Journal articles: 'Viral proteins'

1

Flint, Jane, and Thomas Shenk. "VIRAL TRANSACTIVATING PROTEINS." Annual Review of Genetics 31, no. 1 (December 1997): 177–212. http://dx.doi.org/10.1146/annurev.genet.31.1.177.

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Fischer, Wolfgang B., Gerhard Thiel, and Rainer H. A. Fink. "Viral membrane proteins." European Biophysics Journal 39, no. 7 (August 12, 2009): 1041–42. http://dx.doi.org/10.1007/s00249-009-0525-y.

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Seet, Bruce T., and Grant McFadden. "Viral chemokine‐binding proteins." Journal of Leukocyte Biology 72, no. 1 (July 2002): 24–34. http://dx.doi.org/10.1189/jlb.72.1.24.

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Verdaguer, Nuria, Diego Ferrero, and Mathur R. N. Murthy. "Viruses and viral proteins." IUCrJ 1, no. 6 (October 14, 2014): 492–504. http://dx.doi.org/10.1107/s205225251402003x.

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For more than 30 years X-ray crystallography has been by far the most powerful approach for determining the structures of viruses and viral proteins at atomic resolution. The information provided by these structures, which covers many important aspects of the viral life cycle such as cell-receptor recognition, viral entry, nucleic acid transfer and genome replication, has extensively enriched our vision of the virus world. Many of the structures available correspond to potential targets for antiviral drugs against important human pathogens. This article provides an overview of the current knowledge of different structural aspects of the above-mentioned processes.

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Rosengard, Ariella M., and Joseph M. Ahearn. "Viral complement regulatory proteins." Immunopharmacology 42, no. 1-3 (May 1999): 99–106. http://dx.doi.org/10.1016/s0162-3109(99)00012-0.

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6

Lee, Hyun-Cheol, Kiramage Chathuranga, and Jong-Soo Lee. "Intracellular sensing of viral genomes and viral evasion." Experimental & Molecular Medicine 51, no. 12 (December 2019): 1–13. http://dx.doi.org/10.1038/s12276-019-0299-y.

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AbstractDuring viral infection, virus-derived cytosolic nucleic acids are recognized by host intracellular specific sensors. The efficacy of this recognition system is crucial for triggering innate host defenses, which then stimulate more specific adaptive immune responses against the virus. Recent studies show that signal transduction pathways activated by sensing proteins are positively or negatively regulated by many modulators to maintain host immune homeostasis. However, viruses have evolved several strategies to counteract/evade host immune reactions. These systems involve viral proteins that interact with host sensor proteins and prevent them from detecting the viral genome or from initiating immune signaling. In this review, we discuss key regulators of cytosolic sensor proteins and viral proteins based on experimental evidence.

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Watson, Alastair, Maximillian J. S. Phipps, Howard W. Clark, Chris-Kriton Skylaris, and Jens Madsen. "Surfactant Proteins A and D: Trimerized Innate Immunity Proteins with an Affinity for Viral Fusion Proteins." Journal of Innate Immunity 11, no. 1 (October 5, 2018): 13–28. http://dx.doi.org/10.1159/000492974.

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Innate recognition of viruses is an essential part of the immune response to viral pathogens. This is integral to the maintenance of healthy lungs, which are free from infection and efficient at gaseous exchange. An important component of innate immunity for identifying viruses is the family of C-type collagen-containing lectins, also known as collectins. These secreted, soluble proteins are pattern recognition receptors (PRRs) which recognise pathogen-associated molecular patterns (PAMPs), including viral glycoproteins. These innate immune proteins are composed of trimerized units which oligomerise into higher-order structures and facilitate the clearance of viral pathogens through multiple mechanisms. Similarly, many viral surface proteins form trimeric configurations, despite not showing primary protein sequence similarities across the virus classes and families to which they belong. In this review, we discuss the role of the lung collectins, i.e., surfactant proteins A and D (SP-A and SP-D) in viral recognition. We focus particularly on the structural similarity and complementarity of these trimeric collectins with the trimeric viral fusion proteins with which, we hypothesise, they have elegantly co-evolved. Recombinant versions of these innate immune proteins may have therapeutic potential in a range of infectious and inflammatory lung diseases including anti-viral therapeutics.

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Shalitin, Dror, and Shmuel Wolf. "Interaction between phloem proteins and viral movement proteins." Functional Plant Biology 27, no. 9 (2000): 801. http://dx.doi.org/10.1071/pp99153.

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This paper originates from a presentation at the International Conference on Assimilate Transport and Partitioning, Newcastle, NSW, August 1999 Recent studies support the concept that long-distance signals are involved in the regulation of resource allocation among the various plant organs. Following the finding that viral movement proteins (MPs) can exert an effect on sugar metabolism and resource allocation at sites distant from their expression, we suggested that the MPs interfere with an element(s) involved in the plant’s endogenous long-distance signal network. To provide experimental support for this hypothesis, several unique procedures were employed to identify interactions between viral MPs and phloem sap proteins (PSPs) collected from cut petioles of squash (Cucurbita pepo L. subsp. pepo) and melon (Cucumis melo L.) plants. Far-western experiments with blotted PSPs, using both bacteria-overexpressed and in vitro-translated CMV- and TMV-MPs, revealed that the two virally encoded proteins react specifically with more than one PSP. Moreover, isolation of the naturally folded phloem protein in an affinity column containing a TMV-MP-maltose-binding protein indicated, once again, an interaction between the viral protein and similar PSPs. Two melon PSPs with molecular masses of 8 and 23 kDa were found to specifically interact with both the CMV- and TMV-MPs. The possible effects of this interaction in terms of altering the process of phloem transport and resource allocation are discussed.

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Zhilinskaya, I. N. "Mimicry between respiratory virus proteins and some human immune proteins." Russian Journal of Infection and Immunity 10, no. 2 (May 22, 2020): 305–14. http://dx.doi.org/10.15789/2220-7619-mbr-1179.

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A comparative analysis on search for amino acid sequences in viral proteins causing respiratory infections (or respiratory infections syndrome) homologous to amino acid sequences from some human immune proteins was performed. The following viruses were used for comparative computer analysis: coronavirus (SARS-CoV), serotype C subgroup adenovirus C (adenoid 71 strain), measles virus (ICHINOSE-BA strain), rubella (Therien strain) and respiratory syncytial (B1 strain) virus. The search for homologous sequences in viral and human immune proteins was carried out by computer comparison of 12 amino acid fragments, which were assigned as homologous at identity in ≥ 8 positions. The data obtained showed that viral proteins contained homologous motifs in several host immune proteins involved in regulating both the inflammatory response and immune response. Mechanistically, all viruses studied were characterized by sequences homologous to host immune proteins such as complement system proteins, integrins, apoptosis inhibitory proteins, interleukins, and toll-like receptors. Such cellular proteins are actively involved in regulating host inflammatory process and immune response formation. Upon that, a set of host immune proteins, to which homologous fragments were found in viral proteins, was individual for each virus. Interestingly, the largest amount of homologous fragments (up to 20) was mainly concentrated in viral proteins with polymerase and protease activity suggesting that these proteins apart to their major role were involved in production of viral nucleic acids and might participate in regulating host immune system. Envelope, internal and non-structural viral proteins, homologous fragments were detected in much smaller quantities (from 1 to 4). In addition, two fragments homologous to various motifs of the same cellular protein were detected in some viral proteins. Thus, the data obtained further support our understanding that signs of immune system disorders in viral infections can result from multi-layered processes associated with modulation of host innate and adaptive immune system, and open up new approaches to study interaction of viruses with host immune system and identify new functions of viral proteins.

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Chen, Jidang, and Hinh Ly. "Immunosuppression by viral N proteins." Oncotarget 8, no. 31 (June 22, 2017): 50331–32. http://dx.doi.org/10.18632/oncotarget.18597.

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11

Chen, Irene P., and Melanie Ott. "Viral Hijacking of BET Proteins." Viruses 14, no. 10 (October 17, 2022): 2274. http://dx.doi.org/10.3390/v14102274.

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Proteins of the bromodomain and exterminal domain (BET) family mediate critical host functions such as cell proliferation, transcriptional regulation, and the innate immune response, which makes them preferred targets for viruses. These multidomain proteins are best known as transcriptional effectors able to read acetylated histone and non-histone proteins through their tandem bromodomains. They also contain other short motif-binding domains such as the extraterminal domain, which recognizes transcriptional regulatory proteins. Here, we describe how different viruses have evolved to hijack or disrupt host BET protein function through direct interactions with BET family members to support their own propagation. The network of virus-BET interactions emerges as highly intricate, which may complicate the use of small-molecule BET inhibitors–currently in clinical development for the treatment of cancer and cardiovascular diseases–to treat viral infections.

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12

Stavrou, Spyridon, and Susan R. Ross. "APOBEC3 Proteins in Viral Immunity." Journal of Immunology 195, no. 10 (November 6, 2015): 4565–70. http://dx.doi.org/10.4049/jimmunol.1501504.

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13

STONER, G. L., C. F. RYSCHKEWITSCH, D. L. WALKER, D. SOFFER, D. G. BRAUN, H. K. HOCHKEPPEL, and H. deF WEBSTER. "Early Viral Proteins As Autoantigens." Annals of the New York Academy of Sciences 540, no. 1 Advances in N (November 1988): 665–68. http://dx.doi.org/10.1111/j.1749-6632.1988.tb27206.x.

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14

Costantini, Lindsey M., and Erik L. Snapp. "Going Viral with Fluorescent Proteins." Journal of Virology 89, no. 19 (July 22, 2015): 9706–8. http://dx.doi.org/10.1128/jvi.03489-13.

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Many longstanding questions about dynamics of virus-cell interactions can be answered by combining fluorescence imaging techniques with fluorescent protein (FP) tagging strategies. Successfully creating a FP fusion with a cellular or viral protein of interest first requires selecting the appropriate FP. However, while viral architecture and cellular localization often dictate the suitability of a FP, a FP's chemical and physical properties must also be considered. Here, we discuss the challenges of and offer suggestions for identifying the optimal FPs for studying the cell biology of viruses.

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15

Wuhrrn, Britfa. "Fetal Proteins in Viral TnfeCtions." Acta Medica Scandinavica 205, no. 1-6 (April 24, 2009): 145–48. http://dx.doi.org/10.1111/j.0954-6820.1979.tb06021.x.

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16

Bojagora, Anna, and Vivian Saridakis. "USP7 manipulation by viral proteins." Virus Research 286 (September 2020): 198076. http://dx.doi.org/10.1016/j.virusres.2020.198076.

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17

Wuchty, Stefan, Geoffrey Siwo, and Michael T. Ferdig. "Viral Organization of Human Proteins." PLoS ONE 5, no. 8 (August 25, 2010): e11796. http://dx.doi.org/10.1371/journal.pone.0011796.

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18

Schatz, Malvina, Phuoc Bao Viet Tong, and Bruno Beaumelle. "Unconventional secretion of viral proteins." Seminars in Cell & Developmental Biology 83 (November 2018): 8–11. http://dx.doi.org/10.1016/j.semcdb.2018.03.008.

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19

Xue, Bin, David Blocquel, Johnny Habchi, Alexey V. Uversky, Lukasz Kurgan, Vladimir N. Uversky, and Sonia Longhi. "Structural Disorder in Viral Proteins." Chemical Reviews 114, no. 13 (May 13, 2014): 6880–911. http://dx.doi.org/10.1021/cr4005692.

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20

Krüger, J., and W. B. Fischer. "Assembly of Viral Membrane Proteins." Journal of Chemical Theory and Computation 5, no. 9 (August 12, 2009): 2503–13. http://dx.doi.org/10.1021/ct900185n.

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21

Karlin, S., and V. Brendel. "Charge configurations in viral proteins." Proceedings of the National Academy of Sciences 85, no. 24 (December 1, 1988): 9396–400. http://dx.doi.org/10.1073/pnas.85.24.9396.

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22

Alla Katsnelson, special to C&EN. "Turning viral proteins into treatments." C&EN Global Enterprise 102, no. 15 (May 20, 2024): 10. http://dx.doi.org/10.1021/cen-10215-buscon4.

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23

Marceau, Thomas, and Martine Braibant. "Role of Viral Envelope Proteins in Determining Susceptibility of Viruses to IFITM Proteins." Viruses 16, no. 2 (February 5, 2024): 254. http://dx.doi.org/10.3390/v16020254.

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Interferon-induced transmembrane proteins (IFITMs) are a family of proteins which inhibit infections of various enveloped viruses. While their general mechanism of inhibition seems to be non-specific, involving the tightening of membrane structures to prevent fusion between the viral envelope and cell membrane, numerous studies have underscored the importance of viral envelope proteins in determining the susceptibility of viruses to IFITMs. Mutations in envelope proteins may lead to viral escape from direct interaction with IFITM proteins or result in indirect resistance by modifying the viral entry pathway, allowing the virus to modulate its exposure to IFITMs. In a broader context, the nature of viral envelope proteins and their interaction with IFITMs can play a crucial role in the context of adaptive immunity, leading to viral envelope proteins that are more susceptible to antibody neutralization. The precise mechanisms underlying these observations remain unclear, and further studies in this field could contribute to a better understanding of how IFITMs control viral infections.

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24

Subramanian, T., S. Vijayalingam, and G. Chinnadurai. "Genetic Identification of Adenovirus Type 5 Genes That Influence Viral Spread." Journal of Virology 80, no. 4 (February 15, 2006): 2000–2012. http://dx.doi.org/10.1128/jvi.80.4.2000-2012.2006.

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ABSTRACT The mechanisms that control cell-to-cell spread of human adenoviruses (Ad) are not well understood. Two early viral proteins, E1B-19K and E3-ADP, appear to have opposing effects since viral mutants that are individually deficient in E1B-19K produce large plaques (G. Chinnadurai, Cell 33:759-766, 1983), while mutants deficient in E3-ADP produce small plaques (A. E. Tollefson et al., J. Virol. 70:2296-2306, 1996) on infected cell monolayers. We have used a genetic strategy to identify different viral genes that influence adenovirus type 5 (Ad5) spread in an epithelial cancer cell line. An Ad5 mutant (dl327; lacking most of the E3 region) with the restricted-spread (small-plaque) phenotype was randomly mutagenized with UV, and 27 large-plaque (lp) mutants were isolated. A combination of analyses of viral proteins and genomic DNA sequences have indicated that 23 mutants contained lesions in the E1B region affecting either 19K or both 19K and 55K proteins. Four other lp mutants contained lesions in early regions E1A and E4, in the early L1 region that codes for the i-leader protein, and in late regions that code for the viral structural proteins, penton base, and fiber. Our results suggest that the requirement of E3-ADP for Ad spread could be readily compensated for by abrogation of the functions of E1B-19K and provide genetic evidence that these two viral proteins influence viral spread in opposing manners. In addition to E1B and E3 proteins, other early and late proteins that regulate viral replication and infectivity also influence lateral viral spread. Our studies have identified novel mutations that could be exploited in designing efficient oncolytic Ad vectors.

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Maxwell, Karen L., and Lori Frappier. "Viral Proteomics." Microbiology and Molecular Biology Reviews 71, no. 2 (June 2007): 398–411. http://dx.doi.org/10.1128/mmbr.00042-06.

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SUMMARY Viruses have long been studied not only for their pathology and associated disease but also as model systems for molecular processes and as tools for identifying important cellular regulatory proteins and pathways. Recent advances in mass spectrometry methods coupled with the development of proteomic approaches have greatly facilitated the detection of virion components, protein interactions in infected cells, and virally induced changes in the cellular proteome, resulting in a more comprehensive understanding of viral infection. In addition, a rapidly increasing number of high-resolution structures for viral proteins have provided valuable information on the mechanism of action of these proteins as well as aided in the design and understanding of specific inhibitors that could be used in antiviral therapies. In this paper, we discuss proteomic studies conducted on all eukaryotic viruses and bacteriophages, covering virion composition, viral protein structures, virus-virus and virus-host protein interactions, and changes in the cellular proteome upon viral infection.

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26

Münz, Christian. "Autophagy Proteins in Viral Exocytosis and Anti-Viral Immune Responses." Viruses 9, no. 10 (October 4, 2017): 288. http://dx.doi.org/10.3390/v9100288.

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27

Sawtell, N. M., R. L. Thompson, and R. L. Haas. "Herpes Simplex Virus DNA Synthesis Is Not a Decisive Regulatory Event in the Initiation of Lytic Viral Protein Expression in Neurons In Vivo during Primary Infection or Reactivation from Latency." Journal of Virology 80, no. 1 (January 1, 2006): 38–50. http://dx.doi.org/10.1128/jvi.80.1.38-50.2006.

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ABSTRACT The herpes simplex virus genome can enter a repressed transcriptional state (latency) in sensory neurons of the host nervous system. Although reduced permissiveness of the neuronal environment is widely accepted as a causal factor, the molecular pathway(s) directing and maintaining the viral genome in the latent state remains undefined. Over the past decade, the field has been strongly influenced by the observations of Kosz-Vnenchak et al., which have been interpreted to indicate that, in sensory neurons in vivo, a critical level of viral DNA synthesis within the neuron is required for sufficient viral immediate-early (IE) and early (E) gene expression (M. Kosz-Vnenchak, J. Jacobson, D. M. Coen, and D. M. Knipe, J. Virol. 67:5383-5393, 1993). The levels of IE and E genes are, in turn, thought to regulate the decision to enter the lytic cycle or latency. We have reexamined this issue using new strategies for in situ detection and quantification of viral gene expression in whole tissues. Our results using thymidine kinase-null and rescued mutants as well as wild-type strains in conjunction with viral DNA synthesis blockers demonstrate that (i) despite inhibition of viral DNA replication, many neurons express lytic viral proteins, including IE proteins, during acute infection in the ganglion; (ii) at early times postinoculation, the number of neurons expressing viral proteins in the ganglion is not reduced by inhibition of viral DNA replication; and (iii) following a reactivation stimulus, the numbers of neurons and apparent levels of lytic viral proteins, including IE proteins, are not reduced by inhibition of viral DNA replication. We conclude that viral DNA replication in the neuron per se does not regulate IE gene expression or entry into the lytic cycle.

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28

Manocha, Ekta, Arnaldo Caruso, and Francesca Caccuri. "Viral Proteins as Emerging Cancer Therapeutics." Cancers 13, no. 9 (May 3, 2021): 2199. http://dx.doi.org/10.3390/cancers13092199.

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Viruses are obligatory intracellular parasites that originated millions of years ago. Viral elements cover almost half of the human genome sequence and have evolved as genetic blueprints in humans. They have existed as endosymbionts as they are largely dependent on host cell metabolism. Viral proteins are known to regulate different mechanisms in the host cells by hijacking cellular metabolism to benefit viral replication. Amicable viral proteins, on the other hand, from several viruses can participate in mediating growth retardation of cancer cells based on genetic abnormalities while sparing normal cells. These proteins exert discreet yet converging pathways to regulate events like cell cycle and apoptosis in human cancer cells. This property of viral proteins could be harnessed for their use in cancer therapy. In this review, we discuss viral proteins from different sources as potential anticancer therapeutics.

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29

Zhou, Rui, Li Liu, and Yu Wang. "Viral proteins recognized by different TLRs." Journal of Medical Virology 93, no. 11 (August 17, 2021): 6116–23. http://dx.doi.org/10.1002/jmv.27265.

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30

Agol, Vadim I., and Anatoly P. Gmyl. "Viral security proteins: counteracting host defences." Nature Reviews Microbiology 8, no. 12 (November 9, 2010): 867–78. http://dx.doi.org/10.1038/nrmicro2452.

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31

Hardwick, J. M., and D. S. Bellows. "Viral versus cellular BCL-2 proteins." Cell Death & Differentiation 10, S1 (January 2003): S68—S76. http://dx.doi.org/10.1038/sj.cdd.4401133.

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32

Grand, R. J. A. "Acylation of viral and eukaryotic proteins." Biochemical Journal 258, no. 3 (March 15, 1989): 625–38. http://dx.doi.org/10.1042/bj2580625.

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33

Phelps, D. "Theoretical studies of viral capsid proteins." Current Opinion in Structural Biology 10, no. 2 (April 1, 2000): 170–73. http://dx.doi.org/10.1016/s0959-440x(00)00064-6.

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34

Hughson, Frederick M. "Structural characterization of viral fusion proteins." Current Biology 5, no. 3 (March 1995): 265–74. http://dx.doi.org/10.1016/s0960-9822(95)00057-1.

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35

Backovic, Marija, and Theodore S. Jardetzky. "Class III viral membrane fusion proteins." Current Opinion in Structural Biology 19, no. 2 (April 2009): 189–96. http://dx.doi.org/10.1016/j.sbi.2009.02.012.

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36

Wang, Kai, Shiqi Xie, and Bing Sun. "Viral proteins function as ion channels." Biochimica et Biophysica Acta (BBA) - Biomembranes 1808, no. 2 (February 2011): 510–15. http://dx.doi.org/10.1016/j.bbamem.2010.05.006.

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37

Nevins, Joseph R. "Transcriptional activation by viral regulatory proteins." Trends in Biochemical Sciences 16 (January 1991): 435–39. http://dx.doi.org/10.1016/0968-0004(91)90171-q.

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38

Li, Kun, Ruben M. Markosyan, Yi-Min Zheng, Ottavia Golfetto, Brittani Bungart, Minghua Li, Shilei Ding, et al. "IFITM Proteins Restrict Viral Membrane Hemifusion." PLoS Pathogens 9, no. 1 (January 24, 2013): e1003124. http://dx.doi.org/10.1371/journal.ppat.1003124.

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39

Krajcsi, P., and W. S. Wold. "Viral proteins that regulate cellular signalling." Journal of General Virology 79, no. 6 (June 1, 1998): 1323–35. http://dx.doi.org/10.1099/0022-1317-79-6-1323.

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40

White, J. M. "Viral and Cellular Membrane Fusion Proteins." Annual Review of Physiology 52, no. 1 (October 1990): 675–97. http://dx.doi.org/10.1146/annurev.ph.52.030190.003331.

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41

Khalili, K., and J. Fazakerley. "Viral proteins and blood brain barrier." Journal of Neurovirology 8, no. 3 (January 2002): 43–44. http://dx.doi.org/10.1080/13550280290049985.

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42

Maurer-Stroh, Sebastian, and Frank Eisenhaber. "Myristoylation of viral and bacterial proteins." Trends in Microbiology 12, no. 4 (April 2004): 178–85. http://dx.doi.org/10.1016/j.tim.2004.02.006.

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Ding, Qiong, Lei Zhao, Hong Guo, and Alan C. Zheng. "The nucleocytoplasmic transport of viral proteins." Virologica Sinica 25, no. 2 (April 2010): 79–85. http://dx.doi.org/10.1007/s12250-010-3099-z.

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44

Murphy, Philip M. "Viral Imitations of Host Defense Proteins." JAMA 271, no. 24 (June 22, 1994): 1948. http://dx.doi.org/10.1001/jama.1994.03510480072037.

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Rachita, H. R., and H. A. Nagarajaram. "Viral proteins that bridge unconnected proteins and components in the human PPI network." Mol. BioSyst. 10, no. 9 (2014): 2448–58. http://dx.doi.org/10.1039/c4mb00219a.

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Hindley, Clemence E., Andrew D. Davidson, and David A. Matthews. "Relationship between adenovirus DNA replication proteins and nucleolar proteins B23.1 and B23.2." Journal of General Virology 88, no. 12 (December 1, 2007): 3244–48. http://dx.doi.org/10.1099/vir.0.83196-0.

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Adenovirus infection subverts nucleolar structure and function. B23 is a nucleolar protein present in two isoforms (B23.1 and B23.2) and both isoforms have been identified as stimulatory factors for adenovirus DNA replication. Here, it is demonstrated that the two isoforms of B23, B23.1 and B23.2, interact and co-localize differently with viral DNA replication proteins pTP and DBP in adenovirus-infected cells. Thus, the mechanism by which the two proteins stimulate viral DNA replication is likely to differ. These data also demonstrate the importance of testing both isoforms of B23 for interactions with viral proteins and nucleic acids.

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Kalejta, Robert F. "Tegument Proteins of Human Cytomegalovirus." Microbiology and Molecular Biology Reviews 72, no. 2 (June 2008): 249–65. http://dx.doi.org/10.1128/mmbr.00040-07.

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SUMMARY Human cytomegalovirus (HCMV) is a common, medically relevant human herpesvirus. The tegument layer of herpesvirus virions lies between the genome-containing capsids and the viral envelope. Proteins within the tegument layer of herpesviruses are released into the cell upon entry when the viral envelope fuses with the cell membrane. These proteins are fully formed and active and control viral entry, gene expression, and immune evasion. Most tegument proteins accumulate to high levels during later stages of infection, when they direct the assembly and egress of progeny virions. Thus, viral tegument proteins play critical roles at the very earliest and very last steps of the HCMV lytic replication cycle. This review summarizes HCMV tegument composition and structure as well as the known and speculated functions of viral tegument proteins. Important directions for future investigation and the challenges that lie ahead are identified and discussed.

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Li, Guohui, Xinyu Qi, Zhaoyang Hu, and Qi Tang. "Mechanisms Mediating Nuclear Trafficking Involved in Viral Propagation by DNA Viruses." Viruses 11, no. 11 (November 7, 2019): 1035. http://dx.doi.org/10.3390/v11111035.

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Typical viral propagation involves sequential viral entry, uncoating, replication, gene transcription and protein synthesis, and virion assembly and release. Some viral proteins must be transported into host nucleus to facilitate viral propagation, which is essential for the production of mature virions. During the transport process, nuclear localization signals (NLSs) play an important role in guiding target proteins into nucleus through the nuclear pore. To date, some classical nuclear localization signals (cNLSs) and non-classical NLSs (ncNLSs) have been identified in a number of viral proteins. These proteins are involved in viral replication, expression regulation of viral genes and virion assembly. Moreover, other proteins are transported into nucleus with unknown mechanisms. This review highlights our current knowledge about the nuclear trafficking of cellular proteins associated with viral propagation.

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49

Leslie, Mitch. "A viral arsenal." Science 378, no. 6616 (October 14, 2022): 128–31. http://dx.doi.org/10.1126/science.adf2350.

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Xue, Bin, Robert W. Williams, Christopher J. Oldfield, Gerard Kian-Meng Goh, A. Keith Dunker, and Vladimir N. Uversky. "Viral Disorder or Disordered Viruses: Do Viral Proteins Possess Unique Features?" Protein & Peptide Letters 17, no. 8 (August 1, 2010): 932–51. http://dx.doi.org/10.2174/092986610791498984.

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Journal articles on the topic 'Viral proteins'

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