Objective To investigate the role of dynophin and substance P in pruritus with 5/6 subtotal nephrectomy rats (STNx). Methods 5/6 subtotal nephrectomy rots were prepared. After 24 weeks , STNx rats entered in end stage renal disease(ESRD). Sixty male SD rats were divided into 4 groups, STNx+P group(n=15), STNx+dynophin group( n=15), STNx control group(n=15) and sham operation group(n=15). Substance P (SP), dynophin and saline were intradermal injected separately. After injection, scratch reaction of rats in 30 minutes were recorded. And then SP concentration in blood was estimated by ELISA and SP expression in skin was examined by immunohistochemisty. Results SP concentration in blood of STNx rats were (1010.2±103.5)pg/ml, which increased to (2530.0± 236.3) pg/ml in STNx+SP group and decreased to (612.4±72.2)pg/ml in STNx+dynophin group, and it was the lowest in sham opera- tion group (240.2±36.5)pg/ml. SP expression in skin was similar to that of in blood. The scratch times in STNx+SP group were highest (7.3±1.9 times), there was no significant difference between STNx + dynophin group and STNx control group. Conclusion Pruritus in ESRD rats was correlated to the increase of SP in blood and skin. Intradermal injection of dynophin can decrease SP in blood and skin, but can not induce scratch in STNx rats.

Enterovirus 71 (EV71) is a major agent of hand, foot and mouth disease that can cause a severe burden of disease to children. To identify an effective method for the control and prevention of EV71, we studied the effect of exposure to heat and ultraviolet (UV) light upon EV71 inactivation. We found that exposure to 50 degrees C could not inactivate the infectivity of EV71. However, exposure to 60 degrees C and 70 degrees C could inactivate EV71 effectively. EV71 could be inactivated after exposure to UV light at a distance between the sample and a lamp of 30 cm for 30 min or 60 min because viral genomic RNA was destroyed. However, fetal bovine serum (FBS) could attenuate the inactivation proffered by heat and UV light. Attenuation effects of FBS were correlated positively with FBS concentration. Hence, EV71 can be inactivated by exposure to heat and UV light, and our results could provide guidance on prevention of the spread of EV71.
Disinfection ; instrumentation ; methods ; Enterovirus A, Human ; genetics ; physiology ; radiation effects ; Enterovirus Infections ; virology ; Hot Temperature ; Humans ; Ultraviolet Rays ; Virus Inactivation ; radiation effects

Rotavirus is the leading causal agent of severe acute gastroenteritis in children aged <5 years. A specific pharmacologic agent for the treatment of rotavirus-infected children is lacking. In China, only the Luo Tewei oral vaccine (Lanzhou Institute of Biological Products, Shanghai, China), which is produced from Lanzhou lamb rotavirus vaccine (LLR), is available. Studies have hypothesized that the genotype of LLR is G10P[12], To identify the genotype of LLR by reverse transcription-polymerase chain reaction, we showed that the VP7 and VP4 genotypes of LLR were G10 and P[15], respectively, based on sequencing, alignment and phylogenetic analyses. In conclusion, we identified the genotype of rotavirus strain LLR to be G10P[15].
China ; Genotype ; Humans ; Molecular Sequence Data ; Phylogeny ; Rotavirus ; chemistry ; classification ; genetics ; isolation & purification ; Rotavirus Infections ; virology ; Rotavirus Vaccines ; chemistry ; classification ; genetics ; isolation & purification ; Sequence Homology, Amino Acid ; Viral Proteins ; chemistry ; genetics

Objective To investigate the functional and structural character of VP8 * proteins of the RV vaccine strains,VP8 * core proteins were expressed and purified.Methods The LLR RNA was extracted directly from the vaccine oral liquid,followed by RT-PCR.The VP8 * core fragment was obtained by PCR with specific primers.The full length genes of Rotateq and Rotarix VP8 * were synthesized and the VP8 * core fragments were obtained by PCR.The VP8 * core fragments were cloned to the pET30a vector respectively.The recombinant plasmids were transformed to the BL21 competent cells to do the protein expression.Then the proteins were further purified by affinity chromatography and gel filtration.The protein samples were evaluated by SDS-PAGE.Results The VP8 * core proteins were expressed in soluble form and purified and the protein bands showed at about 20 kDa in the SDS-PAGE.Conclusions The VP8 * core-pET30a plasmids were constructed and the VP8 * core proteins of the RV vaccine strains were successfully expressed and purified,which may provide the basis for the characterization of receptor binding specificity of the RV vaccine strain and the evaluation of the vaccine efficacy.

Objective To explore the binding specificity of the P[14] RV detected directly from the stool samples.Methods The P[14] VP8* protein was expressed and purified and then the binding pattern to synthetic oligosaccharides and saliva samples was carried out.Results The P[14] VP8 * protein showed significant binding to A type HBGA while almost no binding was detected to other HBGAs.Conclusions A-HBGA may be the attachment factor for the P[14] rotavirus.Therefore,the research of the interaction between P [14] RV and HBGAs provides the basis for further characterization of binding patterns of other RV genotypes and the RV surveillance.

Objective To express the VP8 * protein of the rotavirus vaccine strain LLR in the E.coli with the pGEX4T-1 vector,which is important for the further research of the VP8 * protein functions.Methods The LLR VP8 * gene was obtained by virus RNA extraction and RT-PCR.Then it was cloned in the expression vectors pGEX4T-1.The recombinant plasmid pGEX4T-1-VP8 * was transformed to the E.coli BL21.Then the VP8 *-GST fusion protein was expressed and purified by the affinity chromatograph.The protein of interest was validated by SDS-PAGE and Western Blot.Results The molecular weight of the VP8 *-GST fusion protein was about 52 000 according to the SDS-PAGE.The bands of both 52 000 and 26 000 were shown in the Western Blot with the antibody against GST.Conclusions The LLR VP8 * gene was obtained and cloned to the pGEX4T-1 vector.Moreover,the solvable VP8 *-GST fusion protein was successfully expressed and purified.