Journal of Microbiology

Jinmoon Kim

5 Articles

CagL polymorphisms between East Asian and Western Helicobacter pylori are associated with different abilities to induce IL-8 secretion: Yun Hui Choi , Jing Lai , Myeong-A Kim , Aeryun Kim , Jinmoon Kim , Hanfu Su , Linhu Ge , Jeong-Heon Cha; J. Microbiol. 2021;59(8):763-770. Published online June 1, 2021; DOI: https://doi.org/10.1007/s12275-021-1136-2

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Helicobacter pylori colonizes human gastric mucosa. Its infection is associated with gastric diseases including gastric cancer. CagA is one of the most important toxins produced by H. pylori. It is related to gastric cancer which can be injected into host cells via a type IV secretion system (T4SS). CagL is a structural component of T4SS apparatus, which triggers host cell signaling pathway. It has been reported that CagL polymorphisms may influence the severity of disease development. To explore the contribution of CagL polymorphisms between East Asian and Western H. pylori in pathogenesis, cagL gene in G27 H. pylori was swapped by K74 cagL which is identical to East Asian CagL consensus sequence and by Western 26695 H. pylori, resulting in G27ΔcagL/cagLK74 and G27ΔcagL/cagL26695, respectively. Intriguingly, G27ΔcagL/ cagLK74 showed significantly less ability of IL-8 induction than G27ΔcagL/cagL26695 while displayed similar abilities of CagA phosphorylation, and cell elongation. Taken together, this study suggests that the CagL polymorphism may influence IL-8 induction, and K74 CagL has less ability to induce IL-8 secretion than G27 or 26695 CagL. Further research should address how the different capabilities of IL-8 induction between intraspecies-CagL are associated with the large differences of the incidence of gastric cancer between East Asian and Western countries.

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Integrative bioinformatics and machine learning identify shared molecular mechanisms and diagnostic biomarkers between Helicobacter pylori infection and atrial fibrillation
Aojian Deng, Wei Wang, Tomasz W. Kaminski
PLOS One.2026; 21(4): e0346038. CrossRef
Roles of the components of the cag -pathogenicity island encoded type IV secretion system in Helicobacter pylori
Lingzhu Gou, Xiaoping Yang, Jianwei Yun, Zenghui Ma, Xiaofeng Zheng, Hongwei Du, Dekui Zhang
Future Microbiology.2024; 19(14): 1253. CrossRef
Antibacterial and Immunoregulatory Effects of Metformin against Helicobacter pylori Infection in Rat Model
Hassan Valadbeigi, Saeed Khoshnood, Babak Negahdari, Mohd Azmuddin Abdullah, Mohammad Hossein Haddadi, Abhimanyu Abhimanyu
BioMed Research International.2023;[Epub] CrossRef
New CagL Amino Acid Polymorphism Patterns of Helicobacter pylori in Peptic Ulcer and Non-Ulcer Dyspepsia
Reyhan Caliskan, Silva Polat Sari, Bahadir Ercan, Kivanc Derya Peker, Mehtap Omac Sonmez, Ozer Akgul, Burcu Sapmaz, Aliye Soylu, Gokhan Tolga Adas, Yasar Ali Oner, Pelin Yuksel Mayda
Medicina.2022; 58(12): 1738. CrossRef
Geographic diversity in Helicobacter pylori oipA genotype between Korean and United States isolates
Aeryun Kim, Jing Lai, D. Scott Merrell, Ji-Hye Kim, Hanfu Su, Jeong-Heon Cha
Journal of Microbiology.2021; 59(12): 1125. CrossRef

Cot kinase plays a critical role in Helicobacter pylori-induced IL-8 expression: Sungil Jang , Jinmoon Kim , Jeong-Heon Cha; J. Microbiol. 2017;55(4):311-317. Published online March 31, 2017; DOI: https://doi.org/10.1007/s12275-017-7052-9

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Helicobacter pylori is a major pathogen causing various gastric diseases including gastric cancer. Infection of H. pylori induces pro-inflammatory cytokine IL-8 expression in gastric epithelial cells in the initial inflammatory process. It has been known that H. pylori can modulate Ras-Raf-Mek-Erk signal pathway for IL-8 induction. Recently, it has been shown that another signal molecule, cancer Osaka thyroid oncogene/tumor progression locus 2 (Cot/Tpl2) kinase, activates Mek and Erk and plays a role in the Erk pathway, similar to MAP3K signal molecule Raf kinase. Therefore, the objective of this study was to determine whether Cot kinase might be involved in IL-8 induction caused by H. pylori infection. AGS gastric epithelial cells were infected by H. pylori strain G27 or its isogenic mutants lacking cagA or type IV secretion system followed by treatment with Cot kinase inhibitor (KI) or siRNA specific for Cot kinase. Activation of Erk was assessed by Western blot analysis and expression of IL-8 was measured by ELISA. Treatment with Cot KI reduced both transient and sustained Erk activation. It also reduced early and late IL-8 secretion in the gastric epithelial cell line. Furthermore, siRNA knockdown of Cot inhibited early and late IL-8 secretion induced by H. pylori infection. Taken together, these results suggest that Cot kinase might play a critical role in H. pylori type IV secretion apparatus-dependent early IL-8 secretion and CagA-dependent late IL-8 secretion as an alternative signaling molecule in the Erk pathway.

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Helicobacter pylori infection is correlated with the incidence of erosive oral lichen planus and the alteration of the oral microbiome composition
Shutong Li, Yangheng Zhang, Zongcheng Yang, Jingyuan Li, Ya Li, Huanjie Li, Wenjuan Li, Jihui Jia, Shaohua Ge, Yundong Sun
BMC Microbiology.2021;[Epub] CrossRef
Foot-and-Mouth Disease Virus Structural Protein VP1 Destroys the Stability of the TPL2 Trimer by Degradation of TPL2 To Evade Host Antiviral Immunity
Keshan Zhang, Minghao Yan, Junhong Hao, Chaochao Shen, Zixiang Zhu, Dajun Zhang, Jing Hou, Guowei Xu, Dan Li, Haixue Zheng, Xiangtao Liu, Susana López
Journal of Virology.2021;[Epub] CrossRef
Discovery and validation of methylated-differentially expressed genes in Helicobacter pylori-induced gastric cancer
Duanrui Liu, Xiaoli Ma, Fei Yang, Dongjie Xiao, Yanfei Jia, Yunshan Wang
Cancer Gene Therapy.2020; 27(6): 473. CrossRef
Probiotic effect on Helicobacter�pylori attachment and inhibition of inflammation in human gastric epithelial cells
Hanyi Song, Long Zhou, Dongyan Liu, Lihui Ge, Yan Li
Experimental and Therapeutic Medicine.2019;[Epub] CrossRef

Helicobacter pylori outer membrane protein, HomC, shows geographic dependent polymorphism that is influenced by the Bab family: Aeryun Kim , Stephanie L. Servetas , Jieun Kang , Jinmoon Kim , Sungil Jang , Yun Hui Choi , Hanfu Su , Yeong-Eui Jeon , Youngmin A. Hong , Yun-Jung Yoo , D. Scott Merrell , Jeong-Heon Cha; J. Microbiol. 2016;54(12):846-852. Published online November 26, 2016; DOI: https://doi.org/10.1007/s12275-016-6434-8

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The array of outer membrane proteins (OMPs) found in Helicobacter pylori provides a crucial component for persistent colonization within the gastric niche. Not only does H. pylori harbor a wide number of OMPs, but these OMPs often vary across strains; this likely contributes to immune evasion, adaptation during long term colonization, and potentially differential disease progression. Previous work from our group described OMP differences among the Bab family (babA, babB, and babC) and Hom family (homA and homB) from 80 American H. pylori clinical isolates (AH) and 80 South Korean H. pylori clinical isolates (KH). In the current study, we expanded our investigation to include the less well characterized Hom family member, HomC. Overall, we identified and genotyped three homC variants: homCS, homCL, and homCM, in both populations. Similar to other polymorphic genes, the KH group showed less overall diversity, with 97.5% of strains harboring homCL. In contrast, a more heterogeneous profile was observed in strains derived from an American population; we found nearly equal distribution of homCS and homCL. Further analysis of the AH group identified associations between homC polymorphism and bab genotype; in AH strains, there was a significant association between homCL and carriage of babA at locus A. Since babA is an important virulence factor for the development of severe gastric disease, these data may suggest that homC polymorphism plays a role in H. pylori pathogenesis.

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A unique Helicobacter pylori strain to study gastric cancer development
Jeannette M. Whitmire, Ian H. Windham, Morris O. Makobongo, Mandy D. Westland, Sirena C. Tran, Jaume Piñol, Yvonne Hui, Rasha Raheem Alkarkoushi, Oscar Q. Pich, David J. McGee, M. Blanca Piazuelo, Angela Melton-Celsa, Traci L. Testerman, Timothy L. Cover,
Microbiology Spectrum.2025;[Epub] CrossRef
Helicobacter pylori outer membrane protein families and related pathogenesis
Senlin You, Jiao Li, Eng Guan Chua, Alfred Tay, Mohammed Benghezal, Barry Marshall, Hong Tang, Hong Li
Microbial Pathogenesis.2025; 206: 107740. CrossRef
Infiltration to infection: key virulence players of Helicobacter pylori pathogenicity
Arghyadeep Bhattacharjee, Om Saswat Sahoo, Ahana Sarkar, Saurabh Bhattacharya, Rukhsana Chowdhury, Samarjit Kar, Oindrilla Mukherjee
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(Re)-definition of the holo- and apo-Fur direct regulons of Helicobacter pylori
Andrea Vannini, Eva Pinatel, Paolo Emidio Costantini, Simone Pelliciari, Davide Roncarati, Simone Puccio, Gianluca De Bellis, Vincenzo Scarlato, Clelia Peano, Alberto Danielli
Journal of Molecular Biology.2024; 436(10): 168573. CrossRef
Biofilm of Helicobacter pylori: Life Cycle, Features, and Treatment Options
Yasmine Elshenawi, Shuai Hu, Skander Hathroubi
Antibiotics.2023; 12(8): 1260. CrossRef
Recent Progress in Biomarker-Based Diagnostics of Helicobacter pylori , Gastric Cancer-Causing Bacteria
Kirti Saxena, Akanksha Deshwal, Ramesh Namdeo Pudake, Utkarsh Jain, Ravi Mani Tripathi
Biomarkers in Medicine.2023; 17(16): 679. CrossRef
Genomic diversity of Helicobacter pylori populations from different regions of the human stomach
Daniel James Wilkinson, Benjamin Dickins, Karen Robinson, Jody Anne Winter
Gut Microbes.2022;[Epub] CrossRef
Geographic diversity in Helicobacter pylori oipA genotype between Korean and United States isolates
Aeryun Kim, Jing Lai, D. Scott Merrell, Ji-Hye Kim, Hanfu Su, Jeong-Heon Cha
Journal of Microbiology.2021; 59(12): 1125. CrossRef
Virulence of Helicobacter pylori outer membrane proteins: an updated review
Chenjing Xu, Djaleel Muhammad Soyfoo, Yao Wu, Shunfu Xu
European Journal of Clinical Microbiology & Infectious Diseases.2020; 39(10): 1821. CrossRef
Comparative analysis of the Hom family of outer membrane proteins in isolates from two geographically distinct regions: The United States and South Korea
Stephanie L. Servetas, Aeryun Kim, Hanfu Su, Jeong‐Heon Cha, D. Scott Merrell
Helicobacter.2018;[Epub] CrossRef

Role of bacterial γ-glutamyltranspeptidase as a novel virulence factor in bone-resorbing pathogenesis: Jinmoon Kim , Sungil Jang , Aeryun Kim , Hanfu Su , Niluka Gunawardhana , Yeong-Eui Jeon , Eun Jung Bak , Ji-Hye Kim , Jeong-Heon Cha; J. Microbiol. 2016;54(5):396-402. Published online April 20, 2016; DOI: https://doi.org/10.1007/s12275-016-6137-1

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Mammalian γ-glutamyltranspeptidase (GGT) has been identified as a bone-resorbing factor. Since GGT of Bacillus subtilis exhibits similarity in their primary structure and enzymatic characteristics with mammalian GGTs, the bone-resorbing activity of bacterial GGT was examined in this study. Osteoclastogenesis was performed in a co-culture system of mouse calvaria-derived osteoblasts and bone marrow cells. A conditioned medium from GGT-overproducing B. subtilis culture showed significantly higher activity of osteoclast formation than a conditioned medium from wild-type B. subtilis culture. Recombinant GGT (rGGT) of wild-type B. subtilis and an enzymatic activity-defected rGGT of B. subtilis 2288 mutant were expressed in Escherichia coli and purified using His tag. Both purified rGGTs induced similar levels of osteoclastogenesis, suggesting that B. subtilis GGT possesses virulent boneresorbing activity and its activity is probably independent of its enzymatic activity. Furthermore, a recombinant protein of B. subtilis GGT heavy subunit (Bs rGGT/H) showed strong activity of osteoclastogenesis while the light subunit failed to show strong activity, suggesting that the bone-resorbing activity is mainly located at the heavy subunit. More importantly, the GGT enzymatic activity may not be required for this virulence activity since the light subunit contains the catalytic pocket. In addition, B. subtilis rGGT stimulated mRNA expressions of receptor activator of nuclear factor kappa-B ligand (RANKL) and cyclooxygenase-2 (COX-2), while an osteoprotegerin inhibited the osteoclast formation induced by Bs rGGT/H. This is the first demonstration that bacterial GGT itself is sufficient to act as a bone-resorbing virulence factor via RANKL-dependent pathway. Therefore, it can be hypothesized that GGT of periodontopathic bacteria may play an important role as a virulence factor in bone destruction.

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Meenu Saini, Amuliya Kashyap, Shruti Bindal, Kuldeep Saini, Rani Gupta
Frontiers in Microbiology.2021;[Epub] CrossRef
Quantitative analysis of γ-glutamylpeptides by liquid chromatography-mass spectrometry and application for γ-glutamyltransferase assays
Sho Kobayashi, Yoshinori Tokairin, Takeru Miyakoshi, Takuya Saito, Keita Nagaoka, Yoshitaka Ikeda, Junichi Fujii, Hiroyuki Konno
Analytical Biochemistry.2019; 578: 13. CrossRef
Isolation of γ-Glutamyl-Transferase Rich-Bacteria from Mouse Gut by a Near-Infrared Fluorescent Probe with Large Stokes Shift
Tao Liu, Qiu-Long Yan, Lei Feng, Xiao-Chi Ma, Xiang-Ge Tian, Zhen-Long Yu, Jing Ning, Xiao-Kui Huo, Cheng-Peng Sun, Chao Wang, Jing-Nan Cui
Analytical Chemistry.2018; 90(16): 9921. CrossRef
Heterologous expression and enzymatic characterization of γ-glutamyltranspeptidase from Bacillus amyloliquefaciens
Jung-Min Lee, Jaejung Lee, Gyeong-Hwa Nam, Byung-Sam Son, Myoung-Uoon Jang, So-Won Lee, Byung-Serk Hurh, Tae-Jip Kim
Journal of Microbiology.2017; 55(2): 147. CrossRef
Scientific Opinion on the update of the list of QPS‐recommended biological agents intentionally added to food or feed as notified to EFSA†
Antonia Ricci, Ana Allende, Declan Bolton, Marianne Chemaly, Robert Davies, Rosina Girones, Lieve Herman, Konstantinos Koutsoumanis, Roland Lindqvist, Birgit Nørrung, Lucy Robertson, Giuseppe Ru, Moez Sanaa, Marion Simmons, Panagiotis Skandamis, Emma Snar
EFSA Journal.2017;[Epub] CrossRef

Complementation System for Helicobacter pylori: Jinmoon Kim , Sung-Whan Kim , Sungil Jang , D. Scott Merrell , Jeong-Heon Cha; J. Microbiol. 2011;49(3):481-486. Published online June 30, 2011; DOI: https://doi.org/10.1007/s12275-011-1196-9

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Previously Langford et al. (2006) developed the pIR203C04 complementation system for Helicobacter pylori, which can be used to complement and restore phenotypic effects in H. pylori mutant, and furthermore they used the complementation system in vivo experiments to animals without altering the ability of strain SS1 to colonize mice. In their previous study, the pIR203C04 was able to transform 26695, SS1, J99, and 43504 H. pylori strains by an electroporation method. However, in the present study using a natural transformation the pIR203C04 transformed only 26695 H. pylori but not SS1, J99, 7.13, and G27 H. pylori strains. Since the useful complementation system has a limitation of narrow selection among H. pylori strains, we redesigned the complementation system for the improvement. The same intergenic chromosomal site between hp0203 and hp0204 was utilized for the new complementation system because the insertion at the intergenic site didn’t show any polar effects and disruption of other H. pylori genes. The genome sequence analysis showed that the intergenic regions among H. pylori strains may have too low homology to each others to do a homologous recombination. Thus, in addition to the short intergenic region, the fragments of the new complementation system included 3′ conserved parts of hp0203 and hp0204 coding regions. Between the fragments there are a chloramphenicol acetyltransferase cassette and multicloning sites, resulting in pKJMSH. DNA fragment of the interest can be cloned into the multicloning sites of pKJMSH and the fragment can be integrated at the intergenic region of H. pylori chromosome by the homologous recombination. Indeed, by the natural transformation, pKJMSH was able to transform all five H. pylori strains of 26695, SS1, J99, 7.13, and G27, which are common for the investigation of molecular pathogenesis. Thus, the new pKJMSH complementation system is applicable to most H. pylori wild-type stains.

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Huang Yang, Xiaoxing Huang, Xiaochuan Zhang, Xiaoyan Zhang, Xiaohong Xu, Feifei She, Yancheng Wen
Frontiers in Medicine.2022;[Epub] CrossRef
Dynamic Expansion and Contraction ofcagACopy Number inHelicobacter pyloriImpact Development of Gastric Disease
Sungil Jang, Hanfu Su, Faith C. Blum, Sarang Bae, Yun Hui Choi, Aeryun Kim, Youngmin A. Hong, Jinmoon Kim, Ji-Hye Kim, Niluka Gunawardhana, Yeong-Eui Jeon, Yun-Jung Yoo, D. Scott Merrell, Linhu Ge, Jeong-Heon Cha, Martin J. Blaser
mBio.2017;[Epub] CrossRef
Helicobacter pylori outer membrane protein, HomC, shows geographic dependent polymorphism that is influenced by the Bab family
Aeryun Kim, Stephanie L. Servetas, Jieun Kang, Jinmoon Kim, Sungil Jang, Yun Hui Choi, Hanfu Su, Yeong-Eui Jeon, Youngmin A. Hong, Yun-Jung Yoo, D. Scott Merrell, Jeong-Heon Cha
Journal of Microbiology.2016; 54(12): 846. CrossRef

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