Clinical effect of hysteroscopic scar defect orthopedic surgery on cicatrical scar of uterine incision / 中国综合临床

Objective To explore the clinical effect of hysteroscopic scar defect correction in the treatment of cesarean scar.Methods Eighty-four cases patients with cesarean section uterine incision scars who were treated in Affiliated Hospital of Hubei Polytechnic University from August 2015 to July 2016 were selected and randomly divided into observation group with hysteroscopic surgery and control group with vaginal surgery,42 cases in each group.The operation condition,clinical efficacy and the incidence of complications of the two groups were observed and compared.Results The amomt of blood loss,hospitalization expenses,hospitalization time and operation time in the observation group were (22.45±3.78) ml,(3028.89±218.79) yuan,(3.89 ±0.80) d,(20.13±2.90) min respectively,in the control group were (40.56±5.48) ml,(4189.58±269.78)yuan,(5.46 ± 1.02) d,(30.78 ± 6.99) min respectively,the differences were significant (P ＞ 0.05).The incidence of infection,relapse and incisional wound healing in the observation group were significantly lower than in the control group,the differences were significant (P＜0.05).The total effective rate was 90.48％ in the observation group and 85.71％ in the control group after treatment,the difference was not significant(P ＞0.05).Conclusion Hysteroscopic scar repair has the same effect as that of vaginal surgery,but the rate of blood loss and complication is lower than that of vaginal operation,which is safer and more effective.

A Novel Polyclonal Antiserum against Toxoplasma gondii Sodium Hydrogen Exchanger 1

The sodium hydrogen exchanger 1 (NHE1), which functions in maintaining the ratio of Na+ and H+ ions, is widely distributed in cell plasma membranes. It plays a prominent role in pH balancing, cell proliferation, differentiation, adhesion, and migration. However, its exact subcellular location and biological functions in Toxoplasma gondii are largely unclear. In this study, we cloned the C-terminal sequence of T. gondii NHE1 (TgNHE1) incorporating the C-terminal peptide of NHE1 (C-NHE1) into the pGEX4T-1 expression plasmid. The peptide sequence was predicted to have good antigenicity based on the information obtained from an immune epitope database. After induction of heterologous gene expression with isopropyl-b-D-thiogalactoside, the recombinant C-NHE1 protein successfully expressed in a soluble form was purified by glutathione sepharose beads as an immunogen for production of a rabbit polyclonal antiserum. The specificity of this antiserum was confirmed by western blotting and immunofluorescence. The antiserum could reduce T. gondii invasion into host cells, indicated by the decreased TgNHE1 expression in T. gondii parasites that were pre-incubated with antiserum in the process of cell entry. Furthermore, the antiserum reduced the virulence of T. gondii parasites to host cells in vitro, possibly by blocking the release of Ca2+. In this regard, this antiserum has potential to be a valuable tool for further studies of TgNHE1.

Preparation and identification of anti-TgAQP peptide antibody / 中国人兽共患病学报

In this study ,we intended to prepare anti‐Toxoplasma gondii aquaporin (TgAQP) peptide antibody which was used to the application in the detection of the aquaporin expression and its subcellular localization of Toxop lasma gondii (T .gondii) ME49 strain .The B cell peptide antigen was designed based on the TgAQP amino acids sequence .After the pep‐tide antigen was conjugated to the KLH ,the fusion antigen was injected into New Zealand rabbits to prepare polyclonal anti‐body ,followed by identification of ELISA ,Western‐blotting and immunofluorescence assays .The ELISA showed that the titer of anti‐TgAQP antibody was about 1∶40 000 .Western blotting revealed the specific affinity of the antigen to polyclonal anti‐body at 29 .9 kDa protein T .gondii .The protein detected by the indirect immunofluorescence assays was distributed in the cy‐toplasm of the parasite .Thus far ,the anti‐TgAQP polyclonal antibody was successfully prepared ,providing a useful tool for further study of biological function and metabolic characteristics of TgAQP .

Preparation and identification of rabbit polyclonal antibodies against vacuolar proton pyrophosphatase type I of Toxoplasma gondii / 南方医科大学学报

<p><b>OBJECTIVE</b>To prepare and characterize rabbit polyclonal antibodies against Toxoplasma gondii vacuolar proton pyrophosphatase type I (TgVP1).</p><p><b>METHODS AND RESULTS</b>Two synthesized peptides TgVP1-1 and TgVP1-2 as the haptens were conjugated with KLH to immunize rabbits. Indirect ELISA showed that the titers of rabbit anti-TgVP1-1 polyclonal antibody and rabbit anti-TgVP1-2 polyclonal antibody reached 1:128 000. Western blotting results revealed that both purified polyclonal antibodies could specifically bind to a purified 85 kD T. gondii protein predicted as TgVP1. The protein detected by these two polyclonal antibodies was distributed in the cytoplasm of T. gondii tachyzoite, and this distribution pattern was consistent with that of acidocalcisome.</p><p><b>CONCLUSION</b>The peptide-based method of antibody generation is efficient and the obtained TgVP1 polyclonal antibodies possess a high specificity to facilitate further study of T. gondii acidocalcisome and the diagnosis of toxoplasmosis.</p>

SEQUENCING AND HOMOLOGOUS ANALYSIS OF THE SEXUAL STAGE PFS25 GENE FROM PLASMODIUM FAL CIPARUM PFD-3/YN ISOLATE / 中国人兽共患病学报

Malaria vaccines are being developed against different stages in the parasite's life cycle. Although not directly protective ,the sexual stage vaccines would induce antibodies that would prevent infection of mosquitoes when ingestedin a bloodmeal containing sexual stage parasites. pfs25 has been tested to be an important candidate antigen for malarial transmission blocking vaccine . In this report we analyzed the complete code of pfs25 gene of Plasmodium falciparum PFD-3/YN isolate. The result shows that the gene encoding pfs25 of PED-3/YN isolate has a mutant which generates a PstI endonuclease restriction site and shares 99.2％ nucleotide homology with that of NF4 isolate.