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Journal Article
Comparative study of the geographical spread of genogroup II porcine norovirus and human norovirus
Eung Seo Koo , Yong Seok Jeong
J. Microbiol. 2021;59(7):644-650.   Published online July 1, 2021
DOI: https://doi.org/10.1007/s12275-021-1218-1
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  • 1 Crossref
AbstractAbstract PDF
Livestock pigs and porcine norovirus could be candidate tools for future studies on the geographic isolation of norovirus. In this study, we provide the first evidence for geographic isolation of the host as a determinant of the distribution of subgenotypes of the porcine norovirus genogroup II (GII) genotype 11. Environmental water samples were collected from peri-urban streams and estuaries in South Korea between 2014 and 2020. In total, 488 GII region C sequences of norovirus open reading frame 2 were isolated. A total of 14 genotypes were detected, two of which (GII.11 and GII.18) corresponded to porcine norovirus. Five human norovirus genotypes (GII.2, GII.3, GII.4, GII.6, and GII.17) and one porcine norovirus genotype (GII.11) comprised the subgenotypes. Integrated analysis of seasonal and geographical factors revealed that the possibility of the co-emergence of different GII.11 subgenotypes in the same province was lower than that of human norovirus subgenotypes in the same province. Additional algorithms designed to eliminate potential biases further supported the estimated restricted geographical spread of the GII.11 subgenotypes. Fecal contamination source tracking revealed low detection rates of porcine norovirus in the absence of upstream pig farms. These results suggest that a one-sided viral transmission route, mainly dependent on indirect contact owing to the limited chance of direct contact between geographically separated livestock pig populations, may be responsible for the restricted geographical spread of the GII.11 subgenotypes.

Citations

Citations to this article as recorded by  
  • Swine Norovirus: Past, Present, and Future
    Lara Cavicchio, Andrea Laconi, Alessandra Piccirillo, Maria Serena Beato
    Viruses.2022; 14(3): 537.     CrossRef
Research Support, Non-U.S. Gov'ts
Altered mRNA Levels of MOV10, A3G, and IFN-α in Patients with Chronic Hepatitis B
Zhi-Wei Song , Yan-Xiu Ma , Li-Juan Fu , Bao-qing Fu , Xu Teng , Si-Jia Chen , Wei-Zhen Xu , Hong-Xi Gu
J. Microbiol. 2014;52(6):510-514.   Published online May 29, 2014
DOI: https://doi.org/10.1007/s12275-014-3467-8
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  • 9 Crossref
AbstractAbstract PDF
To explore the relationship of the MOV10, A3G, and IFN-α mRNA levels with chronic hepatitis B virus (HBV) infection, Blood samples from 96 patients with chronic hepatitis B (CHB) and 21 healthy individuals as control were collected. HBV DNA load and aminotransferase in the serum were tested using real time PCR and velocity methods, respectively. The MOV10, A3G, and IFN-α mRNA levels in the peripheral blood mononuclear cells (PBMC) were examined through qRT-PCR. The MOV10, A3G, and IFN-α mRNA levels in CHB group was significantly lower than those in the control group (P<0.01, P<0.05, P<0.01, respectively). The A3G mRNA level in the high-HBV DNA load group was lower than that in the low-HBV DNA load group (P<0.05). However, no statistical difference was found in the MOV10 and IFN-α mRNA levels between the two HBV DNA load groups. Furthermore, the MOV10 mRNA level showed positive correlation with IFN-α in the control group. These results indicated that the expression of the innate immune factors MOV10, A3G, and IFN-α is affected by chronic HBV infection.

Citations

Citations to this article as recorded by  
  • MOV10, a novel immunotherapy and prognostic biomarker, contributes to glioma development by regulating autophagy
    Feiyu Wang, Linlin Ruan, Wenbin Yang, Yueben Hu, Yangzhong Guo, Xuanxuan Xiong, Dan Liu, Qiaoli Lv, Shuhui Chen
    Scientific Reports.2026;[Epub]     CrossRef
  • Hepatic exosomes with declined MiR‐27b‐3p trigger RIG‐I/TBK1 signal pathway in macrophages
    Jie You, Wenyu Wu, Mengxin Lu, Yanghao Xie, Rui Miao, Misi Gu, Dong Xi, Weiming Yan, Di Wu, Xiaojing Wang, Tao Chen, Qin Ning, Meifang Han
    Liver International.2022; 42(7): 1676.     CrossRef
  • Unwinding the roles ofRNAhelicaseMOV10
    Aatiqa Nawaz, Temirlan Shilikbay, Geena Skariah, Stephanie Ceman
    WIREs RNA.2022;[Epub]     CrossRef
  • Evolutionary and Expression Analysis of MOV10 and MOV10L1 Reveals Their Origin, Duplication and Divergence
    Shuaiqi Yang, Xiangmin Zhang, Xianpeng Li, Xiu Yin, Lei Teng, Guangdong Ji, Hongyan Li
    International Journal of Molecular Sciences.2022; 23(14): 7523.     CrossRef
  • Roles of APOBEC3 in hepatitis B virus (HBV) infection and hepatocarcinogenesis
    Yuan Zhang, Xiaorong Chen, Yajuan Cao, Zongguo Yang
    Bioengineered.2021; 12(1): 2074.     CrossRef
  • Profiling of LINE-1-Related Genes in Hepatocellular Carcinoma
    Tomoyuki Honda, Md. Arifur Rahman
    International Journal of Molecular Sciences.2019; 20(3): 645.     CrossRef
  • Host Protein Moloney Leukemia Virus 10 (MOV10) Acts as a Restriction Factor of Influenza A Virus by Inhibiting the Nuclear Import of the Viral Nucleoprotein
    Junsong Zhang, Feng Huang, Likai Tan, Chuan Bai, Bing Chen, Jun Liu, Juanran Liang, Chao Liu, Shaoying Zhang, Gen Lu, Yuan Chen, Hui Zhang, S. López
    Journal of Virology.2016; 90(8): 3966.     CrossRef
  • The role of Moloney leukemia virus 10 in hepatitis B virus expression in hepatoma cells
    Yan-Xiu Ma, Di Li, Li-Juan Fu, Bao-qing Fu, Si-Jia Chen, Wei-Zhen Xu, Xu Teng, Zhi-wei Song, Hong-Xi Gu
    Virus Research.2015; 197: 85.     CrossRef
  • RNA helicase MOV10 functions as a co-factor of HIV-1 Rev to facilitate Rev/RRE-dependent nuclear export of viral mRNAs
    Feng Huang, Junsong Zhang, Yijun Zhang, Guannan Geng, Juanran Liang, Yingniang Li, Jingliang Chen, Chao Liu, Hui Zhang
    Virology.2015; 486: 15.     CrossRef
Hepatitis B Virus Core Interacts with the Host Cell Nucleolar Protein, Nucleophosmin 1
Su Jin Lee , Hee Youn Shim , Antony Hsieh , Ji Young Min , Gu hung Jung
J. Microbiol. 2009;47(6):746-752.   Published online February 4, 2010
DOI: https://doi.org/10.1007/s12275-009-2720-z
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  • 19 Crossref
AbstractAbstract PDF
Hepatitis B virus (HBV) genome replication requires the packaging of viral factors (pregenomic RNA and polymerase) as well as host factors, including heat shock proteins and protein kinase C. Previous reports have suggested that there are several unidentified host factors that affect this encapsidation step. In this study, we identified a new host factor, nucleophosmin (B23) that interacts with the HBV core protein 149 (Cp149). We analyzed this factor using NHS-activated sepharose resin and MALDI-TOF MS. Using the BIAcore analysis system, we were also able to deduce that the B23.1 residues 259-294 were required for the interaction between Cp149 and B23.1 in vitro.

Citations

Citations to this article as recorded by  
  • Nucleophosmin: A Nucleolar Phosphoprotein Orchestrating Cellular Stress Responses
    Mohamed S. Taha, Mohammad Reza Ahmadian
    Cells.2024; 13(15): 1266.     CrossRef
  • Live Cell Imaging Reveals HBV Capsid Translocation from the Nucleus To the Cytoplasm Enabled by Cell Division
    Sofia Romero, Nuruddin Unchwaniwala, Edward L. Evans, Kevin W. Eliceiri, Daniel D. Loeb, Nathan M. Sherer, Haitao Guo, Sara Cherry
    mBio.2023;[Epub]     CrossRef
  • The Hepatitis B Virus Interactome: A Comprehensive Overview
    Ellen Van Damme, Jolien Vanhove, Bryan Severyn, Lore Verschueren, Frederik Pauwels
    Frontiers in Microbiology.2021;[Epub]     CrossRef
  • HBV Core Protein Is in Flux between Cytoplasmic, Nuclear, and Nucleolar Compartments
    Smita Nair, Adam Zlotnick, Ralf Bartenschlager, Stephen P. Goff
    mBio.2021;[Epub]     CrossRef
  • Hepatitis B virus biology and life cycle
    Senko Tsukuda, Koichi Watashi
    Antiviral Research.2020; 182: 104925.     CrossRef
  • Nucleophosmin in Its Interaction with Ligands
    Ilaria Cela, Adele Di Matteo, Luca Federici
    International Journal of Molecular Sciences.2020; 21(14): 4885.     CrossRef
  • Implication of B23/NPM1 in Viral Infections, Potential Uses of B23/NPM1 Inhibitors as Antiviral Therapy
    Yadira Lobaina, Yasser Perera
    Infectious Disorders - Drug Targets.2019; 19(1): 2.     CrossRef
  • Nucleolar Localization of HIV-1 Rev Is Required, Yet Insufficient for Production of Infectious Viral Particles
    Jerlisa Ann C. Arizala, Mayumi Takahashi, John C. Burnett, Dominique L. Ouellet, Haitang Li, John J. Rossi
    AIDS Research and Human Retroviruses.2018; 34(11): 961.     CrossRef
  • Nucleophosmin (NPM1)/B23 in the Proteome of Human Astrocytic Cells Restricts Chikungunya Virus Replication
    Rachy Abraham, Sneha Singh, Sreeja R. Nair, Neha Vijay Hulyalkar, Arun Surendran, Abdul Jaleel, Easwaran Sreekumar
    Journal of Proteome Research.2017; 16(11): 4144.     CrossRef
  • Crosstalk between the nucleolus and the DNA damage response
    L M Ogawa, S J Baserga
    Molecular BioSystems.2017; 13(3): 443.     CrossRef
  • The true story and advantages of the famous Hepatitis B virus core particles: Outlook 2016
    P. Pumpens, E. Grens
    Molecular Biology.2016; 50(4): 489.     CrossRef
  • Biophysical Characterization of Nucleophosmin Interactions with Human Immunodeficiency Virus Rev and Herpes Simplex Virus US11
    Kazem Nouri, Jens M. Moll, Lech-Gustav Milroy, Anika Hain, Radovan Dvorsky, Ehsan Amin, Michael Lenders, Luitgard Nagel-Steger, Sebastian Howe, Sander H. J. Smits, Hartmut Hengel, Lutz Schmitt, Carsten Münk, Luc Brunsveld, Mohammad R. Ahmadian, Michael Ne
    PLOS ONE.2015; 10(12): e0143634.     CrossRef
  • NIRF, a Novel Ubiquitin Ligase, Inhibits Hepatitis B Virus Replication Through Effect on HBV Core Protein and H3 Histones
    Guanhua Qian, Bin Hu, Danlin Zhou, Yanyan Xuan, Lu Bai, Changzhu Duan
    DNA and Cell Biology.2015; 34(5): 327.     CrossRef
  • Bridging the past and the future of virology: Surface plasmon resonance as a powerful tool to investigate virus/host interactions
    Marco Rusnati, Paola Chiodelli, Antonella Bugatti, Chiara Urbinati
    Critical Reviews in Microbiology.2015; 41(2): 238.     CrossRef
  • High throughput proteomic analysis and a comparative review identify the nuclear chaperone, Nucleophosmin among the common set of proteins modulated in Chikungunya virus infection
    Rachy Abraham, Prashant Mudaliar, Abdul Jaleel, Jandhyam Srikanth, Easwaran Sreekumar
    Journal of Proteomics.2015; 120: 126.     CrossRef
  • The Impact of Mass Spectrometry–Based Proteomics on Fundamental Discoveries in Virology
    Todd M. Greco, Benjamin A. Diner, Ileana M. Cristea
    Annual Review of Virology.2014; 1(1): 581.     CrossRef
  • Interaction between nucleophosmin and HBV core protein increases HBV capsid assembly
    Heewon Jeong, Min-Hyung Cho, Sung-Gyoo Park, Guhung Jung
    FEBS Letters.2014; 588(6): 851.     CrossRef
  • NPM1/B23: A Multifunctional Chaperone in Ribosome Biogenesis and Chromatin Remodeling
    Mikael S. Lindström
    Biochemistry Research International.2011; 2011: 1.     CrossRef
  • Biosensing applications of surface plasmon resonance-based Biacore technology
    Subash C.B. Gopinath
    Sensors and Actuators B: Chemical.2010; 150(2): 722.     CrossRef
Affinity Maturation of an Anti-Hepatitis B Virus PreS1 Humanized Antibody by Phage Display
Gi-Hyeok Yang , Sun Ok Yoon , Myung Hee Jang , Hyo Jeong Hong
J. Microbiol. 2007;45(6):528-533.
DOI: https://doi.org/2640 [pii]
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AbstractAbstract PDF
In a previous study we generated an anti-Hepatitis B Virus (HBV) preS1 humanized antibody (HzKR127) that showed in vivo HBV-neutralizing activity in chimpanzees. However, the antigen-binding affinity of the humanized antibody may not be sufficient for clinical use and thus affinity maturation is required for better therapeutic efficacy. In this study, phage display technique was employed to increase the affinity of HzKR127. All six amino acid residues (Glu95-Tyr96-Asp97-Glu98-Ala99-Tyr100) in the heavy (H) chain complementarydetermining region 3 (HCDR3) of HzKR127 were randomized and phage-displayed single chain Fv (scFv) library was constructed. After three rounds of panning, 12 different clones exhibiting higher antigen-binding activity than the wild type ScFv were selected and their antigen-binding specificity for the preS1 confirmed. Subsequently, five ScFv clones were converted to whole IgG and subjected to affinity determination. The results showed that two clones (B3 and A19) exhibited an approximately 6 fold higher affinities than that of HzKR127. The affinity-matured humanized antibodies may be useful in anti-HBV immunotherapy.
Journal Article
Detection of Hepatitis B Virus and Mycobacterium tuberculosis in Korean Dental Patients
Sun-A Lee , So Young Yoo , Kee-Sung Kay , Joong-Ki Kook
J. Microbiol. 2004;42(3):239-242.
DOI: https://doi.org/2082 [pii]
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AbstractAbstract PDF
This study examined the detection rate of the hepatitis B virus (HBV) and Mycobacterium tuberculosis (Mtb) in serum and saliva samples, respectively, from 120 dental patients who were unaware if they have or had either hepatitis or tuberculosis. The frequencies of HBsAg and anti-HBs were determined using an immunochromatic assay. Mtb positivity was determined by the PCR method. Of the 120 patients, 7 (5.8%) were HBV positive and 30 (25.0%) were Mtb positive. This highlights the fact that dental health care workers (DHCWs) can be exposed to the risk of infection from blood- or saliva-borne pathogens as a consequence of their work. Therefore, it is very important to prevent cross infection between patients and dental personnel. Accordingly, laboratory tests prior to surgical treatment are needed to determine the infectious state of dental patients in order to prevent the transmission of infectious diseases in dental clinics.
Rapid and Simple Purification of Biologically Active Human Hepatitis B virus Transactivator-X Proteins
Poo, Ha Ryoung , Kim, Sun Ok , Sohn, Mi Jin , Lee, Sook , Lee, Young Ik
J. Microbiol. 1998;36(1):55-58.
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AbstractAbstract PDF
The human hepatitis B virus-X(HBV-X) was cloned into an expression vector, pET3d, containing a T7 promoter and direct expression was induced in Escherichia coli. The expressed HBV-V protein was purified to homogeneity by centrifugation, ion-exchange chromatography and gel filtration. After gel filtration, renaturation of HBV-X were performed using dialysis against serially diluted urea buffer. The biological activity of refolded HBV-X protein was confirmed by enhancement of protein/DNA complexes using gel-shift analysis.

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