A peptide derived from the N-terminal of NS2A for the preparation of ZIKV NS2A recognition polyclonal antibody.

Zika virus non-structural protein NS2A participates in viral replication, organization, and budding, as well as escaping host immunity. NS2A also involved in the induction of microcephaly by ZIKV. However, the above studies were mainly performed through NS2A with a tag due to the lack of available antibodies against NS2A. ZIKV NS2A is a multiplex transmembrane protein, which leads to difficulties in the preparation of its recognition antibodies, thus seriously affecting the study of ZIKV NS2A. In this study, we found that a peptide (GSTDHMDHFSLGVLC) derived from the N-terminal of ZIKV NS2A coupled to KLH induced antibodies recognizing ZIKV NS2A in rabbits. The purified polyclonal antibody recognized ZIKV NS2A in ZIKV-infected cells with high efficiency and specificity, as detected by western blot and immunofluorescence assay. Our study has important implications for the preparation of ZIKV NS2A antibodies and the in-depth study of ZIKV NS2A.

In situ self-assembled N-rich carbon on pristine graphene as a highly effective support and cocatalyst of short Pt nanoparticle chains for superior electrocatalytic activity toward methanol oxidation.

Highly conductive cocatalysts with great promotion effects are critical for the development of pristine graphene supported Pt-based catalysts for the methanol oxidation reaction (MOR) in direct methanol fuel cells (DMFCs). However, identification of these cocatalysts and controlled fabrication of Pt/cocatalyst/graphene hybrids with superior catalytic performance present great challenges. For the first time, pristine graphene supported N-rich carbon (NC) has been controllably fabricated via ionic-liquid-based in situ self-assembly for in situ growth of small and uniformly dispersed Pt NP chains to improve the MOR catalytic activity. It is discovered that the NC serves simultaneously as a linker to facilitate in situ nucleation of Pt, a stabilizer to restrict its growth and aggregation, and a structure-directing agent to induce the formation of Pt NP chains. The obtained nanohybrid shows a much higher forward peak current density than commercial Pt/C and most reported noncovalently functionalized carbon (NFC) supported Pt catalysts, a lower onset potential than almost all commercial Pt/C and NFC supported Pt, and greatly enhanced durability compared to graphene supported Pt NPs and commercial Pt/C. The superior catalytic performance is ascribed to the uniformly dispersed, small-diameter, and short Pt NP chains supported on highly conductive G@NC providing high ECSA and improved CO tolerance and the NC with high content of graphitic N greatly enhancing the intrinsic activity and CO tolerance of Pt and offering numerous binding sites for robustly attaching Pt. This work not only identifies and controllably fabricates a novel cocatalyst to significantly promote the catalytic activity of pristine graphene supported Pt but provides a facile and economical strategy for the controlled synthesis of high-performance integrated catalysts for the MOR in DMFCs.

[Effects of gonadotropin on the expression of growth differentiation factor 9 and 9B in mouse ovary].

OBJECTIVES: To study the effects of gonadotropin on the expression of growth differentiation factor-9 (GDF-9) and -9B (GDF-9B) in mouse ovary. METHODS: We chose follicles of mature mice cultured in vitro and mature BALB/c mice as our animal models. (1) In vivo experiment. Twenty mice were divided into two groups (groups A and B) randomly with ten mice in each group. Each mouse was injected with 10 IU pregnant mare's serum gonadotropin in group A and saline of the same volume was given to the other group. Twenty-four hours later we obtained ovarian tissue and immunohistochemistry and in situ hybridization were performed to detect the expression of GDF-9 and GDF-9B. (2) In vitro experiment. Fifty-eight separated follicles were divided into two groups (groups C and D) randomly and cultured in vitro. Thirty-two follicles in group C were cultured in medium with follicular stimulating hormone (FSH) for 72 hours while 26 were cultured without FSH. Immunohistochemistry was performed to detect the expression of GDF-9 in both groups. RESULTS: We abserved 370 follicles by immunohistochemistry. The weak positive (+ or ++) rate was 22.0% and 46.2% while the strong positive (+++ or ++++) rate was 22.6% and 9.1% in 186 follicles of group A. The weak positive (+ or ++) rate in group B was 42.4% and 42.9% while the strong positive (+++ or ++++) rate was 14.1% and 0.5%. The expression of GDF-9 was higher in group A than that of group B. The weak positive rate, positive rate and strong positive rate in group C was 28.1%, 53.1% and 18.8% while that in group D was 61.5%, 30.8% and 7.7%, respectively. The expression of GDF-9 was higher in group C than that of group D. We observed 362 follicles by in situ hybridization. The weak positive (+ or ++) rate was 31.5% and 46.2% while the strong positive (+++ or ++++) rate was 21.2% and 1.1% in 184 follicles of group A. The weak positive (+ or ++) rate in group B was 39.9% and 41.6% while the strong positive (+++ or ++++) rate was 15.7% and 2.8%. There were no differences in the expression of GDF-9B between groups A and B. CONCLUSION: Gonadotropin increases the expression of GDF-9 in vivo while FSH increases GDF-9 in vitro. Gonadotropin has no effects on the expression of GDF-9B.

Increased expression of stathmin in eutopic endometrium of patients with endometriosis.

BACKGROUND: Stathmin was identified as an endometriosis-related protein by comparative proteomics in our previous study. As a microtubule-destabilizing factor, stathmin was shown to participate in the relay and integration of diverse intracellular signaling pathways involved in cell proliferation, differentiation, and many other cellular activities. To investigate whether stathmin is involved in the pathogenesis of endometriosis, we examined the expression of stathmin in eutopic endometrium of women with or without endometriosis. METHODS: Eutopic endometrium samples were collected from thirty-six patients who were diagnosed as endometriosis and the nineteen age-matched patients who were confirmed to be free of endometriosis surgically and histologically. The expression of stathmin mRNA was detected by real-time PCR, and its protein was detected by Western blotting and immunohistochemistry. RESULTS: Stathmin was overexpressed in eutopic endometrium of women with endometriosis detected by real-time PCR in mRNA levels and by Western blotting in protein levels, without significant difference between proliferative and secretory phase. Immunohistochemistry showed that stathmin protein was localized in both endometrial glandular and stromal cells throughout the menstrual cycle. CONCLUSIONS: Stathmin is overexpressed in endometrium of patients with endometriosis and may play a role in the pathogenesis of endometriosis.