Journal of Microbiology

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RapB Regulates Cell Adhesion and Migration in Dictyostelium, Similar to RapA: Uri Han, Nara Han, Byeonggyu Park, Taeck Joong Jeon; J. Microbiol. 2024;62(8):627-637. Published online June 17, 2024; DOI: https://doi.org/10.1007/s12275-024-00143-y

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Ras small GTPases act as molecular switches in various cellular signaling pathways, including cell migration, proliferation, and differentiation. Three Rap proteins are present in Dictyostelium; RapA, RapB, and RapC. RapA and RapC have been reported to have opposing functions in the control of cell adhesion and migration. Here, we investigated the role of RapB, a member of the Ras GTPase subfamily in Dictyostelium, focusing on its involvement in cell adhesion, migration, and developmental processes. This study revealed that RapB, similar to RapA, played a crucial role in regulating cell morphology, adhesion, and migration. rapB null cells, which were generated by CRISPR/Cas9 gene editing, displayed altered cell size, reduced cell-substrate adhesion, and increased migration speed during chemotaxis. These phenotypes of rapB null cells were restored by the expression of RapB and RapA, but not RapC. Consistent with these results, RapB, similar to RapA, failed to rescue the phenotypes of rapC null cells, spread morphology, increased cell adhesion, and decreased migration speed during chemotaxis. Multicellular development of rapB null cells remained unaffected. These results suggest that RapB is involved in controlling cell morphology and cell adhesion. Importantly, RapB appears to play an inhibitory role in regulating the migration speed during chemotaxis, possibly by controlling cell-substrate adhesion, resembling the functions of RapA. These findings contribute to the understanding of the functional relationships among Ras subfamily proteins.

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Intracellular Calcium Responses to External Calcium Stimuli in Dictyostelium
Dahyeon Kim, Jiseong Seo, Taeck Joong Jeon
Journal of Microbiology and Biotechnology.2025;[Epub] CrossRef

Sporosarcina jeotgali sp. nov., Sporosarcina oncorhynchi sp. nov., and Sporosarcina trichiuri sp. nov., Isolated from Jeotgal, a Traditional Korean Fermented Seafood: Ah-In Yang, Bora Kim, Sung-Hong Joe, Hae-In Joe, Hanna Choe, Ki Hyun Kim, Min Ok Jun, Na-Ri Shin; J. Microbiol. 2024;62(4):285-296. Published online April 8, 2024; DOI: https://doi.org/10.1007/s12275-024-00106-3

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Abstract

Three novel, Gram-stain-positive, obligate aerobic, catalase- and oxidase-positive bacterial strains, designated B2O-1(T), T2O-4(T), and 0.2-SM1T-5(T), were isolated from jeotgal, a traditional Korean fermented seafood. Strains B2O-1(T), T2O-4(T), and 0.2-SM1T-5(T) exhibited distinct colony colors, characterized by pink, yellow, and red opaque circular colonies, respectively. Phylogenetic analysis revealed that three strains formed a paraphyletic clade within the genus Sporosarcina and shared < 99.0% similarity with Sporosarcina aquimarina KCTC 3840(T) and Sporosarcina saromensis KCTC 13119(T) in their 16S rRNA gene sequences. The three strains exhibiting Orthologous Average Nucleotide Identity values < 79.3% and digital DNA-DNA hybridization values < 23.1% within the genus Sporosarcina affirmed their distinctiveness. Strains B2O-1(T), T2O-4(T), and 0.2-SM1T-5(T) contained MK-7 as a sole respiratory menaquinone and A4α type peptidoglycan based on lysine with alanine, glutamic acid, and aspartic acid. The common polar lipids include diphosphatidylglycerol, phosphatidylglycerol, and phosphatidylethanolamine. Strain T2O-4(T) contained one unidentified phospholipid, whereas strain 0.2-SM1T-5(T) contained two unidentified phospholipids. Cellular fatty acid profiles, with C(15:0) anteiso as the major fatty acid, supported the affiliation of the three strains to the genus Sporosarcina. Based on the polyphasic characteristics, strains B2O-1(T) (= KCTC 43506(T) = JCM 36032(T)), T2O-4(T) (= KCTC 43489(T) = JCM 36031(T)), and 0.2-SM1T-5(T) (= KCTC 43519(T) = JCM 36034(T)) represent three novel species within the genus Sporosarcina, named Sporosarcina jeotgali sp. nov., Sporosarcina oncorhynchi sp. nov., and Sporosarcina trichiuri sp. nov., respectively.

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Notification of changes in taxonomic opinion previously published outside the IJSEM. List of Changes in Taxonomic Opinion no. 41
Aharon Oren, Markus Göker
International Journal of Systematic and Evolutionary Microbiology .2025;[Epub] CrossRef
Brevibacterium koreense sp. nov., a moderately halophilic bacterium isolated from jogae-jeotgal, a Korean fermented seafood
Sohee Nam, Yujin Kim, Min Ji Lee, Yeon Bee Kim, Jeong Ui Yun, Mi-Ja Jung, Hye Seon Song, Se Hee Lee, Seok-Jun Kim, Tae Woong Whon
International Journal of Systematic and Evolutionary Microbiology .2025;[Epub] CrossRef
Validation List no. 220. Valid publication of new names and new combinations effectively published outside the IJSEM
Aharon Oren, Markus Göker
International Journal of Systematic and Evolutionary Microbiology .2024;[Epub] CrossRef

Minimal amino acids in the I/LWEQ domain required for anterior/posterior localization in Dictyostelium: Hyeseon Kim , Dong-Yeop Shin , Taeck Joong Jeon; J. Microbiol. 2017;55(5):366-372. Published online January 26, 2017; DOI: https://doi.org/10.1007/s12275-017-6550-0

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Abstract: Establishment of cell polarity is mediated by a series of signal-ing molecules that are asymmetrically activated or localized in the cell upon extracellular stimulation. To understand the mechanism that mediates anterior/posterior asymmetric localization of RapGAP3 during migration, we determined the minimally required amino acids in the I/LWEQ domain that cause posterior localization and found that the minimal region of the F-actin binding domain for posterior localiza-tion could, with some additional deletion at the C-terminal, localize to the anterior. Analysis of the localization and trans-location kinetics to the cell cortex of the truncated proteins suggests that the required regions for anterior/posterior lo-calization might have a preferential binding affinity to pre- existing F-actins at the rear and lateral sides of the cell or newly formed F-actins at the front of the cell, leading to dis-tinct differential sites of the cell.

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

Prevalence of avian influenza virus in wild birds before and after the HPAI H5N8 outbreak in 2014 in South Korea: Jeong-Hwa Shin , Chanjin Woo , Seung-Jun Wang , Jipseol Jeong , In-Jung An , Jong-Kyung Hwang , Seong-Deok Jo , Seung Do Yu , Kyunghee Choi , Hyen-Mi Chung , Jae-Hwa Suh , Seol-Hee Kim; J. Microbiol. 2015;53(7):475-480. Published online June 27, 2015; DOI: https://doi.org/10.1007/s12275-015-5224-z

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Abstract

Since 2003, highly pathogenic avian influenza (HPAI) virus outbreaks have occurred five times in Korea, with four HPAI H5N1 outbreaks and one HPAI H5N8 outbreak. Migratory birds have been suggested to be the first source of HPAI in Korea. Here, we surveyed migratory wild birds for the presence of AI and compared regional AI prevalence in wild birds from September 2012 to April 2014 for birds having migratory pathways in South Korea. Finally, we investigated the prevalence of AI in migratory birds before and after HPAI H5N8 outbreaks. Overall, we captured 1617 migratory wild birds, while 18,817 feces samples and 74 dead birds were collected from major wild bird habitats. A total of 21 HPAI viruses were isolated from dead birds, and 86 low pathogenic AI (LPAI) viruses were isolated from captured birds and from feces samples. Spatiotemporal distribution analysis revealed that AI viruses were spread southward until December, but tended to shift north after January, consistent with the movement of migratory birds in South Korea. Furthermore, we found that LPAI virus prevalences within wild birds were notably higher in 2013?014 than the previous prevalence during the northward migration season. The data from our study demonstrate the importance of the surveillance of AI in wild birds. Future studies including in-depth genetic analysis in combination with evaluation of the movement and ecology of migratory birds might help us to bridge the gaps in our knowledge and better explain, predict, and ultimately prevent future HPAI outbreaks.

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Viruses.2023; 15(2): 472. CrossRef
The global prevalence of highly pathogenic avian influenza A (H5N8) infection in birds: A systematic review and meta-analysis
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Microbial Pathogenesis.2023; 176: 106001. CrossRef
Avian influenza virus surveillance in wild bird in South Korea from 2019 to 2022
Eun-Jee Na, Su-Beom Chae, Jun-Soo Park, Yoon-Ji Kim, Young-Sik Kim, Jae-Ku Oem
Korean Journal of Veterinary Service.2022; 45(4): 285. CrossRef
A literature review of the use of environmental sampling in the surveillance of avian influenza viruses
Grace Hood, Xavier Roche, Aurélie Brioudes, Sophie von Dobschuetz, Folorunso Oludayo Fasina, Wantanee Kalpravidh, Yilma Makonnen, Juan Lubroth, Leslie Sims
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Kyuyoung Lee, Daesung Yu, Beatriz Martínez-López, Hachung Yoon, Sung-Il Kang, Seong-Keun Hong, Ilseob Lee, Yongmyung Kang, Wooseg Jeong, Eunesub Lee
Scientific Reports.2020;[Epub] CrossRef
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Ivette A. Nuñez, Ted M. Ross
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Zhenshun Xu, Jonguk Lee, Daihee Park, Yongwha Chung
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Joon Young Song, Min Joo Choi, Ji Yun Noh, Won Suk Choi, Hee Jin Cheong, Seong-Heon Wie, Jin-Soo Lee, Gyu-Jin Woo, Sang Ho Lee, Woo Joo Kim
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Review

REVIEW] Cell Migration: Regulation of Cytoskeleton by Rap1 in Dictyostelium discoideum: Mi-Rae Lee , Taeck J. Jeon; J. Microbiol. 2012;50(4):555-561. Published online August 25, 2012; DOI: https://doi.org/10.1007/s12275-012-2246-7

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Abstract

Cell movement involves a coordinated regulation of the cytoskeleton, F-actin-mediated protrusions at the front and myosin-mediated contraction of the posterior of a cell. The small GTPase Rap1 functions as a key regulator in the spatial and temporal control of cytoskeleton reorganization for cell migration. This review outlines the establishment of cell polarity by differential localizations of the cytoskeleton and discusses the spatial and temporal regulation of cytoskeleton
reorganization via the Rap1 signaling pathway during chemotaxis with a focus on recent advances in the study of chemotaxis using a simple eukaryotic model organism, Dictyostelium discoideum.

Citations

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RapB Regulates Cell Adhesion and Migration in Dictyostelium, Similar to RapA
Uri Han, Nara Han, Byeonggyu Park, Taeck Joong Jeon
Journal of Microbiology.2024; 62(8): 627. CrossRef
Roles of Rufy3 in experimental subarachnoid hemorrhage-induced early brain injury via accelerating neuronal axon repair and synaptic plasticity
Yang Wang, Jianguo Xu, Wanchun You, Haitao Shen, Xiang Li, Zhengquan Yu, Haiying Li, Gang Chen
Molecular Brain.2022;[Epub] CrossRef
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Yuan Du, Shenglan Li, Tong Zhou, Jing Zhao, Jiguang Liu
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Opposite functions of RapA and RapC in cell adhesion and migration in Dictyostelium
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Animal Cells and Systems.2021; 25(4): 203. CrossRef
Reversible function of RapA with the C-terminus of RapC in Dictyostelium
Dongju Kim, Wonbum Kim, Taeck Joong Jeon
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Research Support, Non-U.S. Gov't

Berberine Inhibits HEp-2 Cell Invasion Induced by Chlamydophila pneumoniae Infection: Li Jun Zhang , Li Jun Zhang , Wei Quan , Bei Bei Wang , Bing Ling Shen , Teng Teng Zhang , Yi Kang; J. Microbiol. 2011;49(5):834-840. Published online November 9, 2011; DOI: https://doi.org/10.1007/s12275-011-1051-z

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Abstract: This study investigated the inhibitory effects of berberine on Chlamydophila (Chlamydia) pneumoniae infection-induced HEp-2 cell invasion and explored the possible mechanisms involved in this process. C. pneumoniae infection resulted in a significant increase in HEp-2 cell invasion when compared with the control cells (P<0.01) in a Matrigel invasion assay. This enhanced cell invasion was strongly suppressed by berberine (50 μM) (P<0.01). In a cell adhesion assay, the infection-induced HEp-2 cell adhesion to Matrigel was also significantly inhibited by berberine (P<0.01). C. pneumoniae infection was found to promote HEp-2 cell migration remarkably (P<0.01), which was markedly suppressed by berberine (P<0.01) in the cell migration assays. There were no statistically significant differences in the expression of matrix metalloproteinase-1 (MMP-1) and MMP-9 in the infected cells and berberine did not change the expression of MMP-1 and MMP-9. These data suggest that berberine inhibits C. pneumoniae infection-induced HEp-2 cell invasion through suppressing HEp-2 cell adhesion and migration, but not through changing the expression of MMP-1 and MMP-9.

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