- Screening of small molecules attenuating biofilm formation of Acinetobacter baumannii by inhibition of ompA promoter activity
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Seok Hyeon Na , Hyejin Jeon , Man Hwan Oh , Yoo Jeong Kim , Je Chul Lee
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J. Microbiol. 2021;59(9):871-878. Published online August 27, 2021
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DOI: https://doi.org/10.1007/s12275-021-1394-z
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77
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12
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12
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 Abstract
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Anti-virulence therapeutic strategies are promising alternatives
against drug-resistant pathogens. Outer membrane
protein A (OmpA) plays a versatile role in the pathogenesis
and antimicrobial resistance of Acinetobacter baumannii.
Therefore, OmpA is an innovative target for anti-virulence
therapy against A. baumannii. This study aimed to develop
a high-throughput screening (HTS) system to discover small
molecules inhibiting the ompA promoter activity of A. baumannii
and screen chemical compounds using the bacterial
growth-based HTS system. The ompA promoter and open
reading frame of nptI fusion plasmids that controlled the
expression of nptI encoding resistance to kanamycin by the
ompA promoter were constructed and then transformed into
A. baumannii ATCC 17978. This reporter strain was applied
to screen small molecules inhibiting the ompA promoter
activity in a chemical library. Of the 7,520 chemical compounds,
15 exhibited ≥ 70% growth inhibition of the report
strain cultured in media containing kanamycin. Three compounds
inhibited the expression of ompA and OmpA in the
outer membrane of A. baumannii ATCC 17978, which subsequently
reduced biofilm formation. In conclusion, our reporter
strain is useful for large-scale screening of small molecules
inhibiting the ompA expression in A. baumannii. Hit
compounds identified by the HTS system are promising scaffolds
to develop novel therapeutics against A. baumannii.
-
Citations
Citations to this article as recorded by  -
A peptide targeting outer membrane protein A of
Acinetobacter baumannii
exhibits antibacterial activity by reducing bacterial pathogenicity
Hui Zhao, Yue Hu, Dan Nie, Na Li, Zhou Chen, Shan Zhou, Mingkai Li, Xiaoyan Xue, James E. Leggett
Antimicrobial Agents and Chemotherapy.2024;[Epub] CrossRef - Acinetobacter baumannii OmpA-like porins: functional characterization of bacterial physiology, antibiotic-resistance, and virulence
Daniela Scribano, Elena Cheri, Arianna Pompilio, Giovanni Di Bonaventura, Manuel Belli, Mario Cristina, Luigi Sansone, Carlo Zagaglia, Meysam Sarshar, Anna Teresa Palamara, Cecilia Ambrosi
Communications Biology.2024;[Epub] CrossRef - Anti-OmpA antibodies as potential inhibitors of Acinetobacter baumannii biofilm formation, adherence to, and proliferation in A549 human alveolar epithelial cells
Hamideh Barati, Zahra Fekrirad, Mohammadreza Jalali Nadoushan, Iraj Rasooli
Microbial Pathogenesis.2024; 186: 106473. CrossRef -
Current and novel therapies for management of
Acinetobacter baumannii
-associated pneumonia
Aye Mya Sithu Shein, Parichart Hongsing, O’Rorke Kevin Smith, Phatthranit Phattharapornjaroen, Kazuhiko Miyanaga, Longzhu Cui, Hitoshi Ishikawa, Mohan Amarasiri, Peter N. Monk, Anthony Kicic, Tanittha Chatsuwan, Daniel Pletzer, Paul G. Higgins, Shuichi Ab
Critical Reviews in Microbiology.2024; : 1. CrossRef - Understanding the mechanisms of antimicrobial resistance and potential therapeutic approaches against the Gram-negative pathogen Acinetobacter baumannii
Vishwani Jamwal, Tashi Palmo, Kuljit Singh
RSC Medicinal Chemistry.2024; 15(12): 3925. CrossRef - Acinetobacter baumannii outer membrane protein A induces autophagy in bone marrow‐derived dendritic cells involving the PI3K/mTOR pathway
Hongyi Tan, Liyan Cao
Immunity, Inflammation and Disease.2023;[Epub] CrossRef - Advances in research on virulence factors ofAcinetobacter baumanniiand their potential as novel therapeutic targets
Jian-Xia Zhou, Ding-Yun Feng, Xia Li, Jia-Xin Zhu, Wen-Bin Wu, Tian-tuo Zhang
Journal of Applied Microbiology.2023;[Epub] CrossRef - Famotidine Enhances Rifampicin Activity against Acinetobacter baumannii by Affecting OmpA
Meng-na Zhang, Xiao-ou Zhao, Qi Cui, Dao-mi Zhu, Muhammad Asif Wisal, Han-dong Yu, Ling-cong Kong, Hong-xia Ma, Laurie E. Comstock
Journal of Bacteriology.2023;[Epub] CrossRef - Factors mediating Acinetobacter baumannii biofilm formation: Opportunities for developing therapeutics
Kirti Upmanyu, Qazi Mohd. Rizwanul Haq, Ruchi Singh
Current Research in Microbial Sciences.2022; 3: 100131. CrossRef - Evaluation the reactivity of a peptide-based monoclonal antibody derived from OmpA with drug resistant pulsotypes of Acinetobacter baumannii as a potential therapeutic approach
Omid Yeganeh, Mahdi Shabani, Parviz Pakzad, Nariman Mosaffa, Ali Hashemi
Annals of Clinical Microbiology and Antimicrobials.2022;[Epub] CrossRef - Therapeutic Effects of Inhibitor of ompA Expression against Carbapenem-Resistant Acinetobacter baumannii Strains
Seok-Hyeon Na, Hyejin Jeon, Man-Hwan Oh, Yoo-Jeong Kim, Mingi Chu, Ill-Young Lee, Je-Chul Lee
International Journal of Molecular Sciences.2021; 22(22): 12257. CrossRef - DksA Modulates Antimicrobial Susceptibility of Acinetobacter baumannii
Nayeong Kim, Joo-Hee Son, Kyeongmin Kim, Hyo-Jeong Kim, Minsang Shin, Je-Chul Lee
Antibiotics.2021; 10(12): 1472. CrossRef
- Novel nuclear targeting coiled-coil protein of Helicobacter pylori showing Ca2+-independent, Mg2+-dependent DNase I activity
-
Young Chul Kwon , Sinil Kim , Yong Seok Lee , Je Chul Lee , Myung-Je Cho , Woo-Kon Lee , Hyung-Lyun Kang , Jae-Young Song , Seung Chul Baik , Hyeon Su Ro
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J. Microbiol. 2016;54(5):387-395. Published online April 20, 2016
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DOI: https://doi.org/10.1007/s12275-016-5631-9
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67
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5
Crossref
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Abstract
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HP0059, an uncharacterized gene of Helicobacter pylori, encodes
a 284-aa-long protein containing a nuclear localization
sequence (NLS) and multiple leucine-rich heptad repeats.
Effects of HP0059 proteins in human stomach cells were assessed
by incubation of recombinant HP0059 proteins with
the AGS human gastric carcinoma cell line. Wild-type HP0059
proteins showed cytotoxicity in AGS cells in a concentrationdependent
manner, whereas NLS mutant protein showed no
effect, suggesting that the cytotoxicity is attributed to host nuclear
localization. AGS cells transfected with pEGFP-HP0059
plasmid showed strong GFP signal merged to the chromosomal
DNA region. The chromosome was fragmented into
multiple distinct dots merged with the GFP signal after 12 h
of incubation. The chromosome fragmentation was further
explored by incubation of AGS chromosomal DNA with recombinant
HP0059 proteins, which leaded to complete degradation
of the chromosomal DNA. HP0059 protein also
degraded circular plasmid DNA without consensus, being an
indication of DNase I activity. The DNase was activated by
MgCl2, but not by CaCl2. The activity was completely blocked
by EDTA. The optimal pH and temperature for DNase activity
were 7.0–8.0 and 55°C, respectively. These results indicate
that HP0059 possesses a novel DNase I activity along
with a role in the genomic instability of human gastric cells,
which may result in the transformation of gastric cells.
-
Citations
Citations to this article as recorded by - The Identification of a Novel Nucleomodulin MbovP467 of Mycoplasmopsis bovis and Its Potential Contribution in Pathogenesis
Abdul Raheem, Doukun Lu, Abdul Karim Khalid, Gang Zhao, Yingjie Fu, Yingyu Chen, Xi Chen, Changmin Hu, Jianguo Chen, Huanchun Chen, Aizhen Guo
Cells.2024; 13(7): 604. CrossRef - Molecular Coevolution of Nuclear and Nucleolar Localization Signals inside the Basic Domain of HIV-1 Tat
Margarita A. Kurnaeva, Arthur O. Zalevsky, Eugene A. Arifulin, Olga M. Lisitsyna, Anna V. Tvorogova, Maria Y. Shubina, Gleb P. Bourenkov, Maria A. Tikhomirova, Daria M. Potashnikova, Anastasia I. Kachalova, Yana R. Musinova, Andrey V. Golovin, Yegor S. Va
Journal of Virology.2022;[Epub] CrossRef - Bacterial nucleomodulins and cancer: An unresolved enigma
Abdul Arif Khan, Zakir Khan
Translational Oncology.2021; 14(1): 100922. CrossRef - TatD DNases of African trypanosomes confer resistance to host neutrophil extracellular traps
Kai Zhang, Ning Jiang, Hongyu Chen, Naiwen Zhang, Xiaoyu Sang, Ying Feng, Ran Chen, Qijun Chen
Science China Life Sciences.2021; 64(4): 621. CrossRef - Origin of the nuclear proteome on the basis of pre-existing nuclear localization signals in prokaryotic proteins
Olga M. Lisitsyna, Margarita A. Kurnaeva, Eugene A. Arifulin, Maria Y. Shubina, Yana R. Musinova, Andrey A. Mironov, Eugene V. Sheval
Biology Direct.2020;[Epub] CrossRef
- Mutational inactivation of OprD in carbapenem-resistant Pseudomonas aeruginosa isolates from Korean hospitals
-
Chi Hyun Kim , Hee Young Kang , Bo Ra Kim , Hyejin Jeon , Yoo Chul Lee , Sang Hwa Lee , Je Chul Lee
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J. Microbiol. 2016;54(1):44-49. Published online January 5, 2016
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DOI: https://doi.org/10.1007/s12275-016-5562-5
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81
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23
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Abstract
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This study investigated the mechanisms underlying the carbapenem
resistance of bloodstream isolates of Pseudomonas
aeruginosa obtained from two Korean hospitals. Of the 79
P. aeruginosa isolates, 22 and 21 were resistant to imipenem
and meropenem, respectively. The 22 imipenem-resistant
P. aeruginosa isolates were classified into 7 sequence types
(STs) and 13 pulsotypes. Twelve imipenem-resistant isolates
from one hospital were found to belong to the international
clone ST111. Two imipenem-resistant P. aeruginosa ST235
isolates carried the blaIMP-6 gene, but the remaining 20 isolates
did not produce carbapenemases. Mutations in the oprD
gene and a related decrease in gene expression were found
in 21 and 5 isolates, respectively. However, all imipenemresistant
P. aeruginosa isolates showed no significant expression
of OprD in the outer membrane as compared with that
of carbapenem-susceptible PAO1 strain. Overexpression of
genes associated with efflux pumps, including mexB, mexD,
mexF, and mexY, was not found in any imipenem-resistant
isolate. One imipenem-resistant P. aeruginosa isolate overexpressed
the ampC gene. Our results show that the low permeability
of drugs due to the mutational inactivation of OprD
is primarily responsible for carbapenem resistance in bloodstream
isolates of P. aeruginosa from Korean hospitals.
-
Citations
Citations to this article as recorded by
- 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
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DOI: https://doi.org/10.1007/s12275-015-5085-5
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73
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0
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15
Crossref
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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
Citations to this article as recorded by - 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
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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
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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
- Acinetobacter baumannii Outer Membrane Protein A Modulates the Biogenesis of Outer Membrane Vesicles
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Dong Chan Moon , Chul Hee Choi , Jung Hwa Lee , Chi-Won Choi , Hye-Yeon Kim , Jeong Soon Park , Seung Il Kim , Je Chul Lee
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J. Microbiol. 2012;50(1):155-160. Published online February 27, 2012
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DOI: https://doi.org/10.1007/s12275-012-1589-4
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111
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0
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94
Crossref
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Abstract
-
Acinetobacter baumannii secretes outer membrane vesicles
(OMVs) during both in vitro and in vivo growth, but the
biogenesis mechanism by which A. baumannii produces
OMVs remains undefined. Outer membrane protein A of
A. baumannii (AbOmpA) is a major protein in the outer
membrane and the C-terminus of AbOmpA interacts with
diaminopimelate of peptidoglycan. This study investigated
the role of AbOmpA in the biogenesis of A. baumannii
OMVs. Quantitative and qualitative approaches were used
to analyze OMV biogenesis in A. baumannii ATCC 19606T
and an isogenic ΔAbOmpA mutant. OMV production was
significantly increased in the ΔAbOmpA mutant compared
to wild-type bacteria as demonstrated by quantitation of
proteins and lipopolysaccharides (LPS) packaged in OMVs.
LPS profiles prepared from OMVs from wild-type bacteria
and the ΔAbOmpA mutant had identical patterns, but
proteomic analysis showed different protein constituents in
OMVs from wild-type bacteria compared to the ΔAbOmpA
mutant. In conclusion, AbOmpA influences OMV biogenesis
by controlling OMV production and protein composition.
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Salmonella enterica
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antigens UreB and CagA induce protection against
Helicobact
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Cai-Hua Zhang, Ding-Ci Lu, Ying Liu, Lingzhi Wang, Gautam Sethi, Zhaowu Ma
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Bacterial outer membrane vesicles provide an alternative pathway for trafficking of
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Infection and Drug Resistance.2023; Volume 16: 19. CrossRef - The Two Faces of Bacterial Membrane Vesicles: Pathophysiological Roles and Therapeutic Opportunities
Himadri B. Thapa, Stephan P. Ebenberger, Stefan Schild
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Biomedicines.2023; 11(2): 568. CrossRef - Vaccine development to control the rising scourge of antibiotic-resistant Acinetobacter baumannii: a systematic review
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Outer Membrane Vesicles of
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DS002 Are Selectively Enriched with TonB-Dependent Transporters and Play a Key Role in Iron Acquisition
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- Immunostimulatory Activity of Dendritic Cells Pulsed with Carbonic Anhydrase IX and Acinetobacter baumannii Outer Membrane Protein A for Renal Cell Carcinoma
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Bo Ra Kim , Eun Kyoung Yang , Sun Hee Kim , Dong Chan Moon , Hwa Jung Kim , Je Chul Lee , Duk Yoon Kim
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J. Microbiol. 2011;49(1):115-120. Published online March 3, 2011
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DOI: https://doi.org/10.1007/s12275-011-1037-x
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Abstract
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Dendritic cell (DC)-based immunotherapy is a potent therapeutic modality for treating renal cell carcinoma (RCC), but development of antigens specific for tumor-targeting and anti-tumor immunity is of great interest for clinical trials. The present study investigated the ability of DCs pulsed with a combination of carbonic anhydrase IX (CA9) as an RCC-specific biomarker and Acinetobacter baumannii outer membrane protein A (AbOmpA) as an immunoadjuvant to induce anti-tumor immunity against murine renal cell carcinoma (RENCA) in a murine model. Murine bone-marrow-derived DCs pulsed with a combination of RENCA lysates and AbOmpA were tested for their capacity to induce DC maturation and T cell responses in vitro. A combination of RENCA lysates and AbOmpA up-regulated the surface expression of co-stimulatory molecules, CD80 and CD86, and the antigen presenting molecules, major histocompatibility (MHC) class I and class II, in DCs. A combination of RENCA lysates and AbOmpA also induced interleukin-12 (IL-12) production in DCs. Next, the immunostimulatory activity of DCs pulsed with a combination of CA9 and AbOmpA
was determined. A combination of CA9 and AbOmpA up-regulated the surface expression of co-stimulatory molecules and antigen presenting molecules in DCs. DCs pulsed with a combination of CA9 and AbOmpA effectively secreted IL-12 but not IL-10. These cells interacted with T cells and formed clusters. DCs pulsed
with CA9 and AbOmpA elicited the secretion of interferon-γ and IL-2 in T cells. In conclusion, a combination of CA9 and AbOmpA enhanced the immunostimulatory activity of DCs, which may effectively induce anti-tumor immunity against human RCC.
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Citations
Citations to this article as recorded by - The Outer Membrane Proteins OmpA, CarO, and OprD of Acinetobacter baumannii Confer a Two-Pronged Defense in Facilitating Its Success as a Potent Human Pathogen
Siva R. Uppalapati, Abhiroop Sett, Ranjana Pathania
Frontiers in Microbiology.2020;[Epub] CrossRef - Host Innate Immune Responses to Acinetobacter baumannii Infection
Wangxue Chen
Frontiers in Cellular and Infection Microbiology.2020;[Epub] CrossRef - Generation of anti-tumour immune response using dendritic cells pulsed with carbonic anhydrase IX-Acinetobacter baumanniiouter membrane protein A fusion proteins against renal cell carcinoma
B-R Kim, E-K Yang, D-Y Kim, S-H Kim, D-C Moon, J-H Lee, H-J Kim, J-C Lee
Clinical and Experimental Immunology.2011; 167(1): 73. CrossRef
- Emergence of Vancomycin-Intermediate Staphylococcus aureus from Predominant Methicillin-Resistant S. aureus Clones in a Korean Hospital
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Hwa Yun Cha , Hyun Ok Kim , Jong Sook Jin , Je Chul Lee
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J. Microbiol. 2010;48(4):533-535. Published online August 20, 2010
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DOI: https://doi.org/10.1007/s12275-010-0062-5
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Abstract
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The genetic and epidemiological features of four vancomycin-intermediate Staphylococcus aureus (VISA) isolates obtained from a Korean hospital were evaluated in this study. The VISA isolates were genotyped as sequence type (ST) 5-staphylococcal cassette chromosome mec (SCCmec) II variant (n=2) and ST239- SCCmec III (n=2), which were derived from the predominant methicillin-resistant S. aureus (MRSA) clones in Korean hospitals. One VISA isolate was acquired during vancomycin treatment, whereas three VISA isolates were obtained from the patients who had not previously been exposed to glycopeptides. As VISA is likely to arise from the predominant MRSA clones and may then possibly spread between patients, the emergence of VISA should be monitored with great care in hospitals.
- Acinetobacter baumannii Outer Membrane Protein A Induces Dendritic Cell Death Through Mitochondrial Targeting
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Jun Sik Lee , Chul Hee Choi , Jung Wook Kim , Je Chul Lee
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J. Microbiol. 2010;48(3):387-392. Published online June 23, 2010
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DOI: https://doi.org/10.1007/s12275-010-0155-1
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Abstract
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Acinetobacter baumannii outer membrane protein A (AbOmpA) is a potential virulence factor that induces epithelial cell death, but its pathologic effects on the immune system have yet to be determined. The present study investigated the pathologic events occurring in dendritic cells (DCs) exposed to a cytotoxic
concentration of AbOmpA. AbOmpA induced early-onset apoptosis and delayed-onset necrosis in DCs. AbOmpA targeted the mitochondria and induced the production of reactive oxygen species (ROS). ROS were directly responsible for both apoptosis and necrosis of AbOmpA-treated DCs. These results demonstrate
that the AbOmpA secreted from A. baumannii induces DC death, which may impair T cell biology to induce adaptive immune responses against A. baumannii.
- Prediction of Bacterial Proteins Carrying A Nuclear Localization Signal and Nuclear Targeting of HsdM from Klebsiella pneumoniae
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Je Chul Lee , Dong Sun Kim , Dong Chan Moon , Jung-Hwa Lee , Mi Jin Kim , Su Man Lee , Yong Seok Lee , Se-Won Kang , Eun Jung Lee , Sang Sun Kang , Eunpyo Lee , Sung Hee Hyun
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J. Microbiol. 2009;47(5):641-645. Published online October 24, 2009
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DOI: https://doi.org/10.1007/s12275-009-0217-4
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Abstract
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Nuclear targeting of bacterial proteins is an emerging pathogenic mechanism whereby bacterial proteins can interact with nuclear molecules and alter the physiology of host cells. The fully sequenced bacterial genome can predict proteins that target the nuclei of host cells based on the presence of nuclear localization
signal (NLS). In the present study, we predicted bacterial proteins with the NLS sequences from Klebsiella pneumoniae by bioinformatic analysis, and 13 proteins were identified as carrying putative NLS sequences. Among them, HsdM, a subunit of KpnAI that is a type I restriction-modification system found in K. pneumoniae, was selected for the experimental proof of nuclear targeting in host cells. HsdM carried
the NLS sequences, 7KKAKAKK13, in the N-terminus. A transient expression of HsdM-EGFP in COS-1 cells exhibited exclusively a nuclear localization of the fusion proteins, whereas the fusion proteins of HsdM with substitutions in residues lysine to alanine in the NLS sequences, 7AAAKAAA13, were localized in the cytoplasm. HsdM was co-localized with importin α in the nuclei of host cells. Recombinant HsdM alone methylated the eukaryotic DNA in vitro assay. Although HsdM tested in this study has not been considered to be a virulence factor, the prediction of NLS motifs from the full sequenced genome of bacteria extends
our knowledge of functional genomics to understand subcellular targeting of bacterial proteins.
- Characterization of Conjugative Plasmids Carrying Antibiotic Resistance Genes Encoding 16S rRNA Methylase, Extended-Spectrum Beta-Lactamase, and/or Plasmid-Mediated AmpC Beta-Lactamase
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Hee Young Kang , Jungmin Kim , Sung Yong Seol , Yoo Chul Lee , Je Chul Lee , Dong Taek Cho
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J. Microbiol. 2009;47(1):68-75. Published online February 20, 2009
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DOI: https://doi.org/10.1007/s12275-008-0158-3
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Abstract
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In this study, we identified extended-spectrum ß-lactamase (ESBL) and plasmid-mediated AmpC ß-lactamase which were associated with 16S rRNA methylase gene on the conjugative plasmid. Among 82 clinical isolates of Enterobacteriaceae that carry 16S rRNA methylase gene (64 strains, armA, and 18 strains, rmtB), blaSHV-12 was detected either alone or combined with blaDHA-1, blaCTX-M-3, and blaCTX-M-14 in 30 strains carrying armA and 6 strains carrying rmtB. The blaCTX-M-3 was detected in 13 of 64 strains carrying armA but no strains carrying rmtB. Whereas blaCTX-M-14 was detected in 15 of 18 strains carrying rmtB but only 2 of 64 strains carrying armA. Overall, blaSHV-12 and blaCTX-M-14 was the most common ESBL gene which was associated with armA and rmtB, respectively. In addition, we found that blaCTX-M-3 localized with armA on the same IncL/M plasmid and blaCTX-M-14 localized with rmtB on the same IncA/C plasmid. Restriction fragment length polymorphism of conjugative plasmids and pulsed-field gel electrophoresis of genomic DNAs revealed that intercellular horizontal transfer of conjugative plasmid and clonal transmission have been occurred at the same time.
- Proteomic Analysis of Outer Membrane Proteins from Acinetobacter baumannii DU202 in Tetracycline Stress Condition
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Sung-Ho Yun , Chi-Won Choi , Soon-Ho Park , Je Chul Lee , Sun-Hee Leem , Jong-Soon Choi , Soohyun Kim , Seung Il Kim
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J. Microbiol. 2008;46(6):720-727. Published online December 24, 2008
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DOI: https://doi.org/10.1007/s12275-008-0202-3
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53
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Abstract
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Acinetobacter baumannii readily developed antimicrobial resistance to clinically available antibiotics. A. baumannii DU202 is a multi-drug resistant strain, and is highly resistant to tetracycline (MIC>1,024μg/ml). The surface proteome of A. baumannii DU202 in response to the sub-minimal inhibitory concentration (subMIC) of tetracycline was analyzed by 2-DE/MS-MS and 1-DE/LC/MS-MS to understand the pathways that form barriers for tetracycline. Membrane expression of major outer membrane proteins (Omps) was significantly decreased in response to the subMIC of tetracycline. These Omps with sizes of 38, 32, 28, and 21 kDa were identified as OmpA38, OmpA32, CarO, and OmpW, respectively. However, transcription level of these Omps was not significantly changed. 1-DE/LC/MS-MS analysis of secreted proteins showed that OmpA38, CarO, OmpW, and other Omps were increasingly secreted at tetracycline condition. This result suggests that A. baumannii actively regulates the membrane expression and the secretion of Omps to overcome antibiotic stress condition.
- Anti-Tumor Activity of Acinetobacter baumannii Outer Membrane Protein A on Dendritic Cell-Based Immunotherapy against Murine Melanoma
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Jun Sik Lee , Jung Wook Kim , Chul Hee Choi , Won Kee Lee , Hae Young Chung , Je Chul Lee
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J. Microbiol. 2008;46(2):221-227. Published online June 11, 2008
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DOI: https://doi.org/10.1007/s12275-008-0052-z
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Abstract
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Acinetobacter baumannii outer membrane protein A (AbOmpA) is a major surface protein that is an important pathogen-associated molecular pattern. Based on our previous findings that AbOmpA induced the phenotypic maturation of dendritic cells (DCs) and drove the Th1 immune response in vitro, we investigated the therapeutic efficacy of AbOmpA-pulsed DC vaccines in a murine melanoma model. The surface expression of co-stimulatory molecules (CD80 and CD86) and major histocompatibility complex class I and II molecules was higher in DCs pulsed with AbOmpA alone or with a combination of B16F10 cell lysates than that of DCs pulsed with B16F10 cell lysates. AbOmpA stimulated the maturation of murine splenic DCs in vivo. In a therapeutic model of murine melanoma, AbOmpA-pulsed DCs significantly retarded tumor growth and improved the survival of tumor-bearing mice. AbOmpA-pulsed DCs significantly enhanced CD8+, interleukin-2+ T cells and CD4+, interferon-γ+ T cells in tumor-bearing mice. These results provide evidence that AbOmpA may be therapeutically useful in adjuvant DC immunotherapy against poorly immunogenic
melanoma without tumor-specific antigens.
- Phenotypic and Genotypic Differences of the Vancomycin-Resistant Enterococcus faecium Isolates from Humans and Poultry in Korea
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Jae Young Oh , Seunghun An , Jong Sook Jin , You Chul Lee , Dong Teak Cho , Je Chul Lee
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J. Microbiol. 2007;45(5):466-472.
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DOI: https://doi.org/2588 [pii]
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Abstract
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A total of 98 vancomycin-resistant Enterococcus faecium (VREF) isolates (58 isolates from patients and 40 isolates from poultry) were compared based on their antimicrobial susceptibility, Tn1546 element organization, and pulsed-field gel electrophoresis (PFGE) patterns. This comparison aided in determining the relationships between the groups of isolates. All the VREF isolates harbored the vanA gene; however, 29 (29.6%) of the isolates exhibited the VanB phenotype-vanA genotype. Furthermore, the VREF isolates from humans and poultry exhibited distinct antimicrobial resistance patterns. The PCR mapping of the Tn1546 elements exhibited 12 different transposon types (A to L). The VREF isolates of poultry were classified into types A to D, whereas the human isolates were classified into types E to L. A PFGE analysis demonstrated a high degree of clonal heterogeneity in both groups of isolates; however, the distinct VREF clones appeared in each group of isolates. The deletion of the vanX-vanY genes or insertion of IS1216V in the intergenic region from the vanX-vanY genes is directly associated with the incongruence of the VanB phenotype-vanA genotype in human VREF isolates. These data suggest that the VREF isolates exhibit distinct phenotypic and genotypic traits according to their origins, which suggests that no evidence exists to substantiate the clonal spread or transfer of vancomycin resistance determinants between humans and poultry.
- A Comparison of Adult and Pediatric Methicillin-Resistant Staphylococcus aureus Isolates Collected from Patients at a University Hospital in Korea
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Jin Yeol Park , Jong Sook Jin , Hee Young Kang , Eun Hee Jeong , Je Chul Lee , Yoo Chul Lee , Sung Yong Seol , Dong Taek Cho , Jungmin Kim
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J. Microbiol. 2007;45(5):447-452.
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DOI: https://doi.org/2591 [pii]
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Abstract
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In this study, we compared the phenotypic and genotypic characteristics of 138 MRSA isolates obtained from adult and pediatric patients (adult, 50; children, 88). The resistance rates against gentamicin, clindamycin, and ciprofloxacin were much higher in the adult MRSA isolates than in the pediatric MRSA isolates. The ermC gene, which is responsible for inducible clindamycin resistance, was detected in 52(59.1%) of the 88 pediatric MRSA isolates but in only 5(10.0%) of the 50 adult MRSA isolates. MRSA isolates of clonal type ST5 with an integration of SCCmec type II/II variants was the most predominant clone among the adult isolates, while clonal type ST72 with an integration of SCCmec IV/IVA was the most predominant clone among the pediatric MRSA isolates. Staphylococcal enterotoxin A and toxic shock syndrome toxin-1 were prevalent among the adult MRSA isolates but not among the pediatric MRSA isolates. The results of this study demonstrated remarkable differences between adult and pediatric MRSA isolates in terms of their antimicrobial susceptibility profiles, SCCmec type, multilocus sequence type, staphylococcal toxin genes, and erythromycin resistance genes.
- Molecular Characterization of Pseudomonas aeruginosa Isolates Resistant to All Antimicrobial Agents, but Susceptible to Colistin, in Daegu, Korea
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Yoo Chul Lee , Byung Jun Ahn , Jong Sook Jin , Jung Uk Kim , Sang Hwa Lee , Do Young Song , Won Kil Lee , Je Chul Lee
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J. Microbiol. 2007;45(4):358-363.
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DOI: https://doi.org/2560 [pii]
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Abstract
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Multi-drug resistant Pseudomonas aeruginosa has been implicated in a variety of serious therapeutic problems in clinical environments. Among the 968 P. aeruginosa isolates obtained from two hospitals in Daegu, Korea, we acquired 17 isolates that were resistant to all available tested antimicrobial agents, with the exception of colistin (colistin-only sensitive). We characterized the antimicrobial susceptibilities, metallo-β-lactamases, and epidemiological relatedness among the colistin-only sensitive P. aeruginosa isolates. All colistin-only sensitive isolates were positive in the modified Hodge test and imipenem-EDTA synergy test, thereby indicating the production of metallo-β-lactamases. 11 isolates from the secondary hospital and six isolates from the tertiary teaching hospital harbored blaVIM-2 and blaIMP-1, respectively. The pulsed-field gel electrophoretic analysis of the SpeI-digested DNA from P. aeruginosa isolates indicated that two different clones of colistin-only sensitive P. aeruginosa originated from each hospital, and had spread within the hospital environment. Overall, colistin-only sensitive P. aeruginosa was detected in Korea for the first time, but no pan-drug resistant bacteria were identified. Nationwide surveillance is required in order to monitor the emergence of colistin-only sensitive or pan-drug resistant bacteria.
- Isolation of Quinolone-Resistant Escherichia coli Found in Major Rivers in Korea
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Dahye Jung , Min Young Lee , Jung Min Kim , Je Chul Lee , Dong Taek Cho , Yeonhee Lee
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J. Microbiol. 2006;44(6):680-684.
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DOI: https://doi.org/2456 [pii]
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Abstract
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Twenty isolates resistant to seven quinolones were isolated from major rivers in Korea. All isolates had three mutations, Ser83→Leu and Asp87→Asn in GyrA and Ser80→Ile or Ser80→Arg in ParC and three isolates had an additional mutation Glu84→Gly or Glu84→Val in ParC. In addition, a clonal spread was not found in these isolates.
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