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Function of VP2 Protein in the Stability of the Secondary Structure of Virus-like Particles of Genogroup II Norovirus at Different pH Levels: Function of VP2 Protein in the Stability of NoV VLPs
Yao Lin , Li Fengling , Wang Lianzhu , Zhai Yuxiu , Jiang Yanhua
J. Microbiol. 2014;52(11):970-975.   Published online October 3, 2014
DOI: https://doi.org/10.1007/s12275-014-4323-6
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  • 32 Crossref
AbstractAbstract PDF
VP2 is the minor structural protein of noroviruses (NoV) and may function in NoV particle stability. To determine the function of VP2 in the stability of the NoV particle, we constructed and purified two kinds of virus-like particles (VLPs), namely, VLPs (VP1) and VLPs (VP1+VP2), from Sf9 cells infected with recombinant baculoviruses by using a Bac-to-Bac? baculovirus expression system. The two kinds of VLPs were treated with different phosphate buffers (pH 2 to pH 8); the secondary structure was then analyzed by far UV circular dichroism (CD) spectroscopy. Results showed that significant disruptions of the secondary structure of proteins were not observed at pH 2 to pH 7. At pH 8, the percentages of α-helix, β-sheet, and β-turn in VLPs (VP1) were decreased from 11% to 8%, from 37% to 32%, and from 20% to 16%, respectively. The percentage of coil was increased from 32% to 44%. By contrast, the percentages of α-helix, β-sheet, and β-turn in VLPs (VP1+VP2) were decreased from 11% to 10%, from 37% to 35%, and from 20% to 19%, respectively. The percentage of coil was increased from 32% to 36%. VLPs (VP1+VP2) was likely more stable than VLPs (VP1), as indicated by the percentage of the secondary structures analyzed by CD. These results suggested that VP2 could stabilize the secondary structure of VLPs under alkaline pH conditions. This study provided novel insights into the molecular mechanism of the function of VP2 in the stability of NoV particles.

Citations

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  • Genomic diversity and comparative phylogenomic analysis of genus Norovirus
    Huijeong Doh, Changhyeon Lee, Nam Yee Kim, Yun-Yong Park, Eun-jeong Kim, Changsun Choi, Seong-il Eyun
    Scientific Reports.2025;[Epub]     CrossRef
  • Progress and challenges in thermal inactivation of norovirus in oysters
    Razieh Sadat Mirmahdi, Naim Montazeri
    Critical Reviews in Food Science and Nutrition.2025; : 1.     CrossRef
  • Advances in human norovirus research: Vaccines, genotype distribution and antiviral strategies
    JunLi Chen, ZhengChao Cheng, Jing Chen, Lingling Qian, Haoran Wang, YuWei Liu
    Virus Research.2024; 350: 199486.     CrossRef
  • GII.6 norovirus major capsid protein VP1 derived from distinct clusters induce cross-blocking effects
    Jie Ma, Jinjin Liu, Chaohong Fu, Yuqi Huo
    Infection, Genetics and Evolution.2024; 122: 105617.     CrossRef
  • Production of infectious reporter murine norovirus by VP2 trans -complementation
    Ryoka Ishiyama, Kazuhiro Yoshida, Kazuki Oikawa, Reiko Takai-Todaka, Akiko Kato, Kumiko Kanamori, Akira Nakanishi, Kei Haga, Kazuhiko Katayama, Christiane E. Wobus
    Journal of Virology.2024;[Epub]     CrossRef
  • Out-of-sync evolutionary patterns and mutual interplay of major and minor capsid proteins in norovirus GII.2
    Ruiquan Xu, Liang Xue, Jingmin Wang, Yiqing Chen, Yingwen Cao, Junshan Gao, Hui Gao, Qingyao Du, Xiaoxia Kou, Lin Yu
    Journal of General Virology .2024;[Epub]     CrossRef
  • Characteristics of Norovirus capsid protein-specific CD8 + T-Cell responses in previously infected individuals
    Taojun He, Yilin Deng, Fang Zhang, Jin Zhang, Luhong Zhu, Qinjin Wang, Jie Ning, Hui Wu, Hanmei Yuan, Bin Li, Chao Wu
    Virulence.2024;[Epub]     CrossRef
  • Near-atomic structures of RHDV reveal insights into capsid assembly and different conformations between mature virion and VLP
    Zhiyang Ruan, Qianqian Shao, Yanhua Song, Bo Hu, Zhiyu Fan, Houjun Wei, Yunshu Liu, Fang Wang, Qianglin Fang, Christiane E. Wobus
    Journal of Virology.2024;[Epub]     CrossRef
  • High yield production of norovirus GII.4 virus-like particles using silkworm pupae and evaluation of their protective immunogenicity
    Akitsu Masuda, Jae Man Lee, Takeshi Miyata, Shintaro Sato, Atsushi Masuda, Masahiro Taniguchi, Ryosuke Fujita, Hiroshi Ushijima, Keisuke Morimoto, Takeru Ebihara, Masato Hino, Kohei Kakino, Hiroaki Mon, Takahiro Kusakabe
    Vaccine.2023; 41(3): 766.     CrossRef
  • Biological and physico-chemical characterization of human norovirus-like particles under various environmental conditions
    Nicole Abou-Hamad, Marie Estienney, Rémi Chassagnon, Marjorie Bon, Philippe Daval-Frerot, Alexis de Rougemont, Stéphane Guyot, Frédéric Bouyer, Gaël Belliot
    Colloids and Surfaces B: Biointerfaces.2023; 231: 113545.     CrossRef
  • Linear epitopes on the capsid protein of norovirus commonly elicit high antibody response among past-infected individuals
    Yilin Deng, Taojun He, Bin Li, Hanmei Yuan, Fang Zhang, Hui Wu, Jie Ning, Yanping Zhang, Aixia Zhai, Chao Wu
    Virology Journal.2023;[Epub]     CrossRef
  • Development and efficacy evaluation of remodeled canine parvovirus-like particles displaying major antigenic epitopes of a giant panda derived canine distemper virus
    Shan Zhao, Xinfeng Han, Yifei Lang, Yue Xie, Zhijie Yang, Qin Zhao, Yiping Wen, Jing Xia, Rui Wu, Xiaobo Huang, Yong Huang, Sanjie Cao, Jingchao Lan, Li Luo, Qigui Yan
    Frontiers in Microbiology.2023;[Epub]     CrossRef
  • Infant antibody and B-cell responses following confirmed pediatric GII.17 norovirus infections functionally distinguish GII.17 genetic clusters
    Camilla A. Strother, Paul D. Brewer-Jensen, Sylvia Becker-Dreps, Omar Zepeda, Samantha May, Fredman Gonzalez, Yaoska Reyes, Benjamin D. McElvany, April M. Averill, Michael L. Mallory, Anna M. Montmayeur, Verónica P. Costantini, Jan Vinjé, Ralph S. Baric,
    Frontiers in Immunology.2023;[Epub]     CrossRef
  • The VP2 protein exhibits cross-interaction to the VP1 protein in norovirus GII.17
    Yingyin Liao, Linping Wang, Xiaojing Hong, Junshan Gao, Yueting Zuo, Yanhui Liang, Yueting Jiang, Jumei Zhang, Aiwu Wu, Liang Xue, Xiaoxia Kou
    Infection, Genetics and Evolution.2022; 100: 105265.     CrossRef
  • Epochal Coevolution of Minor Capsid Protein in Norovirus Gii.4 Variants with Major Capsid Protein Based on Their Interactions Over the Last Five Decades
    Xiaoxia Kou, Xiaojing Hong, Liang Xue, Junshan Gao, Yueting Jiang
    SSRN Electronic Journal .2022;[Epub]     CrossRef
  • First Detection and Genomic Characterization of Bovine Norovirus from Yak
    Yuchen Cui, Xi Chen, Hua Yue, Cheng Tang
    Pathogens.2022; 11(2): 192.     CrossRef
  • Atomic Structure of the Human Sapovirus Capsid Reveals a Unique Capsid Protein Conformation in Caliciviruses
    Naoyuki Miyazaki, Chihong Song, Tomoichiro Oka, Motohiro Miki, Kosuke Murakami, Kenji Iwasaki, Kazuhiko Katayama, Kazuyoshi Murata, Rebecca Ellis Dutch
    Journal of Virology.2022;[Epub]     CrossRef
  • Noroviruses—The State of the Art, Nearly Fifty Years after Their Initial Discovery
    Louisa F. Ludwig-Begall, Axel Mauroy, Etienne Thiry
    Viruses.2021; 13(8): 1541.     CrossRef
  • Immunogenicity and protective potency of Norovirus GII.17 virus-like particle-based vaccine
    Wei Chen, Tao Kang, Rongliang Yuan, Congwen Shao, Shenrong Jing
    Biotechnology Letters.2020; 42(7): 1211.     CrossRef
  • Review Norovirus
    Kazuhiko KATAYAMA
    Uirusu.2020; 70(2): 117.     CrossRef
  • Characterization of the complete genome sequence of the recombinant norovirus GII.P16/GII.4_Sydney_2012 revealed in Russia
    E. V. Zhirakovskaia, A. Y. Tikunov, S. N. Sokolov, B. I. Kravchuk, E. I. Krasnova, N. V. Tikunova
    Vavilov Journal of Genetics and Breeding.2020; 24(1): 69.     CrossRef
  • Human Norovirus Proteins: Implications in the Replicative Cycle, Pathogenesis, and the Host Immune Response
    Claudia P. Campillay-Véliz, Jonatan J. Carvajal, Andrea M. Avellaneda, Darling Escobar, Camila Covián, Alexis M. Kalergis, Margarita K. Lay
    Frontiers in Immunology.2020;[Epub]     CrossRef
  • Genomics Analyses of GIV and GVI Noroviruses Reveal the Distinct Clustering of Human and Animal Viruses
    Lauren A. Ford-Siltz, Lisa Mullis, Yasser M. Sanad, Kentaro Tohma, Cara J. Lepore, Marli Azevedo, Gabriel I. Parra
    Viruses.2019; 11(3): 204.     CrossRef
  • Prevalence and complete genome of bovine norovirus with novel VP1 genotype in calves in China
    Yuelin Wang, Hua Yue, Cheng Tang
    Scientific Reports.2019;[Epub]     CrossRef
  • The coordinating role of the human norovirus minor capsid protein VP2 is essential to functional change and nuclear localization of the major capsid protein VP1
    Zhili Liu, Min Zhang, Zhen Shen, Huifen Chen, Wanju Zhang, Xiaoqing Xu, Zelin Lai, Wenqin Sun, Zheng Zhao, Jun Zhang
    Archives of Virology.2019; 164(4): 1173.     CrossRef
  • Free-Chlorine Disinfection as a Selection Pressure on Norovirus
    Andri Taruna Rachmadi, Masaaki Kitajima, Kozo Watanabe, Sakiko Yaegashi, Joeselle Serrana, Arata Nakamura, Toyoko Nakagomi, Osamu Nakagomi, Kazuhiko Katayama, Satoshi Okabe, Daisuke Sano, Christopher A. Elkins
    Applied and Environmental Microbiology.2018;[Epub]     CrossRef
  • Norovirus assembly and stability
    Ronja Pogan, Jasmin Dülfer, Charlotte Uetrecht
    Current Opinion in Virology.2018; 31: 59.     CrossRef
  • pH-Dependence of RNA Extraction for Norovirus by TRIzol Method
    Deok-Young Jhon
    Journal of Food Hygiene and Safety.2018; 33(1): 71.     CrossRef
  • Persistence and Elimination of Human Norovirus in Food and on Food Contact Surfaces: A Critical Review
    Nigel Cook, Angus Knight, Gary P. Richards
    Journal of Food Protection.2016; 79(7): 1273.     CrossRef
  • Norovirus mechanisms of immune antagonism
    Alexa N Roth, Stephanie M Karst
    Current Opinion in Virology.2016; 16: 24.     CrossRef
  • Infection models of human norovirus: challenges and recent progress
    Sangdo Ha, In-Soo Choi, Changsun Choi, Jinjong Myoung
    Archives of Virology.2016; 161(4): 779.     CrossRef
  • Norovirus Vaccines and Potential Antinorovirus Drugs: Recent Advances and Future Perspectives
    Jacob Kocher, Lijuan Yuan
    Future Virology.2015; 10(7): 899.     CrossRef
Fine Mapping of a Foot-and-Mouth Disease Virus Epitope Recognized by Serotype-Independent Monoclonal Antibody 4B2
Yongzhong Yu , Haiwei Wang , Lei Zhao , Chunyuan Zhang , Zhigang Jiang , Li Yu
J. Microbiol. 2011;49(1):94-101.   Published online March 3, 2011
DOI: https://doi.org/10.1007/s12275-011-0134-1
  • 219 View
  • 0 Download
  • 26 Crossref
AbstractAbstract PDF
VP2 is a structural protein of the foot-and-mouth disease virus (FMDV). In this study, a FMDV serotype-independent monoclonal antibody (MAb), 4B2, was generated. By screening a phage-displayed random 12-peptide library, we found positive phages displaying the consensus motif ETTXLE (X is any amino acid (aa)), which is highly homologous to 6ETTLLE11 at the N-terminus of the VP2 protein. Subsequently, a series of GST-fusion proteins expressing a truncated N-terminus of VP2 were examined by western blot analysis using the MAb 4B2. The results indicated that the motif 6ETTLLE11 of VP2 may be the minimal requirement of the epitope recognized by 4B2. Moreover, a 12-aa peptide 2KKTEETTLLEDR13 was shown to be the minimal unit of the epitope with maximal binding activity to 4B2. Alanine-scanning analysis demonstrated thatThr7, Thr8, and Leu10 are the functional residues of the 4B2 epitope Glu6 and Leu9 are required residues, and Glu11 plays a crucial role in the binding of MAb 4B2. The fine mapping of the epitope indicated that MAb 4B2 has the potential to be used in FMDV diagnosis.

Citations

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  • Identification of Conserved Linear Epitopes on Viral Protein 2 of Foot-and-Mouth Disease Virus Serotype O by Monoclonal Antibodies 6F4.D11.B6 and 8D6.B9.C3
    Wantanee Tommeurd, Kanyarat Thueng-in, Sirin Theerawatanasirikul, Nongnaput Tuyapala, Sukontip Poonsuk, Nantawan Petcharat, Nattarat Thangthamniyom, Porntippa Lekcharoensuk
    Antibodies.2024; 13(3): 67.     CrossRef
  • In Silico characterization of single-chain variable fragment antibodies targeting Foot-and-Mouth disease virus
    Fatema Akter, Manisha Medhi, S.L. Katrapati, Pankaj Dhakarwal, M. Hosamani, SH Basagoudanavar, M. A. Ramakrishnan, V Bhanuprakash, Pallab Chaudhuri, Dhanavelu Muthuchelvan
    Indian Journal of Veterinary Research (The).2024; 33(1): 8.     CrossRef
  • Heterogeneous Nuclear Ribonucleoprotein L Negatively Regulates Foot-and-Mouth Disease Virus Replication through Inhibition of Viral RNA Synthesis by Interacting with the Internal Ribosome Entry Site in the 5′ Untranslated Region
    Chao Sun, Mengmeng Liu, Jitao Chang, Decheng Yang, Bo Zhao, Haiwei Wang, Guohui Zhou, Changjiang Weng, Li Yu, Susana López
    Journal of Virology.2020;[Epub]     CrossRef
  • Diagnostic and Epitope Mapping Potential of Single-Chain Antibody Fragments Against Foot-and-Mouth Disease Virus Serotypes A, SAT1, and SAT3
    Melanie Chitray, Pamela Anne Opperman, Lia Rotherham, Jeanni Fehrsen, Wouter van Wyngaardt, Janine Frischmuth, Elizabeth Rieder, Francois Frederick Maree
    Frontiers in Veterinary Science.2020;[Epub]     CrossRef
  • hnRNP K Is a Novel Internal Ribosomal Entry Site-Transacting Factor That Negatively Regulates Foot-and-Mouth Disease Virus Translation and Replication and Is Antagonized by Viral 3C Protease
    Wenming Liu, Decheng Yang, Chao Sun, Haiwei Wang, Bo Zhao, Guohui Zhou, Li Yu, Julie K. Pfeiffer
    Journal of Virology.2020;[Epub]     CrossRef
  • A Temperature-Dependent Translation Defect Caused by Internal Ribosome Entry Site Mutation Attenuates Foot-and-Mouth Disease Virus: Implications for Rational Vaccine Design
    Decheng Yang, Chao Sun, Rongyuan Gao, Haiwei Wang, Wenming Liu, Kewei Yu, Guohui Zhou, Bo Zhao, Li Yu, Susana López
    Journal of Virology.2020;[Epub]     CrossRef
  • Eight novel single chain antibody fragments recognising VP2 of foot-and-mouth disease virus serotypes A, O, and SAT 2
    Reda Salem, Alaa A. El-Kholy, Mohamed Ibrahim
    Virology.2019; 533: 145.     CrossRef
  • Structural Features of a Conformation-dependent Antigen Epitope on ORFV-B2L Recognized by the 2E4 mAb
    Yongzhong Yu, Wenbo Zhao, Qiang Tan, Xue Zhang, Mengyao Wang, Xuyang Duan, Yuanyuan Liu, Zhijun Wu, Jinzhu Ma, Baifen Song, Rui Zhao, Kui Zhao, Zhengxing Lian, Yudong Cui
    Scientific Reports.2019;[Epub]     CrossRef
  • Cleavages at the three junctions within the foot-and-mouth disease virus capsid precursor (P1–2A) by the 3C protease are mutually independent
    Thea Kristensen, Joseph Newman, Su Hua Guan, Tobias J. Tuthill, Graham J. Belsham
    Virology.2018; 522: 260.     CrossRef
  • Modifications to the Foot-and-Mouth Disease Virus 2A Peptide: Influence on Polyprotein Processing and Virus Replication
    Jonas Kjær, Graham J. Belsham, Tom Gallagher
    Journal of Virology.2018;[Epub]     CrossRef
  • Identification of a protective B-cell epitope of the Staphylococcus aureus GapC protein by screening a phage-displayed random peptide library
    Mengyao Wang, Lu Zhai, Wei Yu, Yuhua Wei, Lizi Wang, Shuo Liu, Wanyu Li, Xiaoting Li, Simiao Yu, Xiaoting Chen, Hua Zhang, Jing Chen, Zhenyue Feng, Liquan Yu, Yudong Cui, Paulo Lee Ho
    PLOS ONE.2018; 13(1): e0190452.     CrossRef
  • Identification of a conserved conformational epitope in the VP2 protein of foot-and-mouth disease virus
    Wenming Liu, Baolin Yang, Mingxia Wang, Weifeng Liang, Haiwei Wang, Decheng Yang, Wenge Ma, Guohui Zhou, Li Yu
    Archives of Virology.2017; 162(7): 1877.     CrossRef
  • Identification of a serotype-independent linear epitope of foot-and-mouth disease virus
    Baolin Yang, Mingxia Wang, Wenming Liu, Zhiqiang Xu, Haiwei Wang, Decheng Yang, Wenge Ma, Guohui Zhou, Li Yu
    Archives of Virology.2017; 162(12): 3875.     CrossRef
  • Determinants of the VP1/2A junction cleavage by the 3C protease in foot-and-mouth disease virus-infected cells
    Thea Kristensen, Preben Normann, Maria Gullberg, Ulrik Fahnøe, Charlotta Polacek, Thomas Bruun Rasmussen, Graham J Belsham
    Journal of General Virology .2017; 98(3): 385.     CrossRef
  • Identification of a conformational neutralizing epitope on the VP1 protein of type A foot-and-mouth disease virus
    Wenming Liu, Baolin Yang, Mingxia Wang, Haiwei Wang, Decheng Yang, Wenge Ma, Guohui Zhou, Li Yu
    Research in Veterinary Science.2017; 115: 374.     CrossRef
  • Separation of foot-and-mouth disease virus leader protein activities; identification of mutants that retain efficient self-processing activity but poorly induce eIF4G cleavage
    Su Hua Guan, Graham J Belsham
    Journal of General Virology.2017; 98(4): 671.     CrossRef
  • Identification of a conserved linear epitope using a monoclonal antibody against non-structural protein 3B of foot-and-mouth disease virus
    Chaosi Li, Weifeng Liang, Wenming Liu, Decheng Yang, Haiwei Wang, Wenge Ma, Guohui Zhou, Li Yu
    Archives of Virology.2016; 161(2): 365.     CrossRef
  • Identification of a conserved linear neutralizing epitope recognized by monoclonal antibody 9A9 against serotype A foot-and-mouth disease virus
    Weifeng Liang, Guohui Zhou, Wenming Liu, Baolin Yang, Chaosi Li, Haiwei Wang, Decheng Yang, Wenge Ma, Li Yu
    Archives of Virology.2016; 161(10): 2705.     CrossRef
  • Modification of the internal ribosome entry site element impairs the growth of foot-and-mouth disease virus in porcine-derived cells
    Chao Sun, Decheng Yang, Rongyuan Gao, Te Liang, Haiwei Wang, Guohui Zhou, Li Yu
    Journal of General Virology.2016; 97(4): 901.     CrossRef
  • Identification of a Conserved Linear B-Cell Epitope of Streptococcus dysgalactiae GapC Protein by Screening Phage-Displayed Random Peptide Library
    Limeng Zhang, Hua Zhang, Ziyao Fan, Xue Zhou, Liquan Yu, Hunan Sun, Zhijun Wu, Yongzhong Yu, Baifen Song, Jinzhu Ma, Chunyu Tong, Xintong Wang, Zhanbo Zhu, Yudong Cui, Mitchell Ho
    PLOS ONE.2015; 10(6): e0131221.     CrossRef
  • Sequence adaptations affecting cleavage of the VP1/2A junction by the 3C protease in foot-and-mouth disease virus-infected cells
    Maria Gullberg, Charlotta Polacek, Graham J. Belsham
    Journal of General Virology .2014; 95(11): 2402.     CrossRef
  • Processing of the VP1/2A Junction Is Not Necessary for Production of Foot-and-Mouth Disease Virus Empty Capsids and Infectious Viruses: Characterization of “Self-Tagged” Particles
    Maria Gullberg, Charlotta Polacek, Anette Bøtner, Graham J. Belsham
    Journal of Virology.2013; 87(21): 11591.     CrossRef
  • Recombinant adenovirus expressing type Asia1 foot-and-mouth disease virus capsid proteins induces protective immunity against homologous virus challenge in mice
    Guohui Zhou, Haiwei Wang, Fang Wang, Li Yu
    Research in Veterinary Science.2013; 94(3): 796.     CrossRef
  • Assembly and characterization of foot-and-mouth disease virus empty capsid particles expressed within mammalian cells
    Maria Gullberg, Bartosz Muszynski, Lindsey J. Organtini, Robert E. Ashley, Susan L. Hafenstein, Graham J. Belsham, Charlotta Polacek
    Journal of General Virology .2013; 94(8): 1769.     CrossRef
  • Insertion of type O-conserved neutralizing epitope into the foot-and-mouth disease virus type Asia1 VP1 G-H loop: effect on viral replication and neutralization phenotype
    Haiwei Wang, Mei Xue, Decheng Yang, Guohui Zhou, Donglai Wu, Li Yu
    Journal of General Virology .2012; 93(7): 1442.     CrossRef
  • Effects of amino acid substitutions in the VP2 B-C loop on antigenicity and pathogenicity of serotype Asia1 foot-and-mouth disease virus
    Mei Xue, Haiwei Wang, Wan Li, Guohui Zhou, Yabin Tu, Li Yu
    Virology Journal.2012;[Epub]     CrossRef

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