48 research outputs found

    Functions of post-conflict bystander affiliations toward aggressors and victims in bottlenose dolphins

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    Post-conflict affiliations initiated by bystanders (bystander affiliation) toward aggressors or victims have been suggested to represent the function of conflict management in some social living species. However, the function of bystander affiliations toward aggressors and victims has not been examined in marine mammals. In the present study, we investigated the function of bystander affiliations to aggressors and victims in bottlenose dolphins: self-protection, the substitute of reconciliation, social facilitation and tension relief of opponents. These bystander affiliations did not reduce post-conflict attacks by former opponents against group members. Bystander affiliation to aggressors tended to be performed by a bystander who had an affiliative relationship with the aggressor but not with the victim. Bystander affiliation to victims also tended to be initiated by a bystander who had an affiliative relationship with the victim but not the aggressor and was close to former opponents at the end of aggressions. Affiliation among group members who stayed near former opponents during aggressions did not increase after aggressions compared to that under control conditions. Renewed aggressions between former opponents decreased after bystander affiliations in our previous study. Bystanders who showed social closeness to former opponents may initiate bystander affiliation toward their affiliative former opponents because they may feel emotion, such as anxiety and excitement, of former opponents. Bystander affiliation toward aggressors and victims may function as tension relief between former opponents. Bystanders of bottlenose dolphins, who may have a relaxed dominant style, might initiate post-conflict affiliation to affiliative individuals unaffected by the dominance relationships among them, unlike despotic specie

    Inhibition of influenza virus replication in cultured cells by RNA-cleaving DNA enzyme

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    AbstractInfluenza virus replication has been effectively inhibited by antisense phosphothioate oligonucleotides targeting the AUG initiation codon of PB2 mRNA. We designed RNA-cleaving DNA enzymes from 10-23 catalytic motif to target PB2-AUG initiation codon and measured their RNA-cleaving activity in vitro. Although the RNA-cleaving activity was not optimal under physiological conditions, DNA enzymes inhibited viral replication in cultured cells more effectively than antisense phosphothioate oligonucleotides. Our data indicated that DNA enzymes could be useful for the control of viral infection

    The RNA Polymerase PB2 Subunit of Influenza A/HongKong/156/1997 (H5N1) Restrict the Replication of Reassortant Ribonucleoprotein Complexes

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    BACKGROUND: Genetic reassortment plays a critical role in the generation of pandemic strains of influenza virus. The influenza virus RNA polymerase, composed of PB1, PB2 and PA subunits, has been suggested to influence the efficiency of genetic reassortment. However, the role of the RNA polymerase in the genetic reassortment is not well understood. METHODOLOGY/PRINCIPAL FINDINGS: Here, we reconstituted reassortant ribonucleoprotein (RNP) complexes, and demonstrated that the PB2 subunit of A/HongKong/156/1997 (H5N1) [HK PB2] dramatically reduced the synthesis of mRNA, cRNA and vRNA when introduced into the polymerase of other influenza strains of H1N1 or H3N2. The HK PB2 had no significant effect on the assembly of the polymerase trimeric complex, or on promoter binding activity or replication initiation activity in vitro. However, the HK PB2 was found to remarkably impair the accumulation of RNP. This impaired accumulation and activity of RNP was fully restored when four amino acids at position 108, 508, 524 and 627 of the HK PB2 were mutated. CONCLUSIONS/SIGNIFICANCE: Overall, we suggest that the PB2 subunit of influenza polymerase might play an important role for the replication of reassortant ribonucleoprotein complexes

    Cooperation in bottlenose dolphins: bidirectional coordination in a rope-pulling task

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    ハンドウイルカがおたがいに協力しあうことを発見. 京都大学プレスリリース. 2019-10-25.In comparison with terrestrial animals, such as primates, there is limited empirical evidence for cooperative behavior in marine mammals under experimental conditions. In this study, we used a cooperative rope-pulling task to investigate how bottlenose dolphins (Tursiops truncatus) coordinate their behavior with a partner. Dolphins successfully learned and were able to perform the task, even when one subject started after the other. In the no-delay condition (i.e., both subjects sent at the same time), one pair of dolphins showed coordinated behaviors. When pairs were successful in solving the task in the delay condition (i.e., one individual sent later than the other), the initiators (i.e., first individual sent) were likely to wait for the follower to arrive, and the follower was likely to swim faster when the initiator did not wait and started pulling the rope alone. These coordinated behaviors might help resolve the given cooperative task. Our results suggest that bottlenose dolphins learn to coordinate their behaviors via trial and error and recognize the necessity of performing simultaneous actions with a partner to successfully accomplish cooperative tasks. In addition, both partners showed behavioral changes over many trials of no-delay and delay conditions, suggesting that bidirectional coordination occurred in the cooperative task

    Artificial hybrids of influenza A virus RNA polymerase reveal PA subunit modulates its thermal sensitivity.

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    BACKGROUND: Influenza A virus can infect a variety of different hosts and therefore has to adapt to different host temperatures for its efficient viral replication. Influenza virus codes for an RNA polymerase of 3 subunits: PB1, PB2 and PA. It is well known that the PB2 subunit is involved in temperature sensitivity, such as cold adaptation. On the other hand the role of the PA subunit in thermal sensitivity is still poorly understood. METHODOLOGY/PRINCIPAL FINDINGS: To test which polymerase subunit(s) were involved in thermal stress we reconstituted artificial hybrids of influenza RNA polymerase in ribonucleoprotein (RNP) complexes and measured steady-state levels of mRNA, cRNA and vRNA at different temperatures. The PA subunit was involved in modulating RNP activity under thermal stress. Residue 114 of the PA subunit was an important determinant of this activity. CONCLUSIONS/SIGNIFICANCE: These findings suggested that influenza A virus may acquire an RNA polymerase adapted to different body temperatures of the host by reassortment of the RNA polymerase genes

    Quantification of Histidine-Containing Dipeptides in Dolphin Serum Using a Reversed-Phase Ion-Pair High-Performance Liquid Chromatography Method

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    The quantification of histidine-containing dipeptides (anserine, carnosine, and balenine) in serum might be a diagnostic tool to assess the health condition of animals. In this study, an existing reversed-phase ion-pair high-performance liquid chromatography (HPLC)–ultraviolet detection method was improved and validated to quantify serum anserine, carnosine, and balenine levels in the dolphin. The serum was deproteinized with trichloroacetic acid and directly injected into the HPLC system. Chromatographic separation of the three histidine-containing dipeptides was achieved on a TSK–gel ODS-80Ts (4.6 mm × 150 mm, 5 µm) analytical column using a mobile phase of 50 mmol/L potassium dihydrogen phosphate (pH 3.4) containing 6 mmol/L 1-heptanesulfonic acid and acetonitrile (96:4). The standard curve ranged from 0.1 µmol/L to 250 µmol/L. The average accuracy of the intra- and inter-analysis of anserine, carnosine, and balenine was 97–106%. The relative standard deviations of total precision (RSDr) of anserine, carnosine, and balenine in dolphin serum were 5.9%, 4.1%, and 2.6%, respectively. The lower limit of quantification of these compounds was 0.11–0.21 µmol/L. These results indicate that the improved method is reliable and concise for the simultaneous determination of anserine, carnosine, and balenine in dolphin serum, and may be useful for evaluation of health conditions in dolphins. Furthermore, this method can also be applied to other biological samples
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