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Journal articles on the topic 'VRNP'

Author: Grafiati

Published: 4 June 2021

Last updated: 11 February 2022

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1

Han, Julianna, Ketaki Ganti, Veeresh Kumar Sali, et al. "Host factor Rab11a is critical for efficient assembly of influenza A virus genomic segments." PLOS Pathogens 17, no. 5 (2021): e1009517. http://dx.doi.org/10.1371/journal.ppat.1009517.

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It is well documented that influenza A viruses selectively package 8 distinct viral ribonucleoprotein complexes (vRNPs) into each virion; however, the role of host factors in genome assembly is not completely understood. To evaluate the significance of cellular factors in genome assembly, we generated a reporter virus carrying a tetracysteine tag in the NP gene (NP-Tc virus) and assessed the dynamics of vRNP localization with cellular components by fluorescence microscopy. At early time points, vRNP complexes were preferentially exported to the MTOC; subsequently, vRNPs associated on vesicles

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2

Fontana, Juan, Kellie A. Jurado, Naiqian Cheng, et al. "Distribution and Redistribution of HIV-1 Nucleocapsid Protein in Immature, Mature, and Integrase-Inhibited Virions: a Role for Integrase in Maturation." Journal of Virology 89, no. 19 (2015): 9765–80. http://dx.doi.org/10.1128/jvi.01522-15.

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ABSTRACTDuring virion maturation, HIV-1 capsid protein assembles into a conical core containing the viral ribonucleoprotein (vRNP) complex, thought to be composed mainly of the viral RNA and nucleocapsid protein (NC). After infection, the viral RNA is reverse transcribed into double-stranded DNA, which is then incorporated into host chromosomes by integrase (IN) catalysis. Certain IN mutations (class II) and antiviral drugs (allosteric IN inhibitors [ALLINIs]) adversely affect maturation, resulting in virions that contain “eccentric condensates,” electron-dense aggregates located outside seemi

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3

Schreiber, André, Laurita Boff, Darisuren Anhlan, et al. "Dissecting the mechanism of signaling-triggered nuclear export of newly synthesized influenza virus ribonucleoprotein complexes." Proceedings of the National Academy of Sciences 117, no. 28 (2020): 16557–66. http://dx.doi.org/10.1073/pnas.2002828117.

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Influenza viruses (IV) exploit a variety of signaling pathways. Previous studies showed that the rapidly accelerated fibrosarcoma/mitogen-activated protein kinase/extracellular signal-regulated kinase (Raf/MEK/ERK) pathway is functionally linked to nuclear export of viral ribonucleoprotein (vRNP) complexes, suggesting that vRNP export is a signaling-induced event. However, the underlying mechanism remained completely enigmatic. Here we have dissected the unknown molecular steps of signaling-driven vRNP export. We identified kinases RSK1/2 as downstream targets of virus-activated ERK signaling.

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4

Bui, Matthew, Elizabeth G. Wills, Ari Helenius, and Gary R. Whittaker. "Role of the Influenza Virus M1 Protein in Nuclear Export of Viral Ribonucleoproteins." Journal of Virology 74, no. 4 (2000): 1781–86. http://dx.doi.org/10.1128/jvi.74.4.1781-1786.2000.

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ABSTRACT The protein kinase inhibitor H7 blocks influenza virus replication, inhibits production of the matrix protein (M1), and leads to a retention of the viral ribonucleoproteins (vRNPs) in the nucleus at late times of infection (K. Martin and A. Helenius, Cell 67:117–130, 1991). We show here that production of assembled vRNPs occurs normally in H7-treated cells, and we have used H7 as a biochemical tool to trap vRNPs in the nucleus. When H7 was removed from the cells, vRNP export was specifically induced in a CHO cell line stably expressing recombinant M1. Similarly, fusion of cells expres

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5

Gao, Qingxia, Cha Yang, Caiyue Ren, et al. "Eukaryotic Translation Elongation Factor 1 Delta Inhibits the Nuclear Import of the Nucleoprotein and PA-PB1 Heterodimer of Influenza A Virus." Journal of Virology 95, no. 2 (2020): e01391-20. http://dx.doi.org/10.1128/jvi.01391-20.

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ABSTRACTThe viral ribonucleoprotein (vRNP) of the influenza A virus (IAV) is responsible for the viral RNA transcription and replication in the nucleus, and its functions rely on host factors. Previous studies have indicated that eukaryotic translation elongation factor 1 delta (eEF1D) may associate with RNP subunits, but its roles in IAV replication are unclear. Herein, we showed that eEF1D was an inhibitor of IAV replication because knockout of eEF1D resulted in a significant increase in virus yield. eEF1D interacted with RNP subunits polymerase acidic protein (PA), polymerase basic 1 (PB1),

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6

Hirayama, Etsuko, Hiromitsu Atagi, Akihiro Hiraki, and Jeman Kim. "Heat Shock Protein 70 Is Related to Thermal Inhibition of Nuclear Export of the Influenza Virus Ribonucleoprotein Complex." Journal of Virology 78, no. 3 (2004): 1263–70. http://dx.doi.org/10.1128/jvi.78.3.1263-1270.2004.

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ABSTRACT The influenza virus genome replicates and forms a viral ribonucleoprotein complex (vRNP) with nucleoprotein (NP) and RNA polymerases in the nuclei of host cells. vRNP is then exported into the cytoplasm for viral morphogenesis at the cell membrane. Matrix protein 1 (M1) and nonstructural protein 2/nuclear export protein (NS2/NEP) work in the nuclear export of vRNP by associating with it. It was previously reported that influenza virus production was inhibited in Madin-Darby canine kidney (MDCK) cells cultured at 41°C because nuclear export of vRNP was blocked by the dissociation of M1

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7

Predicala, Rey, and Yan Zhou. "The role of Ran-binding protein 3 during influenza A virus replication." Journal of General Virology 94, no. 5 (2013): 977–84. http://dx.doi.org/10.1099/vir.0.049395-0.

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Influenza A virus vRNP nuclear export is CRM1-dependent. Ran-binding protein 3 (RanBP3) is a Ran-interacting protein that is best known for its role as a cofactor of CRM1-mediated cargo nuclear export. In this study, we investigated the role of RanBP3 during the influenza A virus life cycle. We found that RanBP3 was phosphorylated at Ser58 in the early and late phases of infection. Knockdown of RanBP3 expression led to vRNP nuclear retention, suggesting that RanBP3 is involved in vRNP nuclear export. Moreover, we demonstrated that the function of RanBP3 during vRNP nuclear export is regulated

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8

Zhang, Junjie, Gang Li, and Xin Ye. "Cyclin T1/CDK9 Interacts with Influenza A Virus Polymerase and Facilitates Its Association with Cellular RNA Polymerase II." Journal of Virology 84, no. 24 (2010): 12619–27. http://dx.doi.org/10.1128/jvi.01696-10.

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ABSTRACT Influenza virus RNA-dependent RNA polymerase scavenges the 5′ cap from host pre-mRNA to prime viral transcription initiation. It is also well established that viral RNA-dependent RNA polymerase (vRNP) associates with cellular RNA polymerase II (Pol II), on which viral replication depends. Here we report that cyclin T1/CDK9 can interact with influenza virus polymerase and facilitate its association with cellular Pol II. The immunodepletion of cyclin T1/CDK9 totally abolished the association of vRNP with the C-terminal domain (CTD) Ser-2-phosphorylated form of RNA polymerase II. Further

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9

Zhang, Junsong, Feng Huang, Likai Tan, et al. "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." Journal of Virology 90, no. 8 (2016): 3966–80. http://dx.doi.org/10.1128/jvi.03137-15.

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ABSTRACTThe viral ribonucleoprotein (vRNP) complex of influenza A viruses (IAVs) contains an RNA-dependent RNA polymerase complex (RdRp) and nucleoprotein (NP) and is the functional unit for viral RNA transcription and replication. The vRNP complex is an important determinant of virus pathogenicity and host adaptation, implying that its function can be affected by host factors. In our study, we identified host protein Moloney leukemia virus 10 (MOV10) as an inhibitor of IAV replication, since depletion of MOV10 resulted in a significant increase in virus yield. MOV10 inhibited the polymerase a

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10

Imai, Masaki, Shinji Watanabe, Ai Ninomiya, Masatsugu Obuchi, and Takato Odagiri. "Influenza B Virus BM2 Protein Is a Crucial Component for Incorporation of Viral Ribonucleoprotein Complex into Virions during Virus Assembly." Journal of Virology 78, no. 20 (2004): 11007–15. http://dx.doi.org/10.1128/jvi.78.20.11007-11015.2004.

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ABSTRACT Influenza B virus contains four integral membrane proteins in its envelope. Of these, BM2 has recently been found to have ion channel activity and is considered to be a functional counterpart to influenza A virus M2, but the role of BM2 in the life cycle of influenza B virus remains unclear. In an effort to explore its function, a number of BM2 mutant viruses were generated by using a reverse genetics technique. The BM2ΔATG mutant virus synthesized BM2 at markedly lower levels but exhibited similar growth to wild-type (wt) virus. In contrast, the BM2 knockout virus, which did not prod

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11

Qin, Chong, Wei Li, Qin Li, et al. "Real-time dissection of dynamic uncoating of individual influenza viruses." Proceedings of the National Academy of Sciences 116, no. 7 (2019): 2577–82. http://dx.doi.org/10.1073/pnas.1812632116.

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Uncoating is an obligatory step in the virus life cycle that serves as an antiviral target. Unfortunately, it is challenging to study viral uncoating due to methodology limitations for detecting this transient and dynamic event. The uncoating of influenza A virus (IAV), which contains an unusual genome of eight segmented RNAs, is particularly poorly understood. Here, by encapsulating quantum dot (QD)-conjugated viral ribonucleoprotein complexes (vRNPs) within infectious IAV virions and applying single-particle imaging, we tracked the uncoating process of individual IAV virions. Approximately 3

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12

Imai, Masaki, Kazunori Kawasaki, and Takato Odagiri. "Cytoplasmic Domain of Influenza B Virus BM2 Protein Plays Critical Roles in Production of Infectious Virus." Journal of Virology 82, no. 2 (2007): 728–39. http://dx.doi.org/10.1128/jvi.01752-07.

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ABSTRACT Influenza B virus BM2 is a type III integral membrane protein that displays H+ ion channel activity. Analysis of BM2 knockout mutants has suggested that this protein is a necessary component for the capture of M1-viral ribonucleoprotein (vRNP) complex at the plasma membrane and for incorporation of vRNP complex into the virion during the assembly process. BM2 comprises 109 amino acid residues and possesses a longer cytoplasmic domain than the other 3 integral membrane proteins (hemagglutinin, neuraminidase, and NB). To explore whether the cytoplasmic domain of BM2 is important for inf

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13

Weber, Friedemann, Otto Haller, and Georg Kochs. "MxA GTPase Blocks Reporter Gene Expression of Reconstituted Thogoto Virus Ribonucleoprotein Complexes." Journal of Virology 74, no. 1 (2000): 560–63. http://dx.doi.org/10.1128/jvi.74.1.560-563.2000.

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ABSTRACT Human MxA protein accumulates in the cytoplasm of interferon-treated cells and inhibits the multiplication of several RNA viruses, including Thogoto virus (THOV), a tick-borne orthomyxovirus that transcribes and replicates its genome in the cell nucleus. The antiviral mechanism of MxA was investigated by using two alternative minireplicon systems in which recombinant viral ribonucleoprotein complexes (vRNPs) of THOV were reconstituted from cloned cDNAs. A chloramphenicol acetyltransferase reporter minigenome RNA was expressed either by T7 RNA polymerase in the cytoplasm of transfected

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14

Roberts, D. W. A., and R. I. Larson. "Vernalization and photoperiodic responses of selected chromosome substitution lines derived from 'Rescue', 'Cadet', and 'Cypress' wheats." Canadian Journal of Genetics and Cytology 27, no. 5 (1985): 586–91. http://dx.doi.org/10.1139/g85-086.

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The vernalization responses of 'Rescue', 'Cadet', 'Cypress', and selected chromosome substitution lines derived from these cultivars were measured by comparing days to ear emergence of vernalized and unvernalized plants under 24- and 16-h photoperiods. The genotype of 'Cadet' appears to be Vrn1Vrni1, vrn4vrn4, vrnxvrnx (where vrnx is an unidentified locus), and of 'Rescue' vrn1vrn1, Vrn3Vrn3, Vrn4Vrn4. 'Cypress' appears to carry Vrn4 and one or both of vrn1, and vrn3. Although some minor photoperiod responses were observed, no loci involved in major photoperiod responses were detected on chrom

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15

Zheng, Weinan, Jing Li, Shanshan Wang, et al. "Phosphorylation Controls the Nuclear-Cytoplasmic Shuttling of Influenza A Virus Nucleoprotein." Journal of Virology 89, no. 11 (2015): 5822–34. http://dx.doi.org/10.1128/jvi.00015-15.

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ABSTRACTThe nucleoprotein (NP) is a major component of the viral ribonucleoprotein (vRNP) complex. During the replication of influenza virus, the vRNP complex undergoes nuclear-cytoplasmic shuttling, during which NP serves as one of the determinants. To date, many phosphorylation sites on NP have been identified, but the biological functions of many of these phosphorylation sites remain unknown. In the present study, the functions of the phosphorylation sites S9, Y10, and Y296 were characterized. These residues are highly conserved, and their phosphorylation was essential for virus growth in c

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16

Eschbach, Jenna E., Jennifer L. Elliott, Wen Li, et al. "Capsid Lattice Destabilization Leads to Premature Loss of the Viral Genome and Integrase Enzyme during HIV-1 Infection." Journal of Virology 95, no. 2 (2020): e00984-20. http://dx.doi.org/10.1128/jvi.00984-20.

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ABSTRACTThe human immunodeficiency virus type 1 (HIV-1) capsid (CA) protein forms a conical lattice around the viral ribonucleoprotein complex (vRNP) consisting of a dimeric viral genome and associated proteins, together constituting the viral core. Upon entry into target cells, the viral core undergoes a process termed uncoating, during which CA molecules are shed from the lattice. Although the timing and degree of uncoating are important for reverse transcription and integration, the molecular basis of this phenomenon remains unclear. Using complementary approaches, we assessed the impact of

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Szabat, Marta, Dagny Lorent, Tomasz Czapik, Maria Tomaszewska, Elzbieta Kierzek, and Ryszard Kierzek. "RNA Secondary Structure as a First Step for Rational Design of the Oligonucleotides towards Inhibition of Influenza A Virus Replication." Pathogens 9, no. 11 (2020): 925. http://dx.doi.org/10.3390/pathogens9110925.

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Influenza is an important research subject around the world because of its threat to humanity. Influenza A virus (IAV) causes seasonal epidemics and sporadic, but dangerous pandemics. A rapid antigen changes and recombination of the viral RNA genome contribute to the reduced effectiveness of vaccination and anti-influenza drugs. Hence, there is a necessity to develop new antiviral drugs and strategies to limit the influenza spread. IAV is a single-stranded negative sense RNA virus with a genome (viral RNA—vRNA) consisting of eight segments. Segments within influenza virion are assembled into v

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Ganti, Ketaki, Julianna Han, Balaji Manicassamy, and Anice C. Lowen. "Rab11a mediates cell-cell spread and reassortment of influenza A virus genomes via tunneling nanotubes." PLOS Pathogens 17, no. 9 (2021): e1009321. http://dx.doi.org/10.1371/journal.ppat.1009321.

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Influenza A virus [IAV] genomes comprise eight negative strand RNAs packaged into virions in the form of viral ribonucleoproteins [vRNPs]. Rab11a plays a crucial role in the transport of vRNPs from the nucleus to the plasma membrane via microtubules, allowing assembly and virus production. Here, we identify a novel function for Rab11a in the inter-cellular transport of IAV vRNPs using tunneling nanotubes [TNTs]as molecular highways. TNTs are F-Actin rich tubules that link the cytoplasm of nearby cells. In IAV-infected cells, Rab11a was visualized together with vRNPs in these actin-rich interce

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Robb, Nicole C., Matt Smith, Frank T. Vreede, and Ervin Fodor. "NS2/NEP protein regulates transcription and replication of the influenza virus RNA genome." Journal of General Virology 90, no. 6 (2009): 1398–407. http://dx.doi.org/10.1099/vir.0.009639-0.

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The influenza virus RNA polymerase transcribes the negative-sense viral RNA segments (vRNA) into mRNA and replicates them via complementary RNA (cRNA) intermediates into more copies of vRNA. It is not clear how the relative amounts of the three RNA products, mRNA, cRNA and vRNA, are regulated during the viral life cycle. We found that in viral ribonucleoprotein (vRNP) reconstitution assays involving only the minimal components required for viral transcription and replication (the RNA polymerase, the nucleoprotein and a vRNA template), the relative levels of accumulation of RNA products differe

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Kesavardhana, Sannula, Teneema Kuriakose, Clifford S. Guy, et al. "ZBP1/DAI ubiquitination and sensing of influenza vRNPs activate programmed cell death." Journal of Experimental Medicine 214, no. 8 (2017): 2217–29. http://dx.doi.org/10.1084/jem.20170550.

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Innate sensing of influenza virus infection induces activation of programmed cell death pathways. We have recently identified Z-DNA–binding protein 1 (ZBP1) as an innate sensor of influenza A virus (IAV). ZBP1-mediated IAV sensing is critical for triggering programmed cell death in the infected lungs. Surprisingly, little is known about the mechanisms regulating ZBP1 activation to induce programmed cell death. Here, we report that the sensing of IAV RNA by retinoic acid inducible gene I (RIG-I) initiates ZBP1-mediated cell death via the RIG-I–MAVS–IFN-β signaling axis. IAV infection induces ub

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Miyake, Yasuyuki, Jeremy J. Keusch, Laure Decamps, et al. "Influenza virus uses transportin 1 for vRNP debundling during cell entry." Nature Microbiology 4, no. 4 (2019): 578–86. http://dx.doi.org/10.1038/s41564-018-0332-2.

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Kurebayashi, Yuki, Shringkhala Bajimaya, Masahiro Watanabe, et al. "Human parainfluenza virus type 1 regulates cholesterol biosynthesis and establishes quiescent infection in human airway cells." PLOS Pathogens 17, no. 9 (2021): e1009908. http://dx.doi.org/10.1371/journal.ppat.1009908.

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Human parainfluenza virus type 1 (hPIV1) and 3 (hPIV3) cause seasonal epidemics, but little is known about their interaction with human airway cells. In this study, we determined cytopathology, replication, and progeny virion release from human airway cells during long-term infection in vitro. Both viruses readily established persistent infection without causing significant cytopathic effects. However, assembly and release of hPIV1 rapidly declined in sharp contrast to hPIV3 due to impaired viral ribonucleocapsid (vRNP) trafficking and virus assembly. Transcriptomic analysis revealed that both

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Makau, Juliann Nzembi, Ken Watanabe, Hiroki Otaki, et al. "A Quinolinone Compound Inhibiting the Oligomerization of Nucleoprotein of Influenza A Virus Prevents the Selection of Escape Mutants." Viruses 12, no. 3 (2020): 337. http://dx.doi.org/10.3390/v12030337.

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The emergence of resistance to currently available anti-influenza drugs has heightened the need for antivirals with novel mechanisms of action. The influenza A virus (IAV) nucleoprotein (NP) is highly conserved and essential for the formation of viral ribonucleoprotein (vRNP), which serves as the template for replication and transcription. Recently, using in silico screening, we identified an antiviral compound designated NUD-1 (a 4-hydroxyquinolinone derivative) as a potential inhibitor of NP. In this study, we further analyzed the interaction between NUD-1 and NP and found that the compound

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Luo, Ling, Weili Han, Jinyan Du, et al. "Chenodeoxycholic Acid from Bile Inhibits Influenza A Virus Replication via Blocking Nuclear Export of Viral Ribonucleoprotein Complexes." Molecules 23, no. 12 (2018): 3315. http://dx.doi.org/10.3390/molecules23123315.

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Influenza A virus (IAV) infection is still a major global threat for humans, especially for the risk groups: young children and the elderly. The currently licensed antiviral drugs target viral factors and are prone to viral resistance. In recent years, a few endogenous small molecules from host, such as estradiol and omega-3 polyunsaturated fatty acid (PUFA)-derived lipid mediator protection D1 (PD1), were demonstrated to be capable of inhibiting IAV infection. Chenodeoxycholic acid (CDCA), one of the main primary bile acids, is synthesized from cholesterol in the liver and classically functio

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Sanchez, Abel, Christian F. Guerrero-Juarez, Jose Ramirez, and Laura L. Newcomb. "Nuclear localized Influenza nucleoprotein N-terminal deletion mutant is deficient in functional vRNP formation." Virology Journal 11, no. 1 (2014): 155. http://dx.doi.org/10.1186/1743-422x-11-155.

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Hu, Yong, Xiaokun Liu, Anding Zhang, et al. "CHD3 facilitates vRNP nuclear export by interacting with NES1 of influenza A virus NS2." Cellular and Molecular Life Sciences 72, no. 5 (2014): 971–82. http://dx.doi.org/10.1007/s00018-014-1726-9.

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Neumann, G. "Influenza A virus NS2 protein mediates vRNP nuclear export through NES-independent interaction with hCRM1." EMBO Journal 19, no. 24 (2000): 6751–58. http://dx.doi.org/10.1093/emboj/19.24.6751.

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Cubitt, Beatrice, Emilio Ortiz-Riano, Benson YH Cheng, et al. "A cell-based, infectious-free, platform to identify inhibitors of lassa virus ribonucleoprotein (vRNP) activity." Antiviral Research 173 (January 2020): 104667. http://dx.doi.org/10.1016/j.antiviral.2019.104667.

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Sarybay, N., Zh Zh Chunetova, D. M. Iskakova, et al. "GENETIC ANALYSIS OF THE TYPES OF DEVELOPMENT OF MUTANT LINES FROM COMMON WHEAT VARIETIES." REPORTS 6, no. 334 (2020): 22–28. http://dx.doi.org/10.32014/2020.2518-1483.131.

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Among cereals, a special place is occupied by wheat as the main food of humanity and in improving the country's economy. The main task of breeding is to produce valuable wheat varieties that are stable to the unfavorable external environment of various natural climatic zones of Kazakhstan, consisting of a combination of valuable features. The prospects for the use of mutants in the process of hybridization are reflected in the achievements of world and domestic selection. The effect of various solutions of chemical compounds on the plant was observed from the first days during the growth of wh

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Root, Christiana N., Elizabeth G. Wills, LaShonn L. McNair, and Gary R. Whittaker. "Entry of influenza viruses into cells is inhibited by a highly specific protein kinase C inhibitor." Journal of General Virology 81, no. 11 (2000): 2697–705. http://dx.doi.org/10.1099/0022-1317-81-11-2697.

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Following binding to cell surface sialic acid, entry of influenza viruses into cells is mediated by endocytosis. Productive entry of influenza virus requires the low-pH environment of the late endosome for fusion and release of the virus into the cytoplasm and transport of the virus genome into the nucleus. We investigated novel mechanisms to inhibit influenza virus infection using highly specific inhibitors of protein kinase C. We found that one inhibitor, bisindolylmaleimide I, prevented replication of influenza A virus in a dose-dependent manner when added at the time of infection, but had

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Katoh, Hiroshi, Yuichiro Nakatsu, Toru Kubota, Masafumi Sakata, Makoto Takeda, and Minoru Kidokoro. "Mumps Virus Is Released from the Apical Surface of Polarized Epithelial Cells, and the Release Is Facilitated by a Rab11-Mediated Transport System." Journal of Virology 89, no. 23 (2015): 12026–34. http://dx.doi.org/10.1128/jvi.02048-15.

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ABSTRACTMumps virus (MuV) is an airborne virus that causes a systemic infection in patients.In vivo, the epithelium is a major replication site of MuV, and thus, the mode of MuV infection of epithelial cells is a subject of interest. Our data in the present study showed that MuV entered polarized epithelial cells via both the apical and basolateral surfaces, while progeny viruses were predominantly released from the apical surface. In polarized cells, intracellular transport of viral ribonucleoprotein (vRNP) complexes was dependent on Rab11-positive endosomes, and vRNP complexes were transport

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Chaimayo, Chutikarn, Tsuyoshi Hayashi, Andrew Underwood, Erin Hodges, and Toru Takimoto. "Selective incorporation of vRNP into influenza A virions determined by its specific interaction with M1 protein." Virology 505 (May 2017): 23–32. http://dx.doi.org/10.1016/j.virol.2017.02.008.

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Davis, Alicia M., Bryan J. Chabolla, and Laura L. Newcomb. "Emerging antiviral resistant strains of influenza A and the potential therapeutic targets within the viral ribonucleoprotein (vRNP) complex." Virology Journal 11, no. 1 (2014): 167. http://dx.doi.org/10.1186/1743-422x-11-167.

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Harris, F. A. J., H. A. Eagles, J. M. Virgona, P. J. Martin, J. R. Condon, and J. F. Angus. "Effect of VRN1 and PPD1 genes on anthesis date and wheat growth." Crop and Pasture Science 68, no. 3 (2017): 195. http://dx.doi.org/10.1071/cp16420.

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Phasic development of wheat is largely determined by the interaction of the VRN1 and PPD1 genes with vernalising temperature and photoperiod. VRN1 and PPD1 are regulatory genes, known to influence freezing tolerance, plant morphology and grain yield as well as phasic development. Forty-seven doubled-haploid lines were characterised for Ppd-B1, Ppd-D1, Vrn-A1, Vrn-B1 and Vrn-D1 to determine the effect of allelic combinations of these genes on timing of anthesis and crop growth rate. The lines were grown in replicated field experiments at two locations in Australia. The VRN1 and PPD1 genes accou

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Avilov, Sergiy V., Dorothée Moisy, Nadia Naffakh, and Stephen Cusack. "Influenza A virus progeny vRNP trafficking in live infected cells studied with the virus-encoded fluorescently tagged PB2 protein." Vaccine 30, no. 51 (2012): 7411–17. http://dx.doi.org/10.1016/j.vaccine.2012.09.077.

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Shimizu, Teppei, Naoki Takizawa, Ken Watanabe, Kyosuke Nagata, and Nobuyuki Kobayashi. "Crucial role of the influenza virus NS2 (NEP) C-terminal domain in M1 binding and nuclear export of vRNP." FEBS Letters 585, no. 1 (2010): 41–46. http://dx.doi.org/10.1016/j.febslet.2010.11.017.

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McCown, Matthew F., and Andrew Pekosz. "The Influenza A Virus M2 Cytoplasmic Tail Is Required for Infectious Virus Production and Efficient Genome Packaging." Journal of Virology 79, no. 6 (2005): 3595–605. http://dx.doi.org/10.1128/jvi.79.6.3595-3605.2005.

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ABSTRACT The M2 integral membrane protein encoded by influenza A virus possesses an ion channel activity that is required for efficient virus entry into host cells. The role of the M2 protein cytoplasmic tail in virus replication was examined by generating influenza A viruses encoding M2 proteins with truncated C termini. Deletion of 28 amino acids (M2Stop70) resulted in a virus that produced fourfold-fewer particles but >1,000-fold-fewer infectious particles than wild-type virus. Expression of the full-length M2 protein in trans restored the replication of the M2 truncated virus. Although

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Martínez-Alonso, Mónica, Narin Hengrung, and Ervin Fodor. "RNA-Free and Ribonucleoprotein-Associated Influenza Virus Polymerases Directly Bind the Serine-5-Phosphorylated Carboxyl-Terminal Domain of Host RNA Polymerase II." Journal of Virology 90, no. 13 (2016): 6014–21. http://dx.doi.org/10.1128/jvi.00494-16.

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ABSTRACTInfluenza viruses subvert the transcriptional machinery of their hosts to synthesize their own viral mRNA. Ongoing transcription by cellular RNA polymerase II (Pol II) is required for viral mRNA synthesis. By a process known as cap snatching, the virus steals short 5′ capped RNA fragments from host capped RNAs and uses them to prime viral transcription. An interaction between the influenza A virus RNA polymerase and the C-terminal domain (CTD) of the large subunit of Pol II has been established, but the molecular details of this interaction remain unknown. We show here that the influen

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Wyżewski, Zbigniew, and Karolina P. Gregorczyk. "The role of antiapoptotic Bcl-2 family proteins in the infection of influenza A virus." Postępy Higieny i Medycyny Doświadczalnej 72 (December 11, 2018): 1043–51. http://dx.doi.org/10.5604/01.3001.0012.7835.

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Bcl-2 family consists proteins responsible for apoptosis regulation. Influence of those factors on the cell viability is essential in the context of viral infections. Antiapoptotic activity of Mcl-1, Bcl-2, Bcl-xL and Bcl-w may favor effective replication IAV by keeping infected cell alive. On the other hand, Bcl-2 plays antiviral role at the late stage of IAV infection. Limiting the transport of newly synthesized vRNP from the cell nucleus to cytosol, Bcl-2 prevents effective montage of the progeny virions. Moreover Bcl-2 is responsible for modification of the IAV HA phosphorylation and conse

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Li, Junping, Libin Liang, Li Jiang, et al. "Viral RNA-binding ability conferred by SUMOylation at PB1 K612 of influenza A virus is essential for viral pathogenesis and transmission." PLOS Pathogens 17, no. 2 (2021): e1009336. http://dx.doi.org/10.1371/journal.ppat.1009336.

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Posttranslational modifications, such as SUMOylation, play specific roles in the life cycle of invading pathogens. However, the effect of SUMOylation on the adaptation, pathogenesis, and transmission of influenza A virus (IAV) remains largely unknown. Here, we found that a conserved lysine residue at position 612 (K612) of the polymerase basic protein 1 (PB1) of IAV is a bona fide SUMOylation site. SUMOylation of PB1 at K612 had no effect on the stability or cellular localization of PB1, but was critical for viral ribonucleoprotein (vRNP) complex activity and virus replication in vitro. When t

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Eagles, H. A., Jayne Wilson, Karen Cane, et al. "Frost-tolerance genes Fr-A2 and Fr-B2 in Australian wheat and their effects on days to heading and grain yield in lower rainfall environments in southern Australia." Crop and Pasture Science 67, no. 2 (2016): 119. http://dx.doi.org/10.1071/cp15276.

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FROST RESISTANCE 2 (FR2) genes of wheat are C-Repeat Binding Factor (CBF) genes with two major alleles known for both Fr-A2 (‘T’ and ‘S’) and Fr-B2 (‘WT’ and ‘DEL’). VERNALIZATION 1 (VRN1) genes have a regulatory role on CBF genes, with known epistatic interactions between Vrn-A1 and Fr-A2 for tolerance to freezing temperatures during vegetative growth. VRN1 genes were also known to affect days to heading and grain yield. Therefore, FR2 genes might also affect these traits. A wide range of cultivars was characterised for VRN1, Fr-A2 and Fr-B2 genes. A third allele of Fr-A2 was found in cvv Exc

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Ozawa, Makoto, Ken Fujii, Yukiko Muramoto, et al. "Contributions of Two Nuclear Localization Signals of Influenza A Virus Nucleoprotein to Viral Replication." Journal of Virology 81, no. 1 (2006): 30–41. http://dx.doi.org/10.1128/jvi.01434-06.

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ABSTRACT The RNA genome of influenza A virus, which forms viral ribonucleoprotein complexes (vRNPs) with viral polymerase subunit proteins (PA, PB1, and PB2) and nucleoprotein (NP), is transcribed and replicated in the nucleus. NP, the major component of vRNPs, has at least two amino acid sequences that serve as nuclear localization signals (NLSs): an unconventional NLS (residues 3 to 13; NLS1) and a bipartite NLS (residues 198 to 216; NLS2). Although both NLSs are known to play a role in nuclear transport, their relative contributions to viral replication are poorly understood. We therefore i

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Dubcovsky, Jorge, Artem Loukoianov, Daolin Fu, Miroslav Valarik, Alexandra Sanchez, and Liuling Yan. "Effect of Photoperiod on the Regulation of Wheat Vernalization Genes VRN1 and VRN2." Plant Molecular Biology 60, no. 4 (2006): 469–80. http://dx.doi.org/10.1007/s11103-005-4814-2.

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Lee, Ju-Young, Michael Edward C. Abundo, and Chang-Won Lee. "Herbal Medicines with Antiviral Activity Against the Influenza Virus, a Systematic Review." American Journal of Chinese Medicine 46, no. 08 (2018): 1663–700. http://dx.doi.org/10.1142/s0192415x18500854.

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The rapidly changing influenza virus has remained a consistent threat to the well-being of a variety of species on the planet. Influenza virus’ high mutation rate has allowed the virus to rapidly and continuously evolve, as well as generate new strains that are resistant to the current commercially available antivirals. Thus, the increased resistance has compelled the scientific community to explore alternative compounds that have antiviral effects against influenza virus. In this paper, the authors systematically review numerous herbal extracts that were shown to have antiviral effects agains

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Kippes, Nestor, Juan M. Debernardi, Hans A. Vasquez-Gross, et al. "Identification of theVERNALIZATION 4gene reveals the origin of spring growth habit in ancient wheats from South Asia." Proceedings of the National Academy of Sciences 112, no. 39 (2015): E5401—E5410. http://dx.doi.org/10.1073/pnas.1514883112.

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Wheat varieties with a winter growth habit require long exposures to low temperatures (vernalization) to accelerate flowering. Natural variation in four vernalization genes regulating this requirement has favored wheat adaptation to different environments. The first three genes (VRN1–VRN3) have been cloned and characterized before. Here we show that the fourth gene,VRN-D4, originated by the insertion of a ∼290-kb region from chromosome arm 5AL into the proximal region of chromosome arm 5DS. The inserted 5AL region includes a copy ofVRN-A1that carries distinctive mutations in its coding and reg

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Seppänen, Mervi M., Kirsi Pakarinen, Venla Jokela, Arja Santanen, and Perttu Virkajärvi. "Timotein kukintaan virittyminen ja sen yhteys korren laatuominaisuuksiin." Suomen Maataloustieteellisen Seuran Tiedote, no. 26 (January 31, 2010): 1–6. http://dx.doi.org/10.33354/smst.75729.

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Kasvuston rakenne määrää suurelta osin nurmikasvien sadon määrän. Tämä havaitaan selvimmin vertailtaessa timotein kevät- ja syyskasvustojen rakennetta ja sadon määrää; kevätsadossa esiintyy runsaasti korrellisia, kukintoja muodostavia versoja, kun taas syksyllä kasvusto on matalaa ja lehtevää, ja kortta muodostavien versojen määrä on alhainen. Kevätsato on myös määrällisesti suurempi. Korrellisten ja kukintoja muodostavien versojen määrä ohjailee myös nurmisadon laadun kehittymistä, sillä korren puutuminen kehityksen edetessä alentaa nopeasti rehun sulavuutta. Koska korren kasvulla ja kukkimis

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Ashour, Joseph, Florian I. Schmidt, Leo Hanke, et al. "Intracellular Expression of Camelid Single-Domain Antibodies Specific for Influenza Virus Nucleoprotein Uncovers Distinct Features of Its Nuclear Localization." Journal of Virology 89, no. 5 (2014): 2792–800. http://dx.doi.org/10.1128/jvi.02693-14.

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ABSTRACTPerturbation of protein-protein interactions relies mostly on genetic approaches or on chemical inhibition. Small RNA viruses, such as influenza A virus, do not easily lend themselves to the former approach, while chemical inhibition requires that the target protein be druggable. A lack of tools thus constrains the functional analysis of influenza virus-encoded proteins. We generated a panel of camelid-derived single-domain antibody fragments (VHHs) against influenza virus nucleoprotein (NP), a viral protein essential for nuclear trafficking and packaging of the influenza virus genome.

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Negulescu, Sorin C., Claudiu V. Kifor, and Constantin Oprean. "Ant Colony Solving Multiple Constraints Problem: Vehicle Route Allocation." International Journal of Computers Communications & Control 3, no. 4 (2008): 366. http://dx.doi.org/10.15837/ijccc.2008.4.2404.

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Ant colonies are successfully used nowadays as multi-agent systems (MAS) to solve difficult optimization problems such as travelling salesman (TSP), quadratic assignment (QAP), vehicle routing (VRP), graph coloring and satisfiability problem. The objective of the research presented in this paper is to adapt an improved version of Ant Colony Optimisation (ACO) algorithm, mainly: the Elitist Ant System (EAS) algorithm in order to solve the Vehicle Route Allocation Problem (VRAP). After a brief introduction in the first section about MAS and their characteristics, the paper presents the rationale

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Muterko, Alexandr, and Elena Salina. "Origin and Distribution of the VRN-A1 Exon 4 and Exon 7 Haplotypes in Domesticated Wheat Species." Agronomy 8, no. 8 (2018): 156. http://dx.doi.org/10.3390/agronomy8080156.

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The high adaptive potential of modern wheat to a wide range of environmental conditions is determined by genetic changes during domestication. Genetic diversity in VRN1 genes is a key contributor to this adaptability. Previously, the association between the transitions C->T within the fourth and seventh exons of VRN-A1, the distinguishing pair haplotypes Ex4C/Ex4T and Ex7C/Ex7T, and the modulation of such agronomically valuable traits as the vernalization requirement duration, frost tolerance and flowering time of wheat have been shown. However, this polymorphism was analyzed in only a few

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Ohta, Keisuke, Hideo Goto, Yusuke Matsumoto, Natsuko Yumine, Masato Tsurudome, and Machiko Nishio. "Graf1 Controls the Growth of Human Parainfluenza Virus Type 2 through Inactivation of RhoA Signaling." Journal of Virology 90, no. 20 (2016): 9394–405. http://dx.doi.org/10.1128/jvi.01471-16.

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ABSTRACTRho GTPases are involved in a variety of cellular activities and are regulated by guanine nucleotide exchange factors and GTPase-activating proteins (GAPs). We found that the activation of Rho GTPases by lysophosphatidic acid promotes the growth of human parainfluenza virus type 2 (hPIV-2). Furthermore, hPIV-2 infection causes activation of RhoA, a Rho GTPase. We hypothesized that Graf1 (also known as ARHGAP26), a GAP, regulates hPIV-2 growth by controlling RhoA signaling. Immunofluorescence analysis showed that hPIV-2 infection altered Graf1 localization from a homogenous distribution

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