An understanding of surface and subsurface water contributions to streamflow is essential for accurate predictions of water supply from mountain watersheds that often serve as water towers for downstream communities. As such, this study used the end‐member mixing analysis technique to investigate source water contributions and hydrologic flow paths of the 264 km2 Boulder Creek Watershed, which drains the Colorado Front Range, USA. Four conservative hydrochemical tracers were used to describe this watershed as a 3 end‐member system, and tracer concentration reconstruction suggested that the application of end‐member mixing analysis was robust. On average from 2009 to 2011, snowmelt and rainwater from the subalpine zone and groundwater sampled from the upper montane zone contributed 54%, 22%, and 24% of the annual streamflow, respectively. These values demonstrate increased rainwater and decreased snow water contributions to streamflow relative to area‐weighted mean values derived from previous work at the headwater scale. Young water (2.3 ± 0.8 months) fractions of streamflow decreased from 18–22% in the alpine catchment to 8–10% in the lower elevation catchments and the watershed outlet with implications for subsurface storage and hydrological connectivity. These results contribute to a process‐based understanding of the seasonal source water composition of a mesoscale watershed that can be used to extrapolate headwater streamflow generation predictions to larger spatial scales.
Classical swine fever virus (CSFV) nonstructural protein NS5A is a multifunctional protein functioning in regulation of viral genome replication, protein translation and assembly by interaction with viral or host proteins. Here, heat shock protein 27 (Hsp27) has been identified as a novel binding partner of NS5A by using His tag "pull down" coupled with shotgun LC-MS/MS, with interaction of both proteins further confirmed by co-immunoprecipitation and laser confocal assays. In PK-15 cells, silencing of Hsp27 expression by siRNA enhanced CSFV replication, and upregulation of Hsp27 inhibited viral proliferation. Additionally, we have shown that overexpression of Hsp27 increased NF-κB signaling induced by TNFα. Blocking NF-κB signaling in PK-15 cells overexpressing Hsp27 by ammonium pyrrolidinedithiocarbamate (PDTC) eliminated the inhibition of CSFV replication by Hsp27. These findings clearly demonstrate that the inhibition of CSFV replication by Hsp27 is mediated via the NF-κB signaling pathway.
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