High abundance ratio of 13^{13}CO to C18^{18}O toward photon-dominated regions in the Orion-A giant molecular cloud

Aims. We derive physical properties such as the optical depths and the column densities of $^{13}$CO and C$^{18}$O to investigate the relationship between the far ultraviolet (FUV) radiation and the abundance ratios between $^{13}$CO and C$^{18}$O. Method. We have carried out wide-field (0.4 deg$^2$) observations with an angular resolution of 25.8 arcsec ($\sim$ 0.05 pc) in $^{13}$CO ($J$=1--0) and C$^{18}$O ($J$=1--0) toward the Orion-A giant molecular cloud using the Nobeyama 45 m telescope in the on-the-fly mode. Results. Overall distributions and velocity structures of the $^{13}$CO and C$^{18}$O emissions are similar to those of the $^{12}$CO ($J$=1--0) emission. The optical depths of the $^{13}$CO and C18O emission lines are estimated to be 0.05 $<$ $\tau_{\rm ^{13}CO}$ $<$ 1.54 and 0.01 $<$ $\tau_{\rm C^{18}O}$ $<$ 0.18, respectively. The column densities of the $^{13}$CO and C$^{18}$O emission lines are estimated to be 0.2 $\times$ 10$^{16}$ $<$ $N_{\rm ^{13}CO}$ $<$ 3.7 $\times$ 10$^{17}$ cm$^{-2}$ and 0.4 $\times$ 10$^{15}$ $<$ $N_{\rm C^{18}O}$ $<$ 3.5 $\times$ 10$^{16}$ cm$^{-2}$, respectively. The abundance ratios between $^{13}$CO and C$^{18}$O, $X_{\rm ^{13}CO}$/$X_{\rm C^{18}O}$, are found to be 5.7 - 33.0. The mean value of $X_{\rm ^{13}CO}$/$X_{\rm C^{18}O}$ in the nearly edge-on photon-dominated regions is found to be 16.47 $\pm$ 0.10, which is a third larger than that the solar system value of 5.5. The mean value of $X_{\rm ^{13}CO}$/$X_{\rm C^{18}O}$ in the other regions is found to be 12.29 $\pm$ 0.02. The difference of the abundance ratio is most likely due to the selective FUV photodissociation of C$^{18}$O.Comment: 11 pages, 9 figures, Accepted to A&

Evidence For Cloud-Cloud Collision and Parsec-Scale Stellar Feedback Within the L1641-N Region

We present high spatial resolution $^{12}$CO ($J=1-0$) images taken by the Nobeyama 45m telescope toward a $48' \times 48'$ area including the L1641-N cluster. The effective spatial resolution of the maps is $21"$, corresponding to 0.04 pc at a distance of 400 pc. A recent 1.1 mm dust continuum map reveals that the dense gas is concentrated in several thin filaments. We find that a few dust filaments are located at the parts where $^{12}$CO ($J=1-0$) emission drops sharply. Furthermore, the filaments have two-components with different velocities. The velocity difference between the two-components is about 3 km s$^{-1}$, corresponding to a Mach number of 10, significantly larger than the local turbulent velocity in the cloud. These facts imply that the collision of the two components (hereafter, the cloud-cloud collision) possibly contributed to the formation of these filaments. Since the two components appear to overlap toward the filaments on the plane of the sky, the collision may have occurred almost along the line of sight. Star formation in the L1641-N cluster was probably triggered by such a collision. We also find several parsec-scale CO shells whose centers are close to either the L1641-N cluster or V 380 Ori cluster. We propose that these shells were created by multiple winds and/or outflows from cluster YSOs, i.e., "protocluster winds." One exceptional dust filament located at the western cloud edge lies along a shell; it is presumably a part of the expanding shell. Both the cloud-cloud collision and protocluster winds are likely to influence the cloud structure and kinematics in this region.Comment: 44 pages, 12 figures, submitted to Ap

Apical Transport of Influenza A Virus Ribonucleoprotein Requires Rab11-positive Recycling Endosome

Influenza A virus RNA genome exists as eight-segmented ribonucleoprotein complexes containing viral RNA polymerase and nucleoprotein (vRNPs). Packaging of vRNPs and virus budding take place at the apical plasma membrane (APM). However, little is known about the molecular mechanisms of apical transport of newly synthesized vRNP. Transfection of fluorescent-labeled antibody and subsequent live cell imaging revealed that punctate vRNP signals moved along microtubules rapidly but intermittently in both directions, suggestive of vesicle trafficking. Using a series of Rab family protein, we demonstrated that progeny vRNP localized to recycling endosome (RE) in an active/GTP-bound Rab11-dependent manner. The vRNP interacted with Rab11 through viral RNA polymerase. The localization of vRNP to RE and subsequent accumulation to the APM were impaired by overexpression of Rab binding domains (RBD) of Rab11 family interacting proteins (Rab11-FIPs). Similarly, no APM accumulation was observed by overexpression of class II Rab11-FIP mutants lacking RBD. These results suggest that the progeny vRNP makes use of Rab11-dependent RE machinery for APM trafficking

Involvement of Hsp90 in Assembly and Nuclear Import of Influenza Virus RNA Polymerase Subunits

Transcription and replication of the influenza virus RNA genome occur in the nuclei of infected cells through the viral RNA-dependent RNA polymerase consisting of PB1, PB2, and PA. We previously identified a host factor designated RAF-1 (RNA polymerase activating factor 1) that stimulates viral RNA synthesis. RAF-1 is found to be identical to Hsp90. Here, we examined the intracellular localization of Hsp90 and viral RNA polymerase subunits and their molecular interaction. Hsp90 was found to interact with PB2 and PB1, and it was relocalized to the nucleus upon viral infection. We found that the nuclear transport of Hsp90 occurs in cells expressing PB2 alone. The nuclear transport of Hsp90 was in parallel with that of the viral RNA polymerase binary complexes, either PB1 and PB2 or PB1 and PA, as well as with that of PB2 alone. Hsp90 also interacted with the binary RNA polymerase complex PB1-PB2, and it was dissociated from the PB1-PB2 complex upon its association with PA. Furthermore, Hsp90 could form a stable PB1-PB2-Hsp90 complex prior to the formation of a ternary polymerase complex by the assembly of PA in the infected cells. These results suggest that Hsp90 is involved in the assembly and nuclear transport of viral RNA polymerase subunits, possibly as a molecular chaperone for the polymerase subunits prior to the formation of a mature ternary polymerase complex

Influenza A Virus Hemagglutinin is Required for the Assembly of Viral Components Including Bundled vRNPs at the Lipid Raft

The influenza glycoproteins, hemagglutinin (HA) and neuraminidase (NA), which are associated with the lipid raft, have the potential to initiate virion budding. However, the role of these viral proteins in infectious virion assembly is still unclear. In addition, it is not known how the viral ribonucleoprotein complex (vRNP) is tethered to the budding site. Here, we show that HA is necessary for the efficient progeny virion production and vRNP packaging in the virion. We also found that the level of HA does not affect the bundling of the eight vRNP segments, despite reduced virion production. Detergent solubilization and a subsequent membrane flotation analysis indicated that the accumulation of nucleoprotein, viral polymerases, NA, and matrix protein 1 (M1) in the lipid raft fraction was delayed without HA. Based on our results, we inferred that HA plays a role in the accumulation of viral components, including bundled vRNPs, at the lipid raft