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Journal articles on the topic 'Orb2'

Author: Grafiati

Published: 4 June 2021

Last updated: 15 February 2022

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1

Sanguanini, Michele, and Antonino Cattaneo. "A continuous model of physiological prion aggregation suggests a role for Orb2 in gating long-term synaptic information." Royal Society Open Science 5, no. 12 (December 2018): 180336. http://dx.doi.org/10.1098/rsos.180336.

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The regulation of mRNA translation at the level of the synapse is believed to be fundamental in memory and learning at the cellular level. The family of cytoplasmic polyadenylation element binding (CPEB) proteins emerged as an important RNA-binding protein family during development and in adult neurons. Drosophila Orb2 (homologue of mouse CPEB3 protein and of the neural isoform of Aplysia CPEB) has been found to be involved in the translation of plasticity-dependent mRNAs and has been associated with long-term memory. Orb2 protein presents two main isoforms, Orb2A and Orb2B, which form an activity-induced amyloid-like functional aggregate, thought to be the translation-inducing state of the RNA-binding protein. Here we present a first two-states continuous differential model for Orb2A–Orb2B aggregation. This model provides new working hypotheses for studying the role of prion-like CPEB proteins in long-term synaptic plasticity. Moreover, this model can be used as a first step to integrate translation- and protein aggregation-dependent phenomena in synaptic facilitation rules.

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2

Stepien, Barbara Krystyna, Cornelia Oppitz, Daniel Gerlach, Ugur Dag, Maria Novatchkova, Sebastian Krüttner, Alexander Stark, and Krystyna Keleman. "RNA-binding profiles of Drosophila CPEB proteins Orb and Orb2." Proceedings of the National Academy of Sciences 113, no. 45 (October 24, 2016): E7030—E7038. http://dx.doi.org/10.1073/pnas.1603715113.

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Localized protein translation is critical in many biological contexts, particularly in highly polarized cells, such as neurons, to regulate gene expression in a spatiotemporal manner. The cytoplasmic polyadenylation element-binding (CPEB) family of RNA-binding proteins has emerged as a key regulator of mRNA transport and local translation required for early embryonic development, synaptic plasticity, and long-term memory (LTM). Drosophila Orb and Orb2 are single members of the CPEB1 and CPEB2 subfamilies of the CPEB proteins, respectively. At present, the identity of the mRNA targets they regulate is not fully known, and the binding specificity of the CPEB2 subfamily is a matter of debate. Using transcriptome-wide UV cross-linking and immunoprecipitation, we define the mRNA-binding sites and targets of Drosophila CPEBs. Both Orb and Orb2 bind linear cytoplasmic polyadenylation element-like sequences in the 3′ UTRs of largely overlapping target mRNAs, with Orb2 potentially having a broader specificity. Both proteins use their RNA-recognition motifs but not the Zinc-finger region for RNA binding. A subset of Orb2 targets is translationally regulated in cultured S2 cells and fly head extracts. Moreover, pan-neuronal RNAi knockdown of these targets suggests that a number of these targets are involved in LTM. Our results provide a comprehensive list of mRNA targets of the two CPEB proteins in Drosophila, thus providing insights into local protein synthesis involved in various biological processes, including LTM.

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3

Hervas, Ruben, Michael J. Rau, Younshim Park, Wenjuan Zhang, Alexey G. Murzin, James A. J. Fitzpatrick, Sjors H. W. Scheres, and Kausik Si. "Cryo-EM structure of a neuronal functional amyloid implicated in memory persistence in Drosophila." Science 367, no. 6483 (March 12, 2020): 1230–34. http://dx.doi.org/10.1126/science.aba3526.

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How long-lived memories withstand molecular turnover is a fundamental question. Aggregates of a prion-like RNA-binding protein, cytoplasmic polyadenylation element–binding (CPEB) protein, is a putative substrate of long-lasting memories. We isolated aggregated Drosophila CPEB, Orb2, from adult heads and determined its activity and atomic structure, at 2.6-angstrom resolution, using cryo–electron microscopy. Orb2 formed ~75-nanometer-long threefold-symmetric amyloid filaments. Filament formation transformed Orb2 from a translation repressor to an activator and “seed” for further translationally active aggregation. The 31–amino acid protofilament core adopted a cross-β unit with a single hydrophilic hairpin stabilized through interdigitated glutamine packing. Unlike the hydrophobic core of pathogenic amyloids, the hydrophilic core of Orb2 filaments suggests how some neuronal amyloids could be a stable yet regulatable substrate of memory.

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4

Welberg, Leonie. "ORB2 marks the spot." Nature Reviews Neuroscience 8, no. 12 (December 2007): 909. http://dx.doi.org/10.1038/nrn2290.

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5

Falk, Alexander S., Silvia A. Cervantes, Maria A. Conrad-Soria, Thalia H. Bajakian, and Ansgar B. Siemer. "Exploring the Orb2 Fibril Core." Biophysical Journal 110, no. 3 (February 2016): 534a. http://dx.doi.org/10.1016/j.bpj.2015.11.2858.

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6

White-Grindley, Erica, Liying Li, Repon Mohammad Khan, Fengzhen Ren, Anita Saraf, Laurence Florens, and Kausik Si. "Contribution of Orb2A Stability in Regulated Amyloid-Like Oligomerization of Drosophila Orb2." PLoS Biology 12, no. 2 (February 11, 2014): e1001786. http://dx.doi.org/10.1371/journal.pbio.1001786.

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7

Oroz, Javier, Sara S. Félix, Eurico J. Cabrita, and Douglas V. Laurents. "Structural transitions in Orb2 prion-like domain relevant for functional aggregation in memory consolidation." Journal of Biological Chemistry 295, no. 52 (October 22, 2020): 18122–33. http://dx.doi.org/10.1074/jbc.ra120.015211.

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The recent structural elucidation of ex vivo Drosophila Orb2 fibrils revealed a novel amyloid formed by interdigitated Gln and His residue side chains belonging to the prion-like domain. However, atomic-level details on the conformational transitions associated with memory consolidation remain unknown. Here, we have characterized the nascent conformation and dynamics of the prion-like domain (PLD) of Orb2A using a nonconventional liquid-state NMR spectroscopy strategy based on 13C detection to afford an essentially complete set of 13Cα, 13Cβ, 1Hα, and backbone 13CO and 15N assignments. At pH 4, where His residues are protonated, the PLD is disordered and flexible, except for a partially populated α-helix spanning residues 55–60, and binds RNA oligos, but not divalent cations. At pH 7, in contrast, His residues are predominantly neutral, and the Q/H segments adopt minor populations of helical structure, show decreased mobility and start to self-associate. At pH 7, the His residues do not bind RNA or Ca2+, but do bind Zn2+, which promotes further association. These findings represent a remarkable case of structural plasticity, based on which an updated model for Orb2A functional amyloidogenesis is suggested.

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8

Hervás, Rubén, Alexey G. Murzin, and Kausik Si. "Implications of the Orb2 Amyloid Structure in Huntington’s Disease." International Journal of Molecular Sciences 21, no. 18 (September 21, 2020): 6910. http://dx.doi.org/10.3390/ijms21186910.

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Huntington’s disease is a progressive, autosomal dominant, neurodegenerative disorder caused by an expanded CAG repeat in the huntingtin gene. As a result, the translated protein, huntingtin, contains an abnormally long polyglutamine stretch that makes it prone to misfold and aggregating. Aggregation of huntingtin is believed to be the cause of Huntington’s disease. However, understanding on how, and why, huntingtin aggregates are deleterious has been hampered by lack of enough relevant structural data. In this review, we discuss our recent findings on a glutamine-based functional amyloid isolated from Drosophila brain and how this information provides plausible structural insight on the structure of huntingtin deposits in the brain.

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9

Ashami, Kidist, Alexander S. Falk, Connor Hurd, Samridhi Garg, Silvia A. Cervantes, Anoop Rawat, and Ansgar B. Siemer. "Droplet and fibril formation of the functional amyloid Orb2." Journal of Biological Chemistry 297, no. 1 (July 2021): 100804. http://dx.doi.org/10.1016/j.jbc.2021.100804.

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10

Kimura, Shingo, Yasufumi Sakakibara, Kosei Sato, Manabu Ote, Hiroki Ito, Masayuki Koganezawa, and Daisuke Yamamoto. "TheDrosophilalingerer protein cooperates with Orb2 in long-term memory formation." Journal of Neurogenetics 29, no. 1 (July 7, 2014): 8–17. http://dx.doi.org/10.3109/01677063.2014.917644.

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11

Hervás, Rubén, Liying Li, Amitabha Majumdar, María del Carmen Fernández-Ramírez, Jay R. Unruh, Brian D. Slaughter, Albert Galera-Prat, et al. "Molecular Basis of Orb2 Amyloidogenesis and Blockade of Memory Consolidation." PLOS Biology 14, no. 1 (January 26, 2016): e1002361. http://dx.doi.org/10.1371/journal.pbio.1002361.

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12

Agnoli, Kirsty, Carolyn A. Lowe, Kate L. Farmer, Seyyed I. Husnain, and Mark S. Thomas. "The Ornibactin Biosynthesis and Transport Genes of Burkholderia cenocepacia Are Regulated by an Extracytoplasmic Function σ Factor Which Is a Part of the Fur Regulon." Journal of Bacteriology 188, no. 10 (May 15, 2006): 3631–44. http://dx.doi.org/10.1128/jb.188.10.3631-3644.2006.

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ABSTRACT Burkholderia cenocepacia mutants that fail to produce the siderophore ornibactin were obtained following mutagenesis with mini-Tn5Tp. These mutants were shown to be growth restricted under conditions of iron depletion. In eight of the mutants, the transposon had integrated into one of two genes, orbI and orbJ, encoding nonribosomal peptide synthetases. In the other mutant, the transposon had inserted into an open reading frame, orbS, located upstream from orbI. The polypeptide product of orbS exhibits a high degree of similarity to the Pseudomonas aeruginosa extracytoplasmic function (ECF) σ factor PvdS but possesses an N-terminal extension of approximately 29 amino acids that is not present in PvdS. Three predicted OrbS-dependent promoters were identified within the ornibactin gene cluster, based on their similarity to PvdS-dependent promoters. The iron-regulated activity of these promoters was shown to require OrbS. Transcription of the orbS gene was found to be under the control of an iron-regulated σ70-dependent promoter. This promoter, but not the OrbS-dependent promoters, was shown to be a target for repression by the global regulator Fur. Our results demonstrate that production of ornibactin by B. cenocepacia in response to iron starvation requires transcription of an operon that is dependent on the Fur-regulated ECF σ factor gene orbS. A mechanism is also proposed for the biosynthesis of ornibactin.

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13

Keleman, Krystyna, Sebastian Krüttner, Mattias Alenius, and Barry J. Dickson. "Function of the Drosophila CPEB protein Orb2 in long-term courtship memory." Nature Neuroscience 10, no. 12 (October 28, 2007): 1587–93. http://dx.doi.org/10.1038/nn1996.

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14

Xu, Shuwa, Nathaniel Hafer, Blessing Agunwamba, and Paul Schedl. "The CPEB Protein Orb2 Has Multiple Functions during Spermatogenesis in Drosophila melanogaster." PLoS Genetics 8, no. 11 (November 29, 2012): e1003079. http://dx.doi.org/10.1371/journal.pgen.1003079.

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15

Bajakian, Thalia H., Silvia A. Cervantes, Maria A. Soria, Maïwenn Beaugrand, Ji Yun Kim, Rachel J. Service, and Ansgar B. Siemer. "Metal Binding Properties of the N-Terminus of the Functional Amyloid Orb2." Biomolecules 7, no. 4 (August 1, 2017): 57. http://dx.doi.org/10.3390/biom7030057.

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16

Santana, Elena, and Sergio Casas-Tintó. "Orb2 as modulator of Brat and their role at the neuromuscular junction." Journal of Neurogenetics 31, no. 4 (October 2, 2017): 181–88. http://dx.doi.org/10.1080/01677063.2017.1393539.

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17

Khan, Mohammed Repon, Liying Li, Consuelo Pérez-Sánchez, Anita Saraf, Laurence Florens, Brian D. Slaughter, Jay R. Unruh, and Kausik Si. "Amyloidogenic Oligomerization Transforms Drosophila Orb2 from a Translation Repressor to an Activator." Cell 163, no. 6 (December 2015): 1468–83. http://dx.doi.org/10.1016/j.cell.2015.11.020.

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18

Mastushita-Sakai, T., E. White-Grindley, J. Samuelson, C. Seidel, and K. Si. "Drosophila Orb2 targets genes involved in neuronal growth, synapse formation, and protein turnover." Proceedings of the National Academy of Sciences 107, no. 26 (June 14, 2010): 11987–92. http://dx.doi.org/10.1073/pnas.1004433107.

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19

Majumdar, Amitabha, Wanda Colón Cesario, Erica White-Grindley, Huoqing Jiang, Fengzhen Ren, Mohammed “Repon” Khan, Liying Li, et al. "Critical Role of Amyloid-like Oligomers of Drosophila Orb2 in the Persistence of Memory." Cell 148, no. 3 (February 2012): 515–29. http://dx.doi.org/10.1016/j.cell.2012.01.004.

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20

Xu, Shuwa, Sanjay Tyagi, and Paul Schedl. "Spermatid Cyst Polarization in Drosophila Depends upon apkc and the CPEB Family Translational Regulator orb2." PLoS Genetics 10, no. 5 (May 15, 2014): e1004380. http://dx.doi.org/10.1371/journal.pgen.1004380.

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21

Hafer, Nathaniel, Shuwa Xu, Krishna Moorthi Bhat, and Paul Schedl. "TheDrosophilaCPEB Protein Orb2 Has a Novel Expression Pattern and Is Important for Asymmetric Cell Division and Nervous System Function." Genetics 189, no. 3 (September 6, 2011): 907–21. http://dx.doi.org/10.1534/genetics.110.123646.

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22

Kiely, Joan, S. B. Haase, Paul Russell, and Janet Leatherwood. "Functions of Fission Yeast Orp2 in DNA Replication and Checkpoint Control." Genetics 154, no. 2 (February 1, 2000): 599–607. http://dx.doi.org/10.1093/genetics/154.2.599.

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Abstract orp2 is an essential gene of the fission yeast Schizosaccharomyces pombe with 22% identity to budding yeast ORC2. We isolated temperature-sensitive alleles of orp2 using a novel plasmid shuffle based on selection against thymidine kinase. Cells bearing the temperature-sensitive allele orp2-2 fail to complete DNA replication at a restrictive temperature and undergo cell cycle arrest. Cell cycle arrest depends on the checkpoint genes rad1 and rad3. Even when checkpoint functions are wild type, the orp2-2 mutation causes high rates of chromosome and plasmid loss. These phenotypes support the idea that Orp2 is a replication initiation factor. Selective spore germination allowed analysis of orp2 deletion mutants. These experiments showed that in the absence of orp2 function, cells proceed into mitosis despite a lack of DNA replication. This suggests either that the Orp2 protein is a part of the checkpoint machinery or more likely that DNA replication initiation is required to induce the replication checkpoint signal.

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23

Vas, Amit, Winnie Mok, and Janet Leatherwood. "Control of DNA Rereplication via Cdc2 Phosphorylation Sites in the Origin Recognition Complex." Molecular and Cellular Biology 21, no. 17 (September 1, 2001): 5767–77. http://dx.doi.org/10.1128/mcb.21.17.5767-5777.2001.

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ABSTRACT Cdc2 kinase is a master regulator of cell cycle progression in the fission yeast Schizosaccharomyces pombe. Our data indicate that Cdc2 phosphorylates replication factor Orp2, a subunit of the origin recognition complex (ORC). Cdc2 phosphorylation of Orp2 appears to be one of multiple mechanisms by which Cdc2 prevents DNA rereplication in a single cell cycle. Cdc2 phosphorylation of Orp2 is not required for Cdc2 to activate DNA replication initiation. Phosphorylation of Orp2 appears first in S phase and becomes maximal in G2 and M when Cdc2 kinase activity is required to prevent reinitiation of DNA replication. A mutant lacking Cdc2 phosphorylation sites in Orp2 (orp2-T4A) allowed greater rereplication of DNA than congenic orp2 wild-type strains when the limiting replication initiation factor Cdc18 was deregulated. Thus, Cdc2 phosphorylation of Orp2 may be redundant with regulation of Cdc18 for preventing reinitiation of DNA synthesis. Since Cdc2 phosphorylation sites are present in Orp2 (also known as Orc2) from yeasts to metazoans, we propose that cell cycle-regulated phosphorylation of the ORC provides a safety net to prevent DNA rereplication and resulting genetic instability.

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24

Uchiyama, Masashi, and Teresa S. F. Wang. "The B-Subunit of DNA Polymerase α-Primase Associates with the Origin Recognition Complex for Initiation of DNA Replication." Molecular and Cellular Biology 24, no. 17 (September 1, 2004): 7419–34. http://dx.doi.org/10.1128/mcb.24.17.7419-7434.2004.

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ABSTRACT The B-subunit (p70/Pol12p) of the DNA polymerase α-primase (Polα-primase) complex is thought to have a regulatory role in an early stage of S phase. We generated a panel of fission yeast thermosensitive mutants of the B-subunit (termed Spb70) to investigate its role in initiation of DNA replication by genetic and biochemical approaches. Here, we show that the fission yeast Spb70 genetically interacts and coprecipitates with origin recognition complex proteins Orp1/Orc1 and Orp2/Orc2 and primase coupling subunit Spp2/p58. A fraction of Spb70 associates with Orp2 on chromatin throughout the cell cycle independent of the other subunits of Polα-primase. Furthermore, primase Spp2/p58 subunit preferentially associates with the unphosphorylated Orp2, and the association requires Spb70. Mutations in orp2+ that abolish or mimic the Cdc2 phosphorylation of Orp2 suppress or exacerbate the thermosensitivity of the spb70 mutants, respectively, indicating that an unphosphorylated Orp2 promotes an Spb70-dependent replication event. Together, these results indicate that the chromatin-bound B-subunit in association with origin recognition complex mediates recruiting Polα-primase complex onto replication origins in G1 pre-Start through an interaction with primase Spp2/p58 subunit. Our results thus suggest a role for the recruited Polα-primase in the initiation of both leading and lagging strands at the replication origins.

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25

Mota, Luı́s Jaime, Leonor Morais Sarmento, and Isabel de Sá-Nogueira. "Control of the Arabinose Regulon in Bacillus subtilisby AraR In Vivo: Crucial Roles of Operators, Cooperativity, and DNA Looping." Journal of Bacteriology 183, no. 14 (July 15, 2001): 4190–201. http://dx.doi.org/10.1128/jb.183.14.4190-4201.2001.

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ABSTRACT The proteins involved in the utilization of l-arabinose by Bacillus subtilis are encoded by thearaABDLMNPQ-abfA metabolic operon and by thearaE/araR divergent unit. Transcription from the ara operon, araE transport gene, andaraR regulatory gene is induced by l-arabinose and negatively controlled by AraR. The purified AraR protein binds cooperatively to two in-phase operators within thearaABDLMNPQ-abfA (ORA1 and ORA2) and araE (ORE1 and ORE2) promoters and noncooperatively to a single operator in the araR (ORR3) promoter region. Here, we have investigated how AraR controls transcription from theara regulon in vivo. A deletion analysis of theara promoters region showed that the five AraR binding sites are the key cis-acting regulatory elements of their corresponding genes. Furthermore, ORE1-ORE2 and ORR3 are auxiliary operators for the autoregulation ofaraR and the repression of araE, respectively. Analysis of mutations designed to prevent cooperative binding of AraR showed that in vivo repression of the ara operon requires communication between repressor molecules bound to two properly spaced operators. This communication implicates the formation of a small loop by the intervening DNA. In an in vitro transcription system, AraR alone sufficed to abolish transcription from thearaABDLMNPQ-abfA operon and araEpromoters, strongly suggesting that it is the major protein involved in the repression mechanism of l-arabinose-inducible expression in vivo. The ara regulon is an example of how the architecture of the promoters is adapted to respond to the particular characteristics of the system, resulting in a tight and flexible control.

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26

Ozaki, Yuki, Shingo Suzuki, Atsuko Shigenari, Sayaka Ito, Yuko Okudaira, Anri Masuya, Shigeki Mitsunaga, Masao Ota, Hidetoshi Inoko, and Takashi Shiina. "OR02." Human Immunology 75 (October 2014): 2. http://dx.doi.org/10.1016/j.humimm.2014.08.005.

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27

Freedom, David, Daniel Magas, Katarzyna Brooks, Bozena Labuda, and Andres Jaramillo. "OR12." Human Immunology 75 (October 2014): 9. http://dx.doi.org/10.1016/j.humimm.2014.08.015.

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28

Li, Fang, Nicole Valenzuela, Xiaohai Zhang, and Elaine F. Reed. "OR22." Human Immunology 75 (October 2014): 19. http://dx.doi.org/10.1016/j.humimm.2014.08.025.

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29

Wang, Qi, Chih-Hung Lai, Mehrnoush Naim, Geraldine Ong, and Nancy L. Reinsmoen. "OR32." Human Immunology 75 (October 2014): 28. http://dx.doi.org/10.1016/j.humimm.2014.08.035.

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30

Gerritsen, Kevin E. H., Marie-Odile Joannis, Lotte Wieten, Birgit L. M. G. Senden-Gijsbers, Frantz Agis, Christina E. M. Voorter, and Marcel G. J. Tilanus. "OR42." Human Immunology 75 (October 2014): 36. http://dx.doi.org/10.1016/j.humimm.2014.08.045.

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31

Willey, Patricia, V. Subramanian, M. Gunasekaran, D. Phelan, R. Delos Santos, J. Wellen, S. Shenoy, and T. Mohanakumar. "OR52." Human Immunology 75 (October 2014): 45. http://dx.doi.org/10.1016/j.humimm.2014.08.055.

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32

Pezzoni, Giulia, Lidia Stercoli, Eleonora Pegoiani, and Emiliana Brocchi. "Antigenic Characterization of ORF2 and ORF3 Proteins of Hepatitis E Virus (HEV)." Viruses 13, no. 7 (July 16, 2021): 1385. http://dx.doi.org/10.3390/v13071385.

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To evaluate the antigenic properties of Hepatitis E Virus (HEV) Open Reading Frame 2 and 3 (ORF2 and ORF3) codified proteins, we expressed different portions of ORF2 and the entire ORF3 in E. coli, a truncated ORF2, was also expressed in baculovirus. A panel of 37 monoclonal antibodies (MAbs) was raised against ORF2 (1–660 amino acids) and MAbs were mapped and characterized using the ORF2 expressed portions. Selected HEV positive and negative swine sera were used to evaluate ORF2 and ORF3 antigens’ immunogenicity. The MAbs were clustered in six groups identifying six antigenic regions along the ORF2. Only MAbs binding to the sixth ORF2 antigenic region (394–608 aa) were found to compete with HEV positive sera and efficiently catch the recombinant antigen expressed in baculovirus. The ORF2 portion from 394–608 aa demonstrated to include most immunogenic epitopes with 85% of HEV positive swine sera reacting against the region from 461–544 aa. Only 5% of the selected HEV sera reacted against the ORF3 antigen.

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33

Lee, Kyung Yong, Sung Woong Bang, Sang Wook Yoon, Seung-Hoon Lee, Jong-Bok Yoon, and Deog Su Hwang. "Phosphorylation of ORC2 Protein Dissociates Origin Recognition Complex from Chromatin and Replication Origins." Journal of Biological Chemistry 287, no. 15 (February 13, 2012): 11891–98. http://dx.doi.org/10.1074/jbc.m111.338467.

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During the late M to the G1 phase of the cell cycle, the origin recognition complex (ORC) binds to the replication origin, leading to the assembly of the prereplicative complex for subsequent initiation of eukaryotic chromosome replication. We found that the cell cycle-dependent phosphorylation of human ORC2, one of the six subunits of ORC, dissociates ORC2, -3, -4, and -5 (ORC2–5) subunits from chromatin and replication origins. Phosphorylation at Thr-116 and Thr-226 of ORC2 occurs by cyclin-dependent kinase during the S phase and is maintained until the M phase. Phosphorylation of ORC2 at Thr-116 and Thr-226 dissociated the ORC2–5 from chromatin. Consistent with this, the phosphomimetic ORC2 protein exhibited defective binding to replication origins as well as to chromatin, whereas the phosphodefective protein persisted in binding throughout the cell cycle. These results suggest that the phosphorylation of ORC2 dissociates ORC from chromatin and replication origins and inhibits binding of ORC to newly replicated DNA.

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34

Guo, H., E. M. Zhou, Z. F. Sun, X. J. Meng, and P. G. Halbur. "Identification of B-cell epitopes in the capsid protein of avian hepatitis E virus (avian HEV) that are common to human and swine HEVs or unique to avian HEV." Journal of General Virology 87, no. 1 (January 1, 2006): 217–23. http://dx.doi.org/10.1099/vir.0.81393-0.

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Avian hepatitis E virus (avian HEV) was recently discovered in chickens from the USA that had hepatitis–splenomegaly (HS) syndrome. The complete genomic sequence of avian HEV shares about 50 % nucleotide sequence identity with those of human and swine HEVs. The open reading frame 2 (ORF2) protein of avian HEV has been shown to cross-react with human and swine HEV ORF2 proteins, but the B-cell epitopes in the avian HEV ORF2 protein have not been identified. Nine synthetic peptides from the predicted four antigenic domains of the avian HEV ORF2 protein were synthesized and corresponding rabbit anti-peptide antisera were generated. Using recombinant ORF2 proteins, convalescent pig and chicken antisera, peptides and anti-peptide rabbit sera, at least one epitope at the C terminus of domain II (possibly between aa 477–492) that is unique to avian HEV, one epitope in domain I (aa 389–410) that is common to avian, human and swine HEVs, and one or more epitopes in domain IV (aa 583–600) that are shared between avian and human HEVs were identified. Despite the sequence difference in ORF2 proteins between avian and mammalian HEVs and similar ORF2 sequence between human and swine HEV ORF2 proteins, rabbit antiserum against peptide 6 (aa 389–399) recognized only human HEV ORF2 protein, suggesting complexity of the ORF2 antigenicity. The identification of these B-cell epitopes in avian HEV ORF2 protein may be useful for vaccine design and may lead to future development of immunoassays for differential diagnosis of avian, swine and human HEV infections.

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35

Mou, Chunxiao, Minmin Wang, Shuonan Pan, and Zhenhai Chen. "Identification of Nuclear Localization Signals in the ORF2 Protein of Porcine Circovirus Type 3." Viruses 11, no. 12 (November 22, 2019): 1086. http://dx.doi.org/10.3390/v11121086.

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Porcine circovirus type 3 (PCV3) contains two major open reading frames (ORFs) and the ORF2 gene encodes the major structural capsid protein. In this study, nuclear localization of ORF2 was demonstrated by fluorescence observation and subcellular fractionation assays in ORF2-transfected PK-15 cells. The subcellular localization of truncated ORF2 indicated that the 38 N-terminal amino acids were responsible for the nuclear localization of ORF2. The truncated and site-directed mutagenesis of this domain were constructed, and the results demonstrated that the basic amino acid residues at positions 8–32 were essential for the strict nuclear localization. The basic motifs 8RRR-R-RRR16 and 16RRRHRRR22 were further shown to be the key functional nucleolar localization signals that guide PCV3 ORF2 into nucleoli. Furthermore, sequence analysis showed that the amino acids of PCV3 nuclear localization signals were highly conserved. Overall, this study provides insight into the biological and functional characteristics of the PCV3 ORF2 protein.

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36

Hynynen, Riikka, Saara Laitinen, Reijo Käkelä, Kimmo Tanhuanpää, Sari Lusa, Christian Ehnholm, Pentti Somerharju, Elina Ikonen, and Vesa M. Olkkonen. "Overexpression of OSBP-related protein 2 (ORP2) induces changes in cellular cholesterol metabolism and enhances endocytosis." Biochemical Journal 390, no. 1 (August 9, 2005): 273–83. http://dx.doi.org/10.1042/bj20042082.

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ORP2 [OSBP (oxysterol-binding protein)-related protein 2] belongs to the 12-member mammalian ORP gene/protein family. We characterize in the present study the effects of inducible ORP2 overexpression on cellular cholesterol metabolism in HeLa cells and compare the results with those obtained for CHO cells (Chinese-hamster ovary cells) that express ORP2 constitutively. In both cell systems, the prominent phenotype is enhancement of [14C]cholesterol efflux to all extracellular acceptors, which results in a reduction of cellular free cholesterol. No change was observed in the plasma membrane cholesterol content or distribution between raft and non-raft domains upon ORP2 expression. However, elevated HMG-CoA (3-hydroxy-3-methylglutaryl-CoA) reductase activity and LDL (low-density lipoprotein) receptor expression, as well as enhanced transport of newly synthesized cholesterol to a cyclodextrin-accessible pool, suggest that the ORP2 expression stimulates transport of cholesterol out of the endoplasmic reticulum. In contrast with ORP2/CHO cells, the inducible ORP2/HeLa cells do not show down-regulation of cholesterol esterification, suggesting that this effect represents an adaptive response to long-term cholesterol depletion in the CHO cell model. Finally, we provide evidence that ORP2 binds PtdIns(3,4,5)P3 and enhances endocytosis, phenomena that are probably interconnected. Our results suggest a function of ORP2 in both cholesterol trafficking and control of endocytic membrane transport.

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Lekcharoensuk, Porntippa, Igor Morozov, Prem S. Paul, Nattarat Thangthumniyom, Worawidh Wajjawalku, and X. J. Meng. "Epitope Mapping of the Major Capsid Protein of Type 2 Porcine Circovirus (PCV2) by Using Chimeric PCV1 and PCV2." Journal of Virology 78, no. 15 (August 1, 2004): 8135–45. http://dx.doi.org/10.1128/jvi.78.15.8135-8145.2004.

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ABSTRACT Type 2 porcine circovirus (PCV2) is associated with postweaning multisystemic wasting syndrome in pigs, whereas the genetically related type 1 PCV (PCV1) is nonpathogenic. In this study, seven monoclonal antibodies (MAbs) against PCV2-ORF2 capsid protein were generated, biologically characterized, and subsequently used to map the antigenic sites of PCV2 capsid protein by using infectious PCV DNA clones containing PCV1/PCV2-ORF2 chimeras. The PCV1/PCV2-ORF2 chimeras were constructed by serial deletions of PCV2-ORF2 and replacement with the corresponding sequences of the PCV1-ORF2. The reactivities of chimeric PCV1/PCV2 clones in transfected PK-15 cells with the seven MAbs were detected by an immunofluorescence assay (IFA). The chimera (r140) with a deletion of 47 amino acids at the N terminus of PCV2-ORF2 reacted strongly to all seven MAbs. Expanding the deletion of PCV2-ORF2 from residues 47 to 57 (r175) abolished the recognition of MAb 3B7, 3C11, 4A10, 6H2, or 8F6 to the chimera. Further deletion of PCV2-ORF2 to 62 residues disrupted the binding of this chimera to all seven MAbs. IFA reactivities with all MAbs were absent when residues 165 to 233 at the C terminus of PCV2-ORF2 was replaced with that of PCV1-ORF2. Extending the sequence of PCV2-ORF2 from residues 165 (r464) to 185 (r526), 200 (r588), or 224 (r652) restored the ability of the three chimeras to react with MAbs 3C11, 6H2, 9H7, and 12G3 but not with 8F6, 3B7, or 4A10. When the four amino acids at the C terminus of r588 were replaced with that of PCV2-ORF2, the resulting chimera (r588F) reacted with all seven MAbs. The results from this study suggest that these seven MAbs recognized at least five different but overlapping conformational epitopes within residues 47 to 63 and 165 to 200 and the last four amino acids at the C terminus of the PCV2 capsid protein.

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Sato, Hitoshi, Lesley Pesnicak, and Jeffrey I. Cohen. "Varicella-Zoster Virus Open Reading Frame 2 Encodes a Membrane Phosphoprotein That Is Dispensable for Viral Replication and for Establishment of Latency." Journal of Virology 76, no. 7 (April 1, 2002): 3575–78. http://dx.doi.org/10.1128/jvi.76.7.3575-3578.2002.

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ABSTRACT Varicella-zoster virus (VZV) encodes six genes that do not have homologs in herpes simplex virus. One of these genes, VZV open reading frame 2 (ORF2), was expressed as a 31-kDa phosphoprotein in the membranes of infected cells. Unlike equine and bovine herpesvirus type 1 ORF2 homologs that are associated with virions, VZV virions contained no detectable ORF2 protein. The ORF2 deletion mutant established a latent infection in cotton rats at a frequency and with a number of VZV genomes similar to that of the parental virus. ORF63 transcripts, a hallmark of latent infection, were present in ganglia latently infected with both the ORF2 deletion mutant and parental VZV. Thus, ORF2 is the first VZV gene shown to be dispensable for establishment of latent infection in an animal model.

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Surjit, Milan, Shahid Jameel, and Sunil K. Lal. "Cytoplasmic Localization of the ORF2 Protein of Hepatitis E Virus Is Dependent on Its Ability To Undergo Retrotranslocation from the Endoplasmic Reticulum." Journal of Virology 81, no. 7 (January 17, 2007): 3339–45. http://dx.doi.org/10.1128/jvi.02039-06.

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ABSTRACT Hepatitis E virus (HEV) is a positive-strand RNA virus that is prevalent in much of the developing world. ORF2 is the major capsid protein of HEV. Although ORF2 is an N-linked glycoprotein, it is abundantly located in the cytoplasm in addition to having membrane and surface localization. The mechanism by which ORF2 protein obtains access to the cytoplasm is unknown. In this report, we prove that initially all ORF2 protein is present in the endoplasmic reticulum and a fraction of it becomes retrotranslocated to the cytoplasm. The ability of ORF2 to be retrotranslocated is dependent on its glycosylation status and follows the canonical dislocation pathway. However, in contrast to general substrates of the dislocation pathway, retrotranslocated ORF2 protein is not a substrate of the 26S proteasome complex and is readily detectable in the cytoplasm in the absence of any protease inhibitor, suggesting that the retrotranslocated protein is stable in the cytoplasm. This study thus defines the pathway by which ORF2 obtains access to the cytoplasm.

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Bertolotti-Ciarlet, Andrea, Sue E. Crawford, Anne M. Hutson, and Mary K. Estes. "The 3′ End of Norwalk Virus mRNA Contains Determinants That Regulate the Expression and Stability of the Viral Capsid Protein VP1: a Novel Function for the VP2 Protein." Journal of Virology 77, no. 21 (November 1, 2003): 11603–15. http://dx.doi.org/10.1128/jvi.77.21.11603-11615.2003.

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ABSTRACT Norwalk virus (NV) is the prototype strain of a group of noncultivable human caliciviruses responsible for epidemic outbreaks of acute gastroenteritis. The capsid protein VP1 is synthesized from a subgenomic RNA that contains two open reading frames (ORFs), ORF2 and ORF3, and the 3′ untranslated region (UTR). ORF2 and ORF3 code for the capsid protein (VP1) and a small structural basic protein (VP2), respectively. We discovered that the yields of virus-like particles (VLPs) composed of VP1 are significantly reduced when this protein is expressed from ORF2 alone. To determine how the 3′ terminus of the NV subgenomic RNA regulates VP1 expression, we compared VP1 expression levels by using recombinant baculovirus constructs containing different 3′ elements. High VP1 levels were detected by using a recombinant baculovirus that contained ORF2, ORF3, and the 3′UTR (ORF2+3+3′UTR). In contrast, expression of VP1 from constructs that lacked the 3′UTR (ORF2+3), ORF3 (ORF2+3′UTR), or both (ORF2 alone) was highly reduced. Elimination of VP2 synthesis from the subgenomic RNA by mutation resulted in VP1 levels similar to those obtained with the ORF2 construct alone, suggesting a cis role for VP2 in upregulation of VP1 expression levels. Comparisons of the kinetics of RNA and capsid protein expression levels by using constructs with or without ORF3 or the 3′UTR revealed that the 3′UTR increased the levels of VP1 RNA, whereas the presence of VP2 resulted in increased levels of VP1. Furthermore, VP2 increased VP1 stability and protected VP1 from disassembly and protease degradation. The increase in VP1 expression levels caused by the presence of VP2 in cis was also observed in mammalian cells.

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Espinosa, Jennifer A., David J. Ortinau, Nina Krey, and Lisa Monahan. "I’ll have the usual: how restaurant brand image, loyalty, and satisfaction keep customers coming back." Journal of Product & Brand Management 27, no. 6 (September 17, 2018): 599–614. http://dx.doi.org/10.1108/jpbm-10-2017-1610.

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Purpose The purpose of this paper is to study how repeat customers utilize their established overall restaurant brand image (ORBI), overall restaurant loyalty, satisfaction and behavioral intentions (revisit, recommend) to reengage with a casual-dining restaurant brand. Design/methodology/approach The study design consists of a mixed-methods, two-phase research approach that includes both qualitative and quantitative data. First, focus groups and in-depth interviews with adult customers reveal preliminary insights on restaurant dining patterns and familiarity with franchised casual dining restaurants. Second, an online self-administered survey tests the influence of ORBI on repeat customers’ overall restaurant loyalty, satisfaction and behavioral intentions. Findings For repeat customers, ORBI positively predicts loyalty and satisfaction. Loyalty and satisfaction mediate the relationship between ORBI and intentions to recommend, while loyalty alone mediates the relationship between ORBI and intentions to revisit a casual dining restaurant. Practical implications Managers looking to stimulate recommendation intentions can increase ORBI, loyalty or satisfaction among repeat customers; or choose some combination of these three predictors. To improve revisit intentions, managers should first increase loyalty, followed by ORBI. Importantly, management needs to tailor information given to repeat customers differently than other customers. Originality/value This paper provides a first conceptualization of how both loyalty and satisfaction jointly mediate the relationships between ORBI and two behavioral intentions (revisit, recommend). The results show that loyalty plays a significant role in these predictive relationships and is more important than satisfaction for enhancing intentions to revisit a restaurant.

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Nawagitgul, Porntippa, Igor Morozov, Steven R. Bolin, Perry A. Harms, Steven D. Sorden, and Prem S. Paul. "Open reading frame 2 of porcine circovirus type 2 encodes a major capsid protein." Journal of General Virology 81, no. 9 (September 1, 2000): 2281–87. http://dx.doi.org/10.1099/0022-1317-81-9-2281.

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Porcine circovirus 2 (PCV2), a single-stranded DNA virus associated with post-weaning multisystemic wasting syndrome of swine, has two potential open reading frames, ORF1 and ORF2, greater than 600 nucleotides in length. ORF1 is predicted to encode a replication-associated protein (Rep) essential for replication of viral DNA, while ORF2 contains a conserved basic amino acid sequence at the N terminus resembling that of the major structural protein of chicken anaemia virus. Thus far, the structural protein(s) of PCV2 have not been identified. In this study, a viral structural protein of 30 kDa was identified in purified PCV2 particles. ORF2 of PCV2 was cloned into a baculovirus expression vector and the gene product was expressed in insect cells. The expressed ORF2 gene product had a molecular mass of 30 kDa, similar to that detected in purified virus particles. The recombinant ORF2 protein self-assembled to form capsid-like particles when viewed by electron microscopy. Antibodies against the ORF2 protein were detected in samples of sera obtained from pigs as early as 3 weeks after experimental infection with PCV2. These results show that the major structural protein of PCV2 is encoded by ORF2 and has a molecular mass of 30 kDa.

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Surjit, Milan, Shahid Jameel, and Sunil K. Lal. "The ORF2 Protein of Hepatitis E Virus Binds the 5′ Region of Viral RNA." Journal of Virology 78, no. 1 (January 1, 2004): 320–28. http://dx.doi.org/10.1128/jvi.78.1.320-328.2004.

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ABSTRACT Hepatitis E virus (HEV) is a major human pathogen in much of the developing world. It is a plus-strand RNA virus with a 7.2-kb polyadenylated genome consisting of three open reading frames, ORF1, ORF2, and ORF3. Of these, ORF2 encodes the major capsid protein of the virus and ORF3 encodes a small protein of unknown function. Using the yeast three-hybrid system and traditional biochemical techniques, we have studied the RNA binding activities of ORF2 and ORF3, two proteins encoded in the 3′ structural part of the genome. Since the genomic RNA from HEV has been postulated to contain secondary structures at the 5′ and 3′ ends, we used these two terminal regions, besides other regions within the genome, in this study. Experiments were designed to test for interactions between the genomic RNA fusion constructs with ORF2 and ORF3 hybrid proteins in a yeast cellular environment. We show here that the ORF2 protein contains RNA binding activity. The ORF2 protein specifically bound the 5′ end of the HEV genome. Deletion analysis of this protein showed that its RNA binding activity was lost when deletions were made beyond the N-terminal 111 amino acids. Finer mapping of the interacting RNA revealed that a 76-nucleotide (nt) region at the 5′ end of the HEV genome was responsible for binding the ORF2 protein. This 76-nt region included the 51-nt HEV sequence, conserved across alphaviruses. Our results support the requirement of this conserved sequence for interaction with ORF2 and also indicate an increase in the strength of the RNA-protein interaction when an additional 44 bases downstream of this 76-nt region were included. Secondary-structure predictions and the location of the ORF2 binding region within the HEV genome indicate that this interaction may play a role in viral encapsidation.

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Cowley, Jeff A., Lee C. Cadogan, Kirsten M. Spann, Nusra Sittidilokratna, and Peter J. Walker. "The Gene Encoding the Nucleocapsid Protein of Gill-Associated Nidovirus of Penaeus monodon Prawns Is Located Upstream of the Glycoprotein Gene." Journal of Virology 78, no. 16 (August 15, 2004): 8935–41. http://dx.doi.org/10.1128/jvi.78.16.8935-8941.2004.

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ABSTRACT The ORF2 gene of Gill-associated virus (GAV) of Penaeus monodon prawns resides 93 nucleotides downstream of the ORF1a-ORF1b gene and encodes a 144-amino-acid hydrophilic polypeptide (15,998 Da; pI, 9.75) containing 20 basic (14%) and 13 acidic (9%) residues and 19 prolines (13%). Antiserum to a synthetic ORF2 peptide or an Escherichia coli-expressed glutathione S-transferase-ORF2 fusion protein detected a 20-kDa protein in infected lymphoid organ and gill tissues in Western blots. The GAV ORF2 fusion protein antiserum also cross-reacted with the p20 nucleoprotein in virions of the closely related Yellow head virus. By immuno-gold electron microscopy, it was observed that the ORF2 peptide antibody localized to tubular GAV nucleocapsids, often at the ends or at lateral cross sections. As GAV appears to contain only two structural protein genes (ORF2 and ORF3), these data indicate that GAV differs from vertebrate nidoviruses in that the gene encoding the nucleocapsid protein is located upstream of the gene encoding the virion glycoproteins.

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Käkelä, Reijo, Kimmo Tanhuanpää, Saara Laitinen, Pentti Somerharju, and Vesa M. Olkkonen. "Overexpression of OSBP-related protein 2 (ORP2) in CHO cells induces alterations of phospholipid species composition." Biochemistry and Cell Biology 83, no. 5 (October 1, 2005): 677–83. http://dx.doi.org/10.1139/o05-056.

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We have previously shown that overexpression of human OSBP-related protein 2 (ORP2) in Chinese hamster ovary (CHO) cells results in increased efflux and reduced esterification of cholesterol. The ORP2-expressing cells also have a reduced level of triacylglycerols. We investigated the effects of ORP2 expression on the phospholipid (PL) molecular species and the neutral lipid (NL) fatty acid composition of CHO cells cultured in the presence or absence of serum lipoproteins. In the presence of lipoproteins, ORP2/CHO cells display an increase in polyunsaturated PL species, and polyunsaturated fatty acids (PUFA) in the diminished NL pool are reduced. The increase of polyunsaturated PL may represent a compensatory response to alterations in cholesterol metabolism. Upon lipoprotein deprivation, the ORP2/CHO cells display a drop in polyunsaturated and an increase in mono and diunsaturated PL species. Our results suggest that this is due to defective recycling of PUFA from the diminished NL pool to PL. Furthermore, the PL PUFA, which are elevated in ORP2/CHO cells, are most likely subject to more rapid turnover than the NL-associated pool. The results provide evidence for a delicate integration of cholesterol, PL, and NL metabolism and a role of ORP2 as a regulator of the cellular lipidome.Key words: cholesterol metabolism, mass spectrometry, neutral lipid, oxysterol binding protein, phospholipid, polyunsaturated fatty acid.

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Angga, Vicky Verry, and Juwita Anggraini. "Dinamika Menjelang Pendirian Partai Rakyat Demokratik di Masa Orde Baru." ASANKA: Journal of Social Science And Education 1, no. 2 (September 22, 2020): 55–66. http://dx.doi.org/10.21154/asanka.v1i2.2198.

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ABSTRACTThe Orba government in carrying out its power is almost always repertive acts of the people. The Orba government also practiced an all-out democracy in the political practice of the day. The condition is inflicting discontent of young men and activists. In the 1992, the action committee began to appear and continue to evolve in the next years. The alliances of student alliances then flourished the role of the action committee. Student alliances evolved into a sectoral student organization, laborers, farms, and culture. Sectoral organizations make a struggle against Orba into boxes. The gathering of sectoral organizations then formed the Democratic People's Unity together in 1994, the Democratic People's Unity on its journey didn't go well, there was a difference of opinion between members. The Democratic People's Unity experiences split and delivers the idea of the party's establishment of members. The party's establishment through an uneasy process in the organization. The Extraordinary Congressman 1996 decided the Democratic People Party's foundation. Party is expected to make the movement get radical. Party as a symbol of resistance to your formal democracy system applied by Orba. The party can also be used as a media resistance against the Orba Hegemoni.ABSTRAKPemerintah Orba dalam melaksanakan kekuasaanya hampir selalu melakukan tindakan represif terhadap rakyat. Pemerintah Orba juga mempraktikkan demokrasi semu dalam praktik politik masa itu. Kondisi ini menimbulkan ketidakpuasan dari pemuda dan aktivis. Pada 1992, komite aksi mulai muncul dan terus berkembang di tahun-tahun berikutnya. Aliansi-aliansi mahasiswa kemudian berkembang mengantikan peran komite aksi. Aliansi mahasiswa berkembang menjadi organisasi sektoral mahasiswa, buruh, tani, dan kebudayaan. Organisasi sektoral membuat perjuangan melawan Orba menjadi terkotak-kotak. Kumpulan dari berbagai organiasi sektoral kemudian membentuk Persatuan Rakyat Demokratik sebagai wadah bersama pada 1994. Persatuan Rakyat Demokratik dalam perjalanannya tidak berjalan lancar, terjadi perbedaan pendapat antar anggota. Persatuan Rakyat Demokratik mengalami perpecahan dan melahirkan ide pendirian partai dari sebagian anggota. Pendirian partai melalui proses yang tidak mudah di dalam organisasi. Kongres Luar Biasa 1996 memutuskan pendirian Partai Rakyat Demokratik. Berdirinya partai diharapkan membuat pergerakan menjadi semakin radikal. Partai sebagai simbol perlawanan terhadap sistem demokrasi semu yang diterapkan Orba. Partai juga dapat digunakan sebagai media perlawanan terhadap hegemoni Orba.

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Taherkhani, Reza, Fatemeh Farshadpour, Manoochehr Makvandi, Hamid Rajabi Memari, Ali Reza Samarbafzadeh, Nasrin Sharifi, Behrouz Naeimi, Saeed Tajbakhsh, and Samad Akbarzadeh. "Cytokine Profiles and Cell Proliferation Responses to Truncated ORF2 Protein in Iranian Patients Recovered from Hepatitis E Infection." Journal of Tropical Medicine 2015 (2015): 1–7. http://dx.doi.org/10.1155/2015/523560.

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Background.The aim of this study was to evaluatehepatitis E virus(HEV) specific cellular immune responses to truncated ORF2 protein in Iranian patients recovered from HEV infection. Information about HEV-specific immune responses could be useful in finding an effective way for development of HEV vaccine.Methods.A truncated form of HEV ORF2 protein containing amino acids 112-608 was used to stimulate peripheral blood mononuclear cells (PBMCs) separated from HEV-recovered and control groups. Finally, the levels of four cytokines, IFN-γELISPOT, and cell proliferative responses following stimulation with the truncated ORF2 protein were assessed in the both groups.Results.The truncated ORF2 protein was able to induce IFN-γELISPOT and cell proliferation responses and to produce significant amounts of IFN-γand IL-12 cytokines, but low amounts of IL-10 and IL-4 cytokinesin vitro. These responses were significantly higher in the recovered group compared to the control group. These results indicate the antigenic nature of the truncated ORF2 protein and production of T helper type 1 cytokines.Conclusion.The truncated ORF2 protein can effectively induce significant cellular immune responsesand can be introduced as a potential vaccine candidate. However, further studies are required to evaluate this proteinin vivo.

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Vargas, Juan Carlos. "De Orbe Novo." Chicago Review 38, no. 3 (1992): 5. http://dx.doi.org/10.2307/25305603.

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Conybeare, Catherine. "Terrarum Orbi Documentum." Augustinian Studies 30, no. 2 (1999): 59–74. http://dx.doi.org/10.5840/augstudies199930218.

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Clarke, D. B. "Urbi et Orbi." Cultural Politics an International Journal 9, no. 3 (January 1, 2013): 377–80. http://dx.doi.org/10.1215/17432197-2347115.

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