pylori interaction perspective
Esmat Abdi, Saeid Latifi-Navid, Fatemeh Abedi Sarvestani, Mohammad Hassan Esmailnejad
Expert Opinion on Therapeutic Targets.2021; 25(8): 685. CrossRef
Non-enzymatic properties of Proteus mirabilis urease subunits
Valquiria Broll, Ana Paula A. Perin, Fernanda C. Lopes, Anne Helene S. Martinelli, Natalia R. Moyetta, Leonardo L. Fruttero, Matheus V.C. Grahl, Augusto F. Uberti, Diogo R. Demartini, Rodrigo Ligabue-Braun, Celia R. Carlini
Process Biochemistry.2021; 110: 263. CrossRef
Nuclear trafficking of bacterial effector proteins
Lena Hoang My Le, Le Ying, Richard L. Ferrero
Cellular Microbiology.2021;[Epub] CrossRef
Proteus mirabilis Urease: Unsuspected Non-Enzymatic Properties Relevant to Pathogenicity
Matheus V. C. Grahl, Augusto F. Uberti, Valquiria Broll, Paula Bacaicoa-Caruso, Evelin F. Meirelles, Celia R. Carlini
International Journal of Molecular Sciences.2021; 22(13): 7205. CrossRef
Helicobacter pylori Outer Membrane Vesicles and Extracellular Vesicles from Helicobacter pylori-Infected Cells in Gastric Disease Development
María Fernanda González, Paula Díaz, Alejandra Sandoval-Bórquez, Daniela Herrera, Andrew F. G. Quest
International Journal of Molecular Sciences.2021; 22(9): 4823. CrossRef
Tracking the cargo of extracellular symbionts into host tissues with correlated electron microscopy and nanoscale secondary ion mass spectrometry imaging
Stephanie K. Cohen, Marie‐Stéphanie Aschtgen, Jonathan B. Lynch, Sabrina Koehler, Fangmin Chen, Stéphane Escrig, Jean Daraspe, Edward G. Ruby, Anders Meibom, Margaret McFall‐Ngai
Cellular Microbiology.2020;[Epub] CrossRef
Role of Probiotics in Prophylaxis of Helicobacter pylori Infection
Kashyapi Chakravarty, Smriti Gaur
Current Pharmaceutical Biotechnology.2019; 20(2): 137. CrossRef
Helicobacter pylori: molecular basis for colonization and survival in gastric environment and resistance to antibiotics. A short review
Sharmila Fagoonee, Rinaldo Pellicano
Infectious Diseases.2019; 51(6): 399. CrossRef
Cross‐Reactivity of Polyclonal Antibodies against Canavalia ensiformis (Jack Bean) Urease and Helicobacter pylori Urease Subunit A Fragments
Zbigniew Jerzy Kaminski, Inga Relich, Iwona Konieczna, Wieslaw Kaca, Beata Kolesinska
Chemistry & Biodiversity.2018;[Epub] CrossRef
Ureases: Historical aspects, catalytic, and non-catalytic properties – A review
Karine Kappaun, Angela Regina Piovesan, Celia Regina Carlini, Rodrigo Ligabue-Braun
Journal of Advanced Research.2018; 13: 3. CrossRef
The Impact of Helicobacter pylori Urease upon Platelets and Consequent Contributions to Inflammation
Adriele Scopel-Guerra, Deiber Olivera-Severo, Fernanda Staniscuaski, Augusto F. Uberti, Natália Callai-Silva, Natália Jaeger, Bárbara N. Porto, Celia R. Carlini
Frontiers in Microbiology.2017;[Epub] CrossRef
A New Role for Helicobacter pylori Urease: Contributions to Angiogenesis
Deiber Olivera-Severo, Augusto F. Uberti, Miguel S. Marques, Marta T. Pinto, Maria Gomez-Lazaro, Céu Figueiredo, Marina Leite, Célia R. Carlini
Frontiers in Microbiology.2017;[Epub] CrossRef

Journal Article

Use of Selected Lactic Acid Bacteria in the Eradication of Helicobacter pylori Infection: Jin-Eung Kim , Min-Soo Kim , Yeo-Sang Yoon , Myung-Jun Chung , Do-Young Yum; J. Microbiol. 2014;52(11):955-962. Published online October 3, 2014; DOI: https://doi.org/10.1007/s12275-014-4355-y

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Abstract

Helicobacter pylori is among the major pathogenic bacteria that cause chronic gastritis and peptic ulcer disease and is related to the development of gastric cancer. Several chemicals, including antibiotics, have been used to eradicate H. pylori; however, they do not always curb the infection. Ten representative type strains of lactic acid bacteria (LAB) were screened for antagonism toward H. pylori via inhibition of urease activity. Strains inhibiting the binding of H. pylori to human gastric cell line cells and suppressing H. pylori-induced interleukin-8 (IL-8) production were also screened. Of these, Pediococcus pentosaseus (SL4), which inhibited the adhesion of H. pylori to MKN-45 gastric cancer cells, Bifidobacterium longum (BG7), with urease inhibiting activity, and Lactococcus lactis (SL3), and Enterococcus faecalis (SL5), which suppressed H. pylori-induced IL-8 production within MKN-45 and AGS cells, were selected. In mouse model, these LAB stains in combination significantly suppressed IL-8 levels in serum. Gastric pH also recovered to normal values after the administration of these LAB. These stains effectively suppressed H. pylori viability, although not to the extent of antibiotic treatment. When used as probiotics, LAB may help decrease the occurrence of gastritis and reduce the risk of H. pylori infection without, inducing side effects.

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Jiahui Xi, Yonghong Li, Hui Zhang, Zhongtian Bai
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Sanjeev Kumar, Md Faruque Ahmad, Priyakshi Nath, Rubina Roy, Rudrarup Bhattacharjee, Eman Shama, Indira Gahatraj, Manisha Sehrawat, Vaishali Dasriya, Harmeet Singh Dhillon, Monica Puniya, Mrinal Samtiya, Tejpal Dhewa, Rotimi E. Aluko, Gulab D. Khedkar, An
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Lactiplantibacillus plantarum ZJ316 Reduces Helicobacter pylori Adhesion and Inflammation by Inhibiting the Expression of Adhesin and Urease Genes
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FERMENTE GIDALARIN İNSAN SAĞLIĞI ÜZERİNDEKİ ETKİLERİ
Büşra AKDENİZ OKTAY, Z. Yeşim ÖZBAŞ
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Research Support, Non-U.S. Gov'ts

Protection Against Helicobacter pylori Infection by a Trivalent Fusion Vaccine Based on a Fragment of Urease B-UreB414: Li Wang Wang , Xiao-Fei Liu , Shi Yun , Xiao-Peng Yuan , Xu-Hu Mao , Chao Wu , Wei-Jun Zhang , Kai-Yun Liu , Gang Guo , Dong-Shui Lu , Wen-De Tong , Ai-Dong Wen , Quan-Ming Zou; J. Microbiol. 2010;48(2):223-228. Published online May 1, 2010; DOI: https://doi.org/10.1007/s12275-009-0233-4

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Abstract: A multivalent fusion vaccine is a promising option for protection against Helicobacter pylori infection. In this study, UreB414 was identified as an antigenic fragment of urease B subunit (UreB) and it induced an antibody inhibiting urease activity. Immunization with UreB414 partially protected mice from H. pylori infection. Furthermore, a trivalent fusion vaccine was constructed by genetically linking heat shock protein A (HspA), H. pylori adhesin A (HpaA), and UreB414, resulting in recombinant HspA-HpaA-UreB414 (rHHU). Its protective effect against H. pylori infection was tested in BALB/c mice. Oral administration of rHHU significantly protected mice from H. pylori infection, which was associated with H. pylori-specific antibody production and Th1/Th2-type immune responses. The results show that a trivalent fusion vaccine efficiently combats H. pylori infection, and that an antigenic fragment of the protein can be used instead of the whole protein to construct a multivalent vaccine.

Phylogeny of a Novel “Helicobacter heilmannii” Organism from a Japanese Patient with Chronic Gastritis Based on DNA Sequence Analysis of 16S rRNA and Urease Genes: Takehisa Matsumoto , Masatomo Kawakubo , Mayumi Shiohara , Toshiko Kumagai , Eiko Hidaka , Kazuyoshi Yamauchi , Kozue Oana , Kenji Matsuzawa , Hiroyoshi Ota , Yoshiyuki Kawakami; J. Microbiol. 2009;47(2):201-207. Published online May 2, 2009; DOI: https://doi.org/10.1007/s12275-008-0313-x

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Abstract: “Helicobacter heilmannii” is an uncultivable spiral-shaped bacterium inhabiting the human gastric mucosa. It is larger and more tightly-coiled than H. pylori. We encountered a patient with chronic gastritis infected a “H. heilmannii”-like organism (HHLO), designated as SH6. Gastric mucosa derived from the patient was orally ingested by specific pathogen free mice. Colonization of the mice by SH6 was confirmed by electron microscopy of gastric tissue specimens. In an attempt to characterize SH6, 16S rRNA and urease genes were sequenced. The 16S rRNA gene sequence was most similar (99.4%; 1,437/1,445 bp) to HHLO C4E from a cheetah. However, the urease gene sequence displayed low similarity (81.7%; 1,240/1,516 bp) with HHLO C4E. Taxonomic analysis disclosed that SH6 represents a novel strain and should constitute a novel taxon in the phylogenetic trees, being discriminated from any other taxon, with the ability of infecting human gastric mucosa.

Characteristics of Urease from Vibrio parahaemolyticus Possessing tdh and trh Genes Isolated in Korea: Young Hee Kim , Jong Sook Kim; J. Microbiol. 2001;39(4):279-285.

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Abstract: Vibrio parahaemolyticus is a halophilic bacterium associated with seafood gastroenteritis. An unusual strain of Kanagawa-positive urease producing Vibrio parahaemolyticus O1 : K1 was isolated from the environment and identified. A polymerase chain reaction assay revealed that this strain harbored both the tdh and trh genes. The urease from this strain was studied. Maximum urease production was induced in LB medium containing 0.2% urea, 0.5% glucose, 2% NaCl and pH 5.5 with 6 h of cultivation at 37 C under aeration. Purification of urease was achieved by the process of whole cell lysate, 65% ammonium sulphate precipitation, DEAE-cellulose ion exchange column chromatography, Sepharose CL-6B gel filtration and oxirane activated Sepharose 6B-urea affinity chromatography with 203 fold purification and 2.2% yield. Analysis of the purified enzyme by SDS-PAGE demonstrated the presence of the subunits with a molecular weight of 85 kDa, 59 kDa, 41 kDa and the molecular weight for the native enzyme by nondenaturing PAGE and gel filtration chromatography was 255 kDa. The purified urease was stable at pH 7.5 and the optimal pH in HEPES buffer was 8.0. The enzyme was stable at 60 C for 2 h with a residual activity of 32%. The addition of 10 uM of NiCl_2 maintained stability for 30 min. The Km value of the purified enzyme was 35.6 mM in urea substrate. The TD_50 (median toxic dose) of the purified urease was 2.5 ug/ml on human leukemia cells.

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