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目的比较大理猪源旋毛虫(Trichinela spiralis)成虫与肌幼虫排泄分泌抗原(Excretory-secretory antigens,ES)的蛋白组分差异,并进一步分析其反应原性,为分离筛选出免疫原性和反应原性强的旋毛虫抗原成分奠定基础。方法分别收集和纯化旋毛虫成虫、肌幼虫虫体,制备ES,采用SDS-PAGE分析成虫和肌幼虫ES蛋白成分,Western blot分析其反应原性。结果经SDS-PAGE分析,旋毛虫成虫ES显示17条蛋白条带,相对分子质量范围在120000～14000之间,其中主带6条,相对分子质量分别为120000、64000、43000、40000、35000、33000;旋毛虫肌幼虫ES显示20条蛋白条带,相对分子质量范围在112000～10000之间,其中主带11条,相对分子质量分别为112000、66000、56000、55000、53000、49000、45000、43000、25000、21000、10000。Westernblot分析表明,旋毛虫成虫ES抗原显示7条反应带,相对分子质量分别为43000、40000、35000、27000、19000、18000、14000,其中相对分子质量43000、40000、27000、18000的条带着色明显;旋毛虫肌幼虫ES抗原显示14条反应带,相对分子质量范围在74000～12000之间,其中相对分子质量53000、49000、45000、43000、35000、27000、18000、12000的条带显色明显。结论旋毛虫成虫和肌幼虫ES抗原蛋白组分均复杂,有共同组分,也有不同组分,旋毛虫ES抗原具有较强的反应原性,是旋毛虫病研究的重要候选抗原。
Objective To compare the protein components of Trichinella spiralis adults with the muscle larval excretory-secretory antigens (ESs) and to further analyze their reactionogenicities. To isolate and screen for the immunogenicity and response Strong Trichinella antigen components laid the foundation. METHODS: Adult and muscle larvae of Trichinella were collected and purified to prepare ES. SDS-PAGE was used to analyze the protein components of adult and muscle larvae, respectively. Results By SDS-PAGE analysis, the adult Trichinella ES display 17 protein bands, the relative molecular mass range between 120000 ~ 14000, of which 6 main bands, the relative molecular mass of 120000,64000,43000,40000,35000, respectively, 33000. ES of Trichinella spiralis larvae showed 20 protein bands with relative molecular mass ranging from 112000 to 10000, of which 11 belonged to the main molecular weight, with relative molecular mass of 112000, 66000, 56000, 55000, 53000, 49000, 45000, 43000, 25000, 21000, 10000. Western blot analysis showed that the ES antigen of adult Trichinella spiralis showed seven reaction bands with relative molecular mass of 43000, 400000, 35000, 27000, 19000, 18000 and 14000, respectively. The bands with relative molecular mass of 43000, The ES antigen of Trichinella spiralis muscle larvae showed 14 reaction bands with relative molecular masses ranging from 74000 to 12000. The bands with relative molecular mass of 53000, 49000, 45000, 43000, 35000, 27000, 18000 and 12000 developed significant color. Conclusion The protein components of ES antigens of adult Trichinella spiralis and Muscle larvae are both complex and have common components and different components. The ES antigen of Trichinella spiralis is highly reactive and is an important antigen candidate for the study of Trichinellosis.