Additional file 6: of Comparative proteomic analysis of QTL CTS-12 derived from wild rice (Oryza rufipogon Griff.), in the regulation of cold acclimation and de-acclimation of rice (Oryza sativa L.) in response to severe chilling stress

Hierarchical clustering of three replicates of quantified proteins in chilling- and recovery-treated samples of DC90 and 9311. CSL1, CSL2, and CSL3 represent the 0-h, 60-h chilling-treated, and 60-h recovery-treated samples of 9311, and CTL1, CTL2, and CTL3 represent the 0-h, 60-h chilling-treated, and 60-h recovery-treated samples of DC90, respectively. C-60 h and R-60 h indicate the chilling- and recovery-treated stages, respectively. R1, R2, and R3 represent three replicates. (TIF 2694 kb

Additional file 2: of Comparative proteomic analysis of QTL CTS-12 derived from wild rice (Oryza rufipogon Griff.), in the regulation of cold acclimation and de-acclimation of rice (Oryza sativa L.) in response to severe chilling stress

Chilling-tolerant phenotypes of DC90 and 9311 under hydroponic culture conditions. A, DC90 and 9311 seedlings before chilling treatment; B, DC90 and 9311 seedlings after 5-day chilling and 7-day recovery treatment. Scale bar = 10 cm. (TIF 2700 kb

Additional file 11: of Comparative proteomic analysis of QTL CTS-12 derived from wild rice (Oryza rufipogon Griff.), in the regulation of cold acclimation and de-acclimation of rice (Oryza sativa L.) in response to severe chilling stress

ROS accumulation, the activity of the ROS scavenging related enzymes, and physiological changes in leaf tissues of DC90 and 9311 under chilling stress and recovery conditions. A, DAB staining of DC90 and 9311 leaf samples under recovery condition; B, NBT staining of DC90 and 9311 leaf samples under recovery condition; C, The relative electrolyte leakage in leaf tissues of DC90 and 9311 during chilling stress and recovery conditions; D, The MDA content in leaf tissues of DC90 and 9311 during chilling stress and recovery conditions; E, The APX activity in leaf tissues of DC90 and 9311 during chilling stress and recovery conditions. Scale bar = 4 mm in A, B. Data in C, D, and E are shown as means ± SD (n = 3). Different letters at top of each column indicate a significant difference at P < 0.05 determined by Tukey’s HSD test. (TIF 9074 kb

Additional file 8: of Comparative proteomic analysis of QTL CTS-12 derived from wild rice (Oryza rufipogon Griff.), in the regulation of cold acclimation and de-acclimation of rice (Oryza sativa L.) in response to severe chilling stress

GO enrichment analysis of DEPs identified in chilling stress and recovery treatment stages of DC90 and 9311 by comparison with its untreated control (P < 0.05). (XLSX 20 kb

Additional file 9: of Comparative proteomic analysis of QTL CTS-12 derived from wild rice (Oryza rufipogon Griff.), in the regulation of cold acclimation and de-acclimation of rice (Oryza sativa L.) in response to severe chilling stress

Profile model analysis of all DEPs identified during the whole period of the chilling and recovery treatment of DC90 and 9311. The number at the bottom-left corner represents the number of DEPs assigned to the corresponding model. Colored profiles indicate a statistically significant number of genes assigned to that category. P < 0.05 was set as the significance level with Bonferroni correction. (TIF 6209 kb

Additional file 10: of Comparative proteomic analysis of QTL CTS-12 derived from wild rice (Oryza rufipogon Griff.), in the regulation of cold acclimation and de-acclimation of rice (Oryza sativa L.) in response to severe chilling stress

The DEPs common to 9311 and DC90 in response to chilling stress and recovery treatment by comparison with untreated controls (XLSX 41 kb

Autophagy enhances the replication of Peste des petits ruminants virus and inhibits caspase-dependent apoptosis in vitro

<p>Peste des petits ruminants (PPR) is an acute and highly contagious disease in small ruminants that causes significant economic losses in developing countries. An increasing number of studies have demonstrated that both autophagy and apoptosis are important cellular mechanisms for maintaining homeostasis, and they participate in the host response to pathogens. However, the crosstalk between apoptosis and autophagy in host cells during PPRV infection has not been clarified. In this study, autophagy was induced upon virus infection in caprine endometrial epithelial cells (EECs), as determined by the appearance of double- and single-membrane autophagy-like vesicles, LC3-I/LC3-II conversion, and p62 degradation. We also found that PPRV infection triggered a complete autophagic response, most likely mediated by the non-structural protein C and nucleoprotein N. Moreover, our results suggest that autophagy not only promotes the replication of PPRV in EECs but also provides a potential mechanism for inhibiting PPRV-induced apoptosis. Inhibiting autophagosome formation by wortmannin and knocking down the essential autophagic proteins Beclin-1 and ATG7 induces caspase-dependent apoptosis in EECs in PPRV infection. However, inhibiting autophagosome and lysosome fusion by NH₄Cl and chloroquine did not increase the number of apoptotic cells. Collectively, these data are the first to indicate that PPRV-induced autophagy inhibits caspase-dependent apoptosis and thus contributes to the enhancement of viral replication and maturity in host cells.</p

Fine mapping of <i>wpb1</i>.

A. Preliminary mapping of wpb1. B. Physical map of the wpb1 locus. Two key recombinants delimited the mapping region. C. Putative ORFs in the mapping region.</p