Adaptive channel selection in IEEE 802.15.4 TSCH networks

Additional files 6: Table S5. Four conjugative transposon gene clusters in the Chryseobacterium indologenes J31 genome

Purification of cellular interaction partner of influenza strains A/Beijing/501/2009(H1N1) NS1.

<p>A, The purified protein complexes were detected by SDS-PAGE. Left panel: the protein complexes purified from A549 cells transfected with pnTAP-NS1 plasmids. Right panel: the protein complexes purified from A549 cells transfected with pnTAP vector. M represents protein marker. The bait protein bands and its cellular interaction proteins identified by mass spectrometry are indicated by an arrow and an asterisk, respectively. B, The purified protein complexes were detected by immunoblotting with antibodies against CBP. Left panel: the protein complexes purified from A549 cells transfected with pnTAP-NS1 plasmids. Right panel: the protein complexes purified from A549 cells transfected with pnTAP vector.</p

Co-localization of NS1 and β-tubulin in the nucleus, and Influenza virus A/Beijing/501/2009(H1N1) NS1 induce apoptosis.

<p>(A), (B), (C), (E), (F), (G). A549 cells were transfected with pCMV5-HA-NS1 and control vector pCMV5, respectively. NS1 was apparent from 24 h post-transfection, mainly in nucleus of A549 cells transfected with pCMV5-HA-NS1 (green color) (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0048340#pone-0048340-g003" target="_blank">Figure 3E</a>). On the other hand, β-tubulin was stained in nucleus and cytoplasm (red color) (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0048340#pone-0048340-g003" target="_blank">Figure 3F</a>).The signals of NS1 and β-tubulin clearly overlapped in nucleus (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0048340#pone-0048340-g003" target="_blank">Figure 3G</a>). (D), (H). The A549 cells transfected with pCMV5-HA-NS1 were stained with Hoechst 33342, and exhibited a stronger blue fluorescence and condensated and fragmented nuclear at 24 h post transfection (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0048340#pone-0048340-g003" target="_blank">Figure 3H</a>).</p

Identification of β-tubulin as a novel NS1-binding protein.

<p>(A) Peptide mass fingerprinting of the 55 kDa protein. The protein was identified as β-tubulin using a program, MASCOT, and the peptides assigned to those of β-tubulin are shown. (B) Confirmation of the 55 kDa protein band in TAP purified protein complexes as β-tubulin. The protein complexes purified from A549 cells transfected with pnTAP-NS1 plasmids and that from pnTAP transfected cells were immunoblotted with the anti-β-tubulin antibody (top panel) or anti-CBP antibody (middle panel). The total cell lysate was also immunoblotted with the anti-CBP antibody (bottom panel). (C) Co-immunoprecipitation analysis of β-tubulin and NS1. The precipitates obtained were immunoblotted with the anti-β-tubulin antibody (top panel) or anti-CBP antibody (middle panel). The total cell lysate was immunoblotted with the anti-CBP antibody (bottom panel). (D) An illustration of the various NS1 truncations used to map the β-tubulin-binding domain in the NS1 protein. NS1 Full (NS1 full-length); NS1 N (NS1 N- terminal domain, that is the RNA binding domain); and NS1 C (NS C-terminal domain, that is the effector domain). (E–F) The N-terminal domain of NS1 interacts with β-tubulin. Left panel: the purified GST-fused NS1 proteins stained by coomassie brilliant blue. Right panel: the purified GST-fused NS1 proteins complexes obtained were detected by immunoblotting with anti-GST antibodies (top panel) or anti-β-tubulin antibodies (bottom panel).</p