中文摘要：

目的原核表达旋毛虫相对分子质量（Mr）43000抗原基因（Ts43）并对重组蛋白进行抗原性鉴定。方法将旋毛虫抗原基因Ts43克隆入原核表达载体pET30a（＋），构建重组表达质粒pET30a（＋）-Ts43，经测序分析正确后转化大肠埃希菌BL21，以异丙基-β-D硫代半乳糖苷（IPTG）诱导表达。十二烷基磺酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）和蛋白质印迹分析（Western blotting analysis）鉴定重组蛋白的抗原性。结果SDS-PAGE结果显示表达产物为Mr 41000的重组融合蛋白，IPTG诱导4h时表达量最大，薄层凝胶光密度扫描显示表达的融合蛋白占菌体蛋白总量的14．7％。Western blotting结果显示该重组蛋白可被旋毛虫、乡土旋毛虫及纳氏旋毛虫感染小鼠血清及旋毛虫病患者血清识别，与人芽囊原虫、微小隐孢子虫感染小鼠和正常小鼠血清和正常人血清无交叉反应，但与棘球蚴病、囊尾蚴病、日本血吸虫病、并殖吸虫病及华支睾吸虫病患者血清均有交叉反应。结论旋毛虫Ts43基因的重组蛋白具有较好的抗原性，但与某些寄生虫病患者血清有交叉反应。

英文摘要：

To express the antigen gene Ts43 of Trichinella spiralis and identify the antigenicity of the recombinant protein, the antigen gene Ts43 of T. spiralis was cloned into the prokaryotic expression vector pET30a（＋） and the recombinant pET30a（＋ ）-Ts43 was constructed. The recombinant plasmid was transformed into an E. coli BL21 and induced by IPTG. The antigenicity of the recombinant protein was identified by SDS-PAGE and Western blotting. The results showed the relative molecular weight of the expressed fusion protein was about 41 000 and the expression level peaked at 4 h post-incubation. The portion of the fusion protein accounted for 14. 7% of all the protein by thin-layer gel optical scanning. On Western blotting analysis,the recombinant protein was recognized by sera from mice infected with T. spiralis （T1） , with T. nativa （T2） and T. nelsoni （TT） as well as sera of patients with trichinellosis,but not cross-reacted with sera from mice infected with B. hominis, C. parum, and sera from normal mice and persons. However, the recombinant protein was cross-reacted with sera from patients with echinococcosis, cysticercosis, schistosomiasis, paragonimiasis and clonorchiasis. The recombinant protein of T. spiralis Ts43 antigen gene has the antigenicity, but it shows the cross-reaction with sera from patients with certain other parasitic diseases.