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Journal articles on the topic 'Non-structural proteins'

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Author: Grafiati

Published: 4 June 2021

Last updated: 6 September 2023

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1

Zeidler, Julianna, Lorena Fernandes-Siqueira, Glauce Barbosa, and Andrea Da Poian. "Non-Canonical Roles of Dengue Virus Non-Structural Proteins." Viruses 9, no. 3 (March 13, 2017): 42. http://dx.doi.org/10.3390/v9030042.

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2

Petric, M., R. H. Yolken, E. J. Dubovi, M. Wiskerchen, and M. S. Collett. "Baculovirus expression of pestivirus non-structural proteins." Journal of General Virology 73, no. 7 (July 1, 1992): 1867–71. http://dx.doi.org/10.1099/0022-1317-73-7-1867.

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3

Hu, Liya, Sue E. Crawford, Joseph M. Hyser, Mary K. Estes, and BV Venkataram Prasad. "Rotavirus non-structural proteins: structure and function." Current Opinion in Virology 2, no. 4 (August 2012): 380–88. http://dx.doi.org/10.1016/j.coviro.2012.06.003.

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4

Tam, Donald, Ana C. Lorenzo-Leal, Luis Ricardo Hernández, and Horacio Bach. "Targeting SARS-CoV-2 Non-Structural Proteins." International Journal of Molecular Sciences 24, no. 16 (August 20, 2023): 13002. http://dx.doi.org/10.3390/ijms241613002.

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Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is an enveloped respiratory β coronavirus that causes coronavirus disease (COVID-19), leading to a deadly pandemic that has claimed millions of lives worldwide. Like other coronaviruses, the SARS-CoV-2 genome also codes for non-structural proteins (NSPs). These NSPs are found within open reading frame 1a (ORF1a) and open reading frame 1ab (ORF1ab) of the SARS-CoV-2 genome and encode NSP1 to NSP11 and NSP12 to NSP16, respectively. This study aimed to collect the available literature regarding NSP inhibitors. In addition, we searched the natural product database looking for similar structures. The results showed that similar structures could be tested as potential inhibitors of the NSPs.

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5

Rohaim, Mohammed A., Rania F. El Naggar, Emily Clayton, and Muhammad Munir. "Structural and functional insights into non-structural proteins of coronaviruses." Microbial Pathogenesis 150 (January 2021): 104641. http://dx.doi.org/10.1016/j.micpath.2020.104641.

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6

Pressman, E. K. "Heterocomplexes of tick-borne encephalitis structural and non-structural proteins." FEBS Letters 333, no. 3 (November 1, 1993): 268–70. http://dx.doi.org/10.1016/0014-5793(93)80667-j.

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7

Essen, Lars-Oliver. "Structural genomics of “non-standard” proteins: a chance for membrane proteins?" Gene Function & Disease 3, no. 12 (October 2002): 39–48. http://dx.doi.org/10.1002/1438-826x(200210)3:1/2<39::aid-gnfd39>3.0.co;2-6.

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8

Kaščáková, Barbora, Zdenek Franta, Zdeno Gardian, Ivana Kutá Smatanová, and Roman Tůma. "Molecular biology and structural study of avian orthoreovirus non-structural proteins." Acta Crystallographica Section A Foundations and Advances 77, a2 (August 14, 2021): C853. http://dx.doi.org/10.1107/s0108767321088450.

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9

Joachimiak, Andrzej, Changsoo Chang, Michael Endres, Robert Jedrzejczak, Youngchang Kim, Natalia Maltseva, Karolina Michalska, et al. "Crystallography of SARS-CoV-2 non-structural proteins." Acta Crystallographica Section A Foundations and Advances 76, a1 (August 2, 2020): a217. http://dx.doi.org/10.1107/s0108767320097858.

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10

Yan, Jing, Jianlin Cheng, Lukasz Kurgan, and Vladimir N. Uversky. "Structural and functional analysis of “non-smelly” proteins." Cellular and Molecular Life Sciences 77, no. 12 (September 5, 2019): 2423–40. http://dx.doi.org/10.1007/s00018-019-03292-1.

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11

Xia, Ning-Shao, Hai-Jie Yang, Jun Zhang, Chang-Qing Lin, Ying-Bin Wang, Juan Wang, Mei-Yun Zhan, and MH Ng. "Prokaryotical expression of structural and non-structural proteins of hepatitis G virus." World Journal of Gastroenterology 7, no. 5 (2001): 642. http://dx.doi.org/10.3748/wjg.7.5.642.

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12

Xia, Ning-Shao, Hai-Jie Yang, Jun Zhang, Chang-Qing Lin, Ying-Bin Wang, Juan Wang, Mei-Yun Zhan, and MH Ng. "Prokaryotical expression of structural and non-structural proteins of hepatitis G virus." World Journal of Gastroenterology 7, no. 5 (2001): 642. http://dx.doi.org/10.3748/wjg.7.642.

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13

Xia, Ning-Shao, Hai-Jie Yang, Jun Zhang, Chang-Qing Lin, Ying-Bin Wang, Juan Wang, Mei-Yun Zhan, and MH Ng. "Prokaryotical expression of structural and non-structural proteins of hepatitis G virus." World Journal of Gastroenterology 7, no. 5 (2001): 642. http://dx.doi.org/10.3748/wjg.v7.i5.642.

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14

Chen, Shun, Zhen Wu, Mingshu Wang, and Anchun Cheng. "Innate Immune Evasion Mediated by Flaviviridae Non-Structural Proteins." Viruses 9, no. 10 (October 7, 2017): 291. http://dx.doi.org/10.3390/v9100291.

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15

Andreeva, Antonina, Andreas Prlić, Tim J. P. Hubbard, and Alexey G. Murzin. "SISYPHUS—structural alignments for proteins with non-trivial relationships." Nucleic Acids Research 35, suppl_1 (October 26, 2006): D253—D259. http://dx.doi.org/10.1093/nar/gkl746.

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16

Chakraborty, Asit Kumar. "Multi-Alignment Comparison of Coronavirus Non-Structural Proteins Nsp13- Nsp16 with Ribosomal Proteins and other DNA/RNA Modifying Enzymes Suggested their Roles in the Regulation of Host Protein Synthesis." International Journal of Clinical & Medical Informatics 3, no. 1 (June 1, 2020): 7–19. http://dx.doi.org/10.46619/ijcmi.2020.1024.

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17

Golubeva, Volha A., Thales C. Nepomuceno, Giuliana de Gregoriis, Rafael D. Mesquita, Xueli Li, Sweta Dash, Patrícia P. Garcez, et al. "Network of Interactions between ZIKA Virus Non-Structural Proteins and Human Host Proteins." Cells 9, no. 1 (January 8, 2020): 153. http://dx.doi.org/10.3390/cells9010153.

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The Zika virus (ZIKV) is a mosquito-borne Flavivirus and can be transmitted through an infected mosquito bite or through human-to-human interaction by sexual activity, blood transfusion, breastfeeding, or perinatal exposure. After the 2015–2016 outbreak in Brazil, a strong link between ZIKV infection and microcephaly emerged. ZIKV specifically targets human neural progenitor cells, suggesting that proteins encoded by ZIKV bind and inactivate host cell proteins, leading to microcephaly. Here, we present a systematic annotation of interactions between human proteins and the seven non-structural ZIKV proteins corresponding to a Brazilian isolate. The interaction network was generated by combining tandem-affinity purification followed by mass spectrometry with yeast two-hybrid screens. We identified 150 human proteins, involved in distinct biological processes, as interactors to ZIKV non-structural proteins. Our interacting network is composed of proteins that have been previously associated with microcephaly in human genetic disorders and/or animal models. Further, we show that the protein inhibitor of activated STAT1 (PIAS1) interacts with NS5 and modulates its stability. This study builds on previously published interacting networks of ZIKV and genes related to autosomal recessive primary microcephaly to generate a catalog of human cellular targets of ZIKV proteins implicated in processes related to microcephaly in humans. Collectively, these data can be used as a resource for future characterization of ZIKV infection biology and help create a basis for the discovery of drugs that may disrupt the interaction and reduce the health damage to the fetus.

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18

Khasnatinov, Maxim A., Andrew Tuplin, Dmitri J. Gritsun, Mirko Slovak, Maria Kazimirova, Martina Lickova, Sabina Havlikova, et al. "Tick-Borne Encephalitis Virus Structural Proteins Are the Primary Viral Determinants of Non-Viraemic Transmission between Ticks whereas Non-Structural Proteins Affect Cytotoxicity." PLOS ONE 11, no. 6 (June 24, 2016): e0158105. http://dx.doi.org/10.1371/journal.pone.0158105.

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19

Sawada, Kengo, Shintaro Minami, and Geroge Chijenji. "2PT004 Common structural / sequence features of proteins that share non-sequential structural similarity(The 50th Annual Meeting of the Biophysical Society of Japan)." Seibutsu Butsuri 52, supplement (2012): S120. http://dx.doi.org/10.2142/biophys.52.s120_2.

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20

Baumann, Alexander, Lukas Pfeifer, and Birgit Classen. "Arabinogalactan-proteins from non-coniferous gymnosperms have unusual structural features." Carbohydrate Polymers 261 (June 2021): 117831. http://dx.doi.org/10.1016/j.carbpol.2021.117831.

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21

Hao, Wenzhuo, Lingyan Wang, and Shitao Li. "Roles of the Non-Structural Proteins of Influenza A Virus." Pathogens 9, no. 10 (October 3, 2020): 812. http://dx.doi.org/10.3390/pathogens9100812.

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Influenza A virus (IAV) is a segmented, negative single-stranded RNA virus that causes seasonal epidemics and has a potential for pandemics. Several viral proteins are not packed in the IAV viral particle and only expressed in the infected host cells. These proteins are named non-structural proteins (NSPs), including NS1, PB1-F2 and PA-X. They play a versatile role in the viral life cycle by modulating viral replication and transcription. More importantly, they also play a critical role in the evasion of the surveillance of host defense and viral pathogenicity by inducing apoptosis, perturbing innate immunity, and exacerbating inflammation. Here, we review the recent advances of these NSPs and how the new findings deepen our understanding of IAV–host interactions and viral pathogenesis.

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22

Eifan, Saleh, Esther Schnettler, Isabelle Dietrich, Alain Kohl, and Anne-Lie Blomström. "Non-Structural Proteins of Arthropod-Borne Bunyaviruses: Roles and Functions." Viruses 5, no. 10 (October 4, 2013): 2447–68. http://dx.doi.org/10.3390/v5102447.

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23

Teterina, Natalya L., Chris Lauber, Kenneth S. Jensen, Eric A. Levenson, Alexander E. Gorbalenya, and Ellie Ehrenfeld. "Identification of tolerated insertion sites in poliovirus non-structural proteins." Virology 409, no. 1 (January 2011): 1–11. http://dx.doi.org/10.1016/j.virol.2010.09.028.

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24

Solanki, Vandana, Monalisa Tiwari, and Vishvanath Tiwari. "Immunoinformatic approach to design a multiepitope vaccine targeting non-mutational hotspot regions of structural and non-structural proteins of the SARS CoV2." PeerJ 9 (March 23, 2021): e11126. http://dx.doi.org/10.7717/peerj.11126.

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Background The rapid Severe Acute Respiratory Syndrome Coronavirus 2 (SARS CoV2) outbreak caused severe pandemic infection worldwide. The high mortality and morbidity rate of SARS CoV2 is due to the unavailability of vaccination and mutation in this virus. The present article aims to design a potential vaccine construct VTC3 targeting the non-mutational region of structural and non-structural proteins of SARS CoV2. Methods In this study, vaccines were designed using subtractive proteomics and reverse vaccinology. To target the virus adhesion and evasion, 10 different structural and non-structural proteins have been selected. Shortlisted proteins have been screened for B cell, T cell and IFN gamma interacting epitopes. 3D structure of vaccine construct was modeled and evaluated for its physicochemical properties, immunogenicity, allergenicity, toxicity and antigenicity. The finalized construct was implemented for docking and molecular dynamics simulation (MDS) with different toll-like receptors (TLRs) and human leukocyte antigen (HLA). The binding energy and dissociation construct of the vaccine with HLA and TLR was also calculated. Mutational sensitivity profiling of the designed vaccine was performed, and mutations were reconfirmed from the experimental database. Antibody production, clonal selection, antigen processing, immune response and memory generation in host cells after injection of the vaccine was also monitored using immune simulation. Results Subtractive proteomics identified seven (structural and non-structural) proteins of this virus that have a role in cell adhesion and infection. The different epitopes were predicted, and only extracellular epitopes were selected that do not have similarity and cross-reactivity with the host cell. Finalized epitopes of all proteins with minimum allergenicity and toxicity were joined using linkers to designed different vaccine constructs. Docking different constructs with different TLRs and HLA demonstrated a stable and reliable binding affinity of VTC3 with the TLRs and HLAs. MDS analysis further confirms the interaction of VTC3 with HLA and TLR1/2 complex. The VTC3 has a favorable binding affinity and dissociation constant with HLA and TLR. The VTC3 does not have similarities with the human microbiome, and most of the interacting residues of VTC3 do not have mutations. The immune simulation result showed that VTC3 induces a strong immune response. The present study designs a multiepitope vaccine targeting the non-mutational region of structural and non-structural proteins of the SARS CoV2 using an immunoinformatic approach, which needs to be experimentally validated.

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25

Mohl, Bjorn-Patrick, Adeline Kerviel, Thomas Labadie, Eiko Matsuo, and Polly Roy. "Differential Localization of Structural and Non-Structural Proteins during the Bluetongue Virus Replication Cycle." Viruses 12, no. 3 (March 20, 2020): 343. http://dx.doi.org/10.3390/v12030343.

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Members of the Reoviridae family assemble virus factories within the cytoplasm of infected cells to replicate and assemble virus particles. Bluetongue virus (BTV) forms virus inclusion bodies (VIBs) that are aggregates of viral RNA, certain viral proteins, and host factors, and have been shown to be sites of the initial assembly of transcriptionally active virus-like particles. This study sought to characterize the formation, composition, and ultrastructure of VIBs, particularly in relation to virus replication. In this study we have utilized various microscopic techniques, including structured illumination microscopy, and virological assays to show for the first time that the outer capsid protein VP5, which is essential for virus maturation, is also associated with VIBs. The addition of VP5 to assembled virus cores exiting VIBs is required to arrest transcriptionally active core particles, facilitating virus maturation. Furthermore, we observed a time-dependent association of the glycosylated non-structural protein 3 (NS3) with VIBs, and report on the importance of the two polybasic motifs within NS3 that facilitate virus trafficking and egress from infected cells at the plasma membrane. Thus, the presence of VP5 and the dynamic nature of NS3 association with VIBs that we report here provide novel insight into these previously less well-characterized processes.

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26

Plchova, Helena, Tomas Moravec, Petr Dedic, and Noemi Cerovska. "Expression of Recombinant Potato leafroll virus Structural and Non-structural Proteins for Antibody Production." Journal of Phytopathology 159, no. 2 (August 26, 2010): 130–32. http://dx.doi.org/10.1111/j.1439-0434.2010.01740.x.

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27

CAMBRA, M., M. ASENSIO, M. T. GORRIS, E. PÉREZ, E. CAMARASA, J. A. GARCIÁ, J. J. MOYA, D. LÓPEZ-ABELLA, C. VELA, and A. SANZ. "Detection of plum pox potyvirus using monoclonal antibodies to structural and non-structural proteins." EPPO Bulletin 24, no. 3 (September 1994): 569–77. http://dx.doi.org/10.1111/j.1365-2338.1994.tb01070.x.

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28

Tolfvenstam, Thomas, Anders Lundqvist, Michael Levi, Britta Wahren, and Kristina Broliden. "Mapping of B-cell epitopes on human Parvovirus B19 non-structural and structural proteins." Vaccine 19, no. 7-8 (November 2000): 758–63. http://dx.doi.org/10.1016/s0264-410x(00)00258-9.

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29

Bengs, Suvi, Jane Marttila, Petri Susi, and Jorma Ilonen. "Elicitation of T-cell responses by structural and non-structural proteins of coxsackievirus B4." Journal of General Virology 96, no. 2 (February 1, 2015): 322–30. http://dx.doi.org/10.1099/vir.0.069062-0.

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30

Dharmapalan, Babitha Thekkiniyedath, Raja Biswas, Sathianarayanan Sankaran, Baskar Venkidasamy, Muthu Thiruvengadam, Ginson George, Maksim Rebezov, et al. "Inhibitory Potential of Chromene Derivatives on Structural and Non-Structural Proteins of Dengue Virus." Viruses 14, no. 12 (November 28, 2022): 2656. http://dx.doi.org/10.3390/v14122656.

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Dengue fever is a mosquito-borne viral disease that has become a serious health issue across the globe. It is caused by a virus of the Flaviviridae family, and it comprises five different serotypes (DENV-1 to DENV-5). As there is no specific medicine or effective vaccine for controlling dengue fever, there is an urgent need to develop potential inhibitors against it. Traditionally, various natural products have been used to manage dengue fever and its co-morbid conditions. A detailed analysis of these plants revealed the presence of various chromene derivatives as the major phytochemicals. Inspired by these observations, authors have critically analyzed the anti-dengue virus potential of various 4H chromene derivatives. Further, in silico, in vitro, and in vivo reports of these scaffolds against the dengue virus are detailed in the present manuscript. These analogues exerted their activity by interfering with various stages of viral entry, assembly, and replications. Moreover, these analogues mainly target envelope protein, NS2B-NS3 protease, and NS5 RNA-dependent RNA polymerase, etc. Overall, chromene-containing analogues exerted a potent activity against the dengue virus and the present review will be helpful for the further exploration of these scaffolds for the development of novel antiviral drug candidates.

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31

Music, Nedzad, and Carl A. Gagnon. "The role of porcine reproductive and respiratory syndrome (PRRS) virus structural and non-structural proteins in virus pathogenesis." Animal Health Research Reviews 11, no. 2 (April 14, 2010): 135–63. http://dx.doi.org/10.1017/s1466252310000034.

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AbstractPorcine reproductive and respiratory syndrome (PRRS) is an economically devastating viral disease affecting the swine industry worldwide. The etiological agent, PRRS virus (PRRSV), possesses a RNA viral genome with nine open reading frames (ORFs). The ORF1a and ORF1b replicase-associated genes encode the polyproteins pp1a and pp1ab, respectively. The pp1a is processed in nine non-structural proteins (nsps): nsp1α, nsp1β, and nsp2 to nsp8. Proteolytic cleavage of pp1ab generates products nsp9 to nsp12. The proteolytic pp1a cleavage products process and cleave pp1a and pp1ab into nsp products. The nsp9 to nsp12 are involved in virus genome transcription and replication. The 3′ end of the viral genome encodes four minor and three major structural proteins. The GP2a, GP3and GP4(encoded by ORF2a, 3 and 4), are glycosylated membrane associated minor structural proteins. The fourth minor structural protein, the E protein (encoded by ORF2b), is an unglycosylated membrane associated protein. The viral envelope contains two major structural proteins: a glycosylated major envelope protein GP5(encoded by ORF5) and an unglycosylated membrane M protein (encoded by ORF6). The third major structural protein is the nucleocapsid N protein (encoded by ORF7). All PRRSV non-structural and structural proteins are essential for virus replication, and PRRSV infectivity is relatively intolerant to subtle changes within the structural proteins. PRRSV virulence is multigenic and resides in both the non-structural and structural viral proteins. This review discusses the molecular characteristics, biological and immunological functions of the PRRSV structural and nsps and their involvement in the virus pathogenesis.

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32

Pascut, Devis, Minh Hoang, Nhu N. Q. Nguyen, Muhammad Yogi Pratama, and Claudio Tiribelli. "HCV Proteins Modulate the Host Cell miRNA Expression Contributing to Hepatitis C Pathogenesis and Hepatocellular Carcinoma Development." Cancers 13, no. 10 (May 19, 2021): 2485. http://dx.doi.org/10.3390/cancers13102485.

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Hepatitis C virus (HCV) genome encodes for one long polyprotein that is processed by cellular and viral proteases to generate 10 polypeptides. The viral structural proteins include the core protein, and the envelope glycoproteins E1 and E2, present at the surface of HCV particles. Non-structural (NS) proteins consist of NS1, NS2, NS3, NS4A, NS4B, NS5a, and NS5b and have a variable function in HCV RNA replication and particle assembly. Recent findings evidenced the capacity of HCV virus to modulate host cell factors to create a favorable environment for replication. Indeed, increasing evidence has indicated that the presence of HCV is significantly associated with aberrant miRNA expression in host cells, and HCV structural and non-structural proteins may be responsible for these alterations. In this review, we summarize the recent findings on the role of HCV structural and non-structural proteins in the modulation of host cell miRNAs, with a focus on the molecular mechanisms responsible for the cell re-programming involved in viral replication, immune system escape, as well as the oncogenic process. In this regard, structural and non-structural proteins have been shown to modulate the expression of several onco-miRNAs or tumor suppressor miRNAs.

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33

Ren, Jing, Chao Ma, Mengqing Li, Yueyi Dang, Xiuzhu Yu, and Shuangkui Du. "Physicochemical, Structural Structural and Functional Properties of Non-Waxy and Waxy Proso Millet Protein." Foods 12, no. 5 (March 6, 2023): 1116. http://dx.doi.org/10.3390/foods12051116.

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The physicochemical, structural and functional properties of proso millet protein from waxy and non-waxy proso millet were investigated. The secondary structures of proso millet proteins consisted mainly of a β-sheet and ɑ-helix. The two diffraction peaks of proso millet protein appeared at around 9° and 20°. The solubility of non-waxy proso millet protein was higher than that of waxy proso millet protein at different pH values. Non-waxy proso millet protein had a relatively better emulsion stability index (ESI), whereas waxy proso millet protein had a better emulsification activity index (EAI). Non-waxy proso millet protein showed a higher maximum denaturation temperature (Td) and enthalpy change (ΔH) than its waxy counterpart, indicating a more ordered conformation. Waxy proso millet exhibited higher surface hydrophobicity and oil absorption capacity (OAC) than non-waxy proso millet, suggesting that the former may have potential applications as a functional ingredient in the food industry. There was no significant difference in the intrinsic fluorescence spectra of different waxy and non-waxy proso millet proteins at pH 7.0.

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SALEM, SAEED, MOHAMMED J. ZAKI, and CHRISTOPHER BYSTROFF. "ITERATIVE NON-SEQUENTIAL PROTEIN STRUCTURAL ALIGNMENT." Journal of Bioinformatics and Computational Biology 07, no. 03 (June 2009): 571–96. http://dx.doi.org/10.1142/s0219720009004205.

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Structural similarity between proteins gives us insights into their evolutionary relationships when there is low sequence similarity. In this paper, we present a novel approach called SNAP for non-sequential pair-wise structural alignment. Starting from an initial alignment, our approach iterates over a two-step process consisting of a superposition step and an alignment step, until convergence. We propose a novel greedy algorithm to construct both sequential and non-sequential alignments. The quality of SNAP alignments were assessed by comparing against the manually curated reference alignments in the challenging SISY and RIPC datasets. Moreover, when applied to a dataset of 4410 protein pairs selected from the CATH database, SNAP produced longer alignments with lower rmsd than several state-of-the-art alignment methods. Classification of folds using SNAP alignments was both highly sensitive and highly selective. The SNAP software along with the datasets are available online at

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35

Baļķe, Ina, Gunta Resēviča, Dace Skrastiņa, and Andris Zeltiņš. "Expression and characterisation of the ryegrass mottle virus non-structural proteins." Proceedings of the Latvian Academy of Sciences. Section B. Natural, Exact, and Applied Sciences. 64, no. 5-6 (January 1, 2010): 215–22. http://dx.doi.org/10.2478/v10046-010-0035-4.

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Expression and characterisation of the ryegrass mottle virus non-structural proteins The Ryegrass mottle virus (RGMoV) single-stranded RNA genome is organised into four open reading frames (ORF) which encode several proteins: ORF1 encodes protein P1, ORF2a contains the membrane-associated 3C-like serine protease, genome-linked protein VPg and a P16 protein gene. ORF2b encodes replicase RdRP and the only structural protein, coat protein, is synthesised from ORF3. To obtain the non-structural proteins in preparative quantities and to characterise them, the corresponding RGMoV gene cDNAs were cloned in pET- and pColdI-derived expression vectors and overexpressed in several E. coli host cells. For protease and RdRP, the best expression system containing pColdI vector and E. coli WK6 strain was determined. VPg and P16 proteins were obtained from the pET- or pACYC- vectors and E. coli BL21 (DE3) host cells and purified using Ni-Sepharose affinity chromatography. Attempts to crystallize VPg and P16 were unsuccessful, possibly due to non-structured amino acid sequences in both protein structures. Methods based on bioinformatic analysis indicated that the entire VPg domain and the C-terminal part of the P16 contain unstructured amino acid stretches, which possibly prevented the formation of crystals.

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36

Leventhal, Shanna S., Drew Wilson, Heinz Feldmann, and David W. Hawman. "A Look into Bunyavirales Genomes: Functions of Non-Structural (NS) Proteins." Viruses 13, no. 2 (February 18, 2021): 314. http://dx.doi.org/10.3390/v13020314.

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In 2016, the Bunyavirales order was established by the International Committee on Taxonomy of Viruses (ICTV) to incorporate the increasing number of related viruses across 13 viral families. While diverse, four of the families (Peribunyaviridae, Nairoviridae, Hantaviridae, and Phenuiviridae) contain known human pathogens and share a similar tri-segmented, negative-sense RNA genomic organization. In addition to the nucleoprotein and envelope glycoproteins encoded by the small and medium segments, respectively, many of the viruses in these families also encode for non-structural (NS) NSs and NSm proteins. The NSs of Phenuiviridae is the most extensively studied as a host interferon antagonist, functioning through a variety of mechanisms seen throughout the other three families. In addition, functions impacting cellular apoptosis, chromatin organization, and transcriptional activities, to name a few, are possessed by NSs across the families. Peribunyaviridae, Nairoviridae, and Phenuiviridae also encode an NSm, although less extensively studied than NSs, that has roles in antagonizing immune responses, promoting viral assembly and infectivity, and even maintenance of infection in host mosquito vectors. Overall, the similar and divergent roles of NS proteins of these human pathogenic Bunyavirales are of particular interest in understanding disease progression, viral pathogenesis, and developing strategies for interventions and treatments.

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37

Watts, Anthony. "High-resolution, non-crystallographic structural studies of large integral membrane proteins." Biochemical Society Transactions 22, no. 3 (August 1, 1994): 801–5. http://dx.doi.org/10.1042/bst0220801.

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38

Himeda, Toshiki, and Yoshiro Ohara. "Roles of two non-structural viral proteins in virus-induced demyelination." Clinical and Experimental Neuroimmunology 2, no. 3 (April 11, 2011): 49–58. http://dx.doi.org/10.1111/j.1759-1961.2011.00021.x.

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39

Gopi, Soundhararajan, and Athi N. Naganathan. "Non-specific DNA-driven quinary interactions promote structural transitions in proteins." Physical Chemistry Chemical Physics 22, no. 22 (2020): 12671–77. http://dx.doi.org/10.1039/d0cp01758b.

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We show strong evidence for the long-range electrostatic potential of DNA to influence the conformational status and distribution of states accessible to a protein chain well before the binding event.

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Shortle, David R. "Structural analysis of non-native states of proteins by NMR methods." Current Opinion in Structural Biology 6, no. 1 (February 1996): 24–30. http://dx.doi.org/10.1016/s0959-440x(96)80091-1.

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Gilbreth, Ryan N., and Shohei Koide. "Structural insights for engineering binding proteins based on non-antibody scaffolds." Current Opinion in Structural Biology 22, no. 4 (August 2012): 413–20. http://dx.doi.org/10.1016/j.sbi.2012.06.001.

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Ranz, Ana I., Julita G. Miguet, Carmen Anaya, Angel Venteo, Elena Cortés, Carmen Vela, and Antonio Sanz. "Diagnostic methods for African horsesickness virus using monoclonal antibodies to structural and non-structural proteins." Veterinary Microbiology 33, no. 1-4 (November 1992): 143–53. http://dx.doi.org/10.1016/0378-1135(92)90042-r.

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Tsunoda, Ikuo, Jane E. Libbey, and Robert S. Fujinami. "Immunization with structural and non-structural proteins of Theiler’s murine encephalomyelitis virus alters demyelinating disease." Journal of NeuroVirology 18, no. 2 (March 9, 2012): 127–37. http://dx.doi.org/10.1007/s13365-012-0087-0.

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Lan, Yu-Ching, Hsin-Fu Liu, Yi-Ping Shih, Jyh-Yuan Yang, Hour-Young Chen, and Yi-Ming Arthur Chen. "Phylogenetic analysis and sequence comparisons of structural and non-structural SARS coronavirus proteins in Taiwan." Infection, Genetics and Evolution 5, no. 3 (April 2005): 261–69. http://dx.doi.org/10.1016/j.meegid.2004.08.005.

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Verma, Mansi, Shradha Bhatnagar, Kavita Kumari, Nidhi Mittal, Shivani Sukhralia, Shruthi Gopirajan AT, P. S. Dhanaraj, and Rup Lal. "Highly conserved epitopes of DENV structural and non-structural proteins: Candidates for universal vaccine targets." Gene 695 (May 2019): 18–25. http://dx.doi.org/10.1016/j.gene.2019.02.001.

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Gómez, Dory, and Carlos A. Guerrero. "Interaction between proteins of the PPARγ and NFκB immune response pathways and rotavirus non-structural proteins." Acta virologica 66, no. 01 (2022): 39–54. http://dx.doi.org/10.4149/av_2022_105.

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Klaitong, Paeka, and Duncan R. Smith. "Roles of Non-Structural Protein 4A in Flavivirus Infection." Viruses 13, no. 10 (October 15, 2021): 2077. http://dx.doi.org/10.3390/v13102077.

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Infections with viruses in the genus Flavivirus are a worldwide public health problem. These enveloped, positive sense single stranded RNA viruses use a small complement of only 10 encoded proteins and the RNA genome itself to remodel host cells to achieve conditions favoring viral replication. A consequence of the limited viral armamentarium is that each protein exerts multiple cellular effects, in addition to any direct role in viral replication. The viruses encode four non-structural (NS) small transmembrane proteins (NS2A, NS2B, NS4A and NS4B) which collectively remain rather poorly characterized. NS4A is a 16kDa membrane associated protein and recent studies have shown that this protein plays multiple roles, including in membrane remodeling, antagonism of the host cell interferon response, and in the induction of autophagy, in addition to playing a role in viral replication. Perhaps most importantly, NS4A has been implicated as playing a critical role in fetal developmental defects seen as a consequence of Zika virus infection during pregnancy. This review provides a comprehensive overview of the multiple roles of this small but pivotal protein in mediating the pathobiology of flaviviral infections.

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Wang, Guoguo, Mengjia Xie, Wei Wu, and Zhongzhou Chen. "Structures and Functional Diversities of ASFV Proteins." Viruses 13, no. 11 (October 21, 2021): 2124. http://dx.doi.org/10.3390/v13112124.

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African swine fever virus (ASFV), the causative pathogen of the recent ASF epidemic, is a highly contagious double-stranded DNA virus. Its genome is in the range of 170~193 kbp and encodes 68 structural proteins and over 100 non-structural proteins. Its high pathogenicity strains cause nearly 100% mortality in swine. Consisting of four layers of protein shells and an inner genome, its structure is obviously more complicated than many other viruses, and its multi-layered structures play different kinds of roles in ASFV replication and survival. Each layer possesses many proteins, but very few of the proteins have been investigated at a structural level. Here, we concluded all the ASFV proteins whose structures were unveiled, and explained their functions from the view of structures. Those structures include ASFV AP endonuclease, dUTPases (E165R), pS273R protease, core shell proteins p15 and p35, non-structural proteins pA151R, pNP868R (RNA guanylyltransferase), major capsid protein p72 (gene B646L), Bcl-2-like protein A179L, histone-like protein pA104R, sulfhydryl oxidase pB119L, polymerase X and ligase. These novel structural features, diverse functions, and complex molecular mechanisms promote ASFV to escape the host immune system easily and make this large virus difficult to control.

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Krogerus, Camilla, Olga Samuilova, Tuija Pöyry, Eija Jokitalo, and Timo Hyypiä. "Intracellular localization and effects of individually expressed human parechovirus 1 non-structural proteins." Journal of General Virology 88, no. 3 (March 1, 2007): 831–41. http://dx.doi.org/10.1099/vir.0.82201-0.

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Human parechovirus 1 (HPEV-1) has many unique features compared with other picornaviruses and it has been shown that the replication complex formed during HPEV-1 infection is different from that of other picornaviruses. Here, the intracellular localization and functional effects of individually expressed HPEV-1 non-structural proteins were studied. The 2A and 3D proteins were found diffusely in the cytoplasm and nucleus of the cell. The 3A and 3AB proteins were observed to co-localize with the markers for the Golgi apparatus, whereas 2B co-localized with markers for the endoplasmic reticulum and the 2C and 2BC proteins were observed mainly on the surface of lipid droplets. The 2C protein, which has been implicated in replication-complex formation in enterovirus-infected cells, was not able to induce vesicles similar to those seen in HPEV-1-infected cells when expressed individually. However, in superinfected cells, the fusion protein was able to relocate to the virus replication complexes. Similar to other picornaviruses, HPEV-1 was found to interfere with cellular secretion, but this function could not be ascribed to any of the individually expressed non-structural proteins.

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Nurjanah, Diana, and N. L. P. I. Dharmayanti. "Biological Characteristics of West Nile Virus and Its Correlation with the Development of Antiviral Drugs and Vaccines." Indonesian Bulletin of Animal and Veterinary Sciences 29, no. 3 (September 8, 2019): 118. http://dx.doi.org/10.14334/wartazoa.v29i3.1993.

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West Nile virus (WNV) is a zoonotic RNA virus. Its genome encodes 3 structural and 7 non-structural proteins. Mutations can occur in both structural and non-structural proteins of the virus. Mutations can enhance the pathogenicity and virulence, but some mutations are beneficial for the development of vaccines. Licensed vaccines are only available for horses, while vaccines for humans are still under development. In Indonesia, WNV infection was detected in 2014 in West and East Java, but vaccines and antiviral drugs in both animals and humans are not yet available. This review describe the characteristic of structural and non-structural proteins of WNV and its correlation with mutations and the development of vaccines and antiviral drugs. Molecular identification and further research is needed to predict, prevent and control WNV infections in vectors, susceptible animals and humans.

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