Risk surveillance with spatial distribution of Organochlorine Pesticides (OCPs) from sedimentary samples of Chenab River.

A pioneering study employed a holistic geostatistical approach to predict the spatial variability of a non sampled area in the Chenab River, Pakistan, using kriging interpolation for organochlorine pesticide (OCP)-polluted risk zones. The Present research intended to investigate the carcinogenic and non-carcinogenic human health risks, contamination levels, and spatial variation of OCPs in the Chenab River, Pakistan. The residual OCP content in sediment samples (n = 120) ranged from 0.056 to 32.14 ng/g. DDE and α-HCH were prevalent among all the samples analyzed, with mean concentrations of 15.84 ± 8.02 and 12.45 ± 6.72 ng/g, respectively. The order of magnitude of OCPs in sediment samples was DDTs > α-HCH > chlorothalonil > heptachlor > endosulfan > aldrin > dieldrin. The findings of the single (SPI) and Nemerow (Nel) pollution index of α-HCH, heptachlor, and aldrin depicted the Chenab River as a serious pollution risk zone. The outcomes of the Pearson correlation coefficient analysis represent the positive correlation among all OCPs, revealing the common origin. Distribution trends showed substantially higher (p < 0.05) contents of analyzed OCPs along the downstream zone. With regards to USEPA human health hazard assessment model, the estimated non-carcinogenic (ΣHI) and non-carcinogenic (ΣTCR) risk ranged from 1.1 × 10-5 to 1.0 × 10-1, 4.0 × 10-8 to 3.2 × 10-4 respectively. TCR >10-4 illustrated a substantial cancer health risk posed by α-HCH, heptachlor, aldrin, and dieldrin in the downstream zone. We recommend the urgent cessation of the ongoing discharge of OCPs into the Chenab River, which needs to be highlighted owing to the significant cancer risk to public health to ensure the good health and wellbeings.

Recombinant Newcastle Disease virus capsids displaying enterovirus 71 VP1 fragment induce a strong immune response in rabbits.

The complete VP1 protein of EV71 was truncated into six segments and fused to the C-terminal ends of full-length nucleocapsid protein (NPfl) and truncated NP (NPt; lacks 20% amino acid residues from its C-terminal end) of newcastle disease virus (NDV). Western blot analysis using anti-VP1 rabbit serum showed that the N-terminal region of the VP1 protein contains a major antigenic region. The recombinant proteins carrying the truncated VP1 protein, VP1(1-100), were expressed most efficiently in Escherichia coli as determined by Western blot analysis. Electron microscopic analysis of the purified recombinant protein, NPt-VP(1-100) revealed that it predominantly self-assembled into intact ring-like structures whereas NPfl-VP(1-100) recombinant proteins showed disrupted ring-like formations. Rabbits immunized with the purified NPt-VP(1-100) and NPfl-VP(1-100) exhibited a strong immune response against the complete VP1 protein. The antisera of these recombinant proteins also reacted positively with authentic enterovirus 71 and the closely related Coxsackievirus A16 when analyzed by an immunofluorescence assay suggesting their potential as immunological reagents for the detection of anti-enterovirus 71 antibodies in serum samples.