{"title":"卡氏肺囊虫抗原的表达克隆。","authors":"A G Smulian, J R Stringer, M J Linke, P D Walzer","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>We undertook expression cloning of Pneumocystis carinii antigens to overcome the difficulties encountered in purification of these antigens. Using monoclonal antibodies to the P. carinii gp120 antigen and polyclonal rabbit antiserum to rat-derived P. carinii, we have isolated cDNA clones encoding immunoreactive moieties. A cDNA clone encoding the 3' portion of a 45-55 kDa antigen of rat-derived P. carinii, was the most abundant clone isolated. The peptide encoded by this cDNA has a novel sequence with a repeated motif rich in glutamic acid residues. Affinity-purified antibodies to this peptide reacted with the 45-55 kDa band of rat-derived P. carinii. The fusion protein was recognized by serum antibodies from rats with natural exposure to P. carinii. The production of this recombinant protein should allow more detailed studies of the host-parasite relationship of this important opportunistic infection.</p>","PeriodicalId":22758,"journal":{"name":"The Journal of protozoology","volume":"38 6","pages":"8S-10S"},"PeriodicalIF":0.0000,"publicationDate":"1991-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Expression cloning of Pneumocystis carinii antigens.\",\"authors\":\"A G Smulian, J R Stringer, M J Linke, P D Walzer\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>We undertook expression cloning of Pneumocystis carinii antigens to overcome the difficulties encountered in purification of these antigens. Using monoclonal antibodies to the P. carinii gp120 antigen and polyclonal rabbit antiserum to rat-derived P. carinii, we have isolated cDNA clones encoding immunoreactive moieties. A cDNA clone encoding the 3' portion of a 45-55 kDa antigen of rat-derived P. carinii, was the most abundant clone isolated. The peptide encoded by this cDNA has a novel sequence with a repeated motif rich in glutamic acid residues. Affinity-purified antibodies to this peptide reacted with the 45-55 kDa band of rat-derived P. carinii. The fusion protein was recognized by serum antibodies from rats with natural exposure to P. carinii. The production of this recombinant protein should allow more detailed studies of the host-parasite relationship of this important opportunistic infection.</p>\",\"PeriodicalId\":22758,\"journal\":{\"name\":\"The Journal of protozoology\",\"volume\":\"38 6\",\"pages\":\"8S-10S\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1991-11-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"The Journal of protozoology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"The Journal of protozoology","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
摘要
为了克服卡氏肺囊虫抗原纯化过程中遇到的困难，我们进行了卡氏肺囊虫抗原的表达克隆。利用carinii P. gp120抗原单克隆抗体和鼠源carinii P.兔多克隆抗血清，我们分离到了编码免疫反应片段的cDNA克隆。一个cDNA克隆编码大鼠源性卡氏弓形虫抗原的3'部分45-55 kDa，是最丰富的克隆。该cDNA编码的肽具有一个具有丰富谷氨酸残基的重复基序的新序列。该肽的亲和纯化抗体与大鼠源性卡氏疟原虫45-55 kDa带反应。该融合蛋白可被自然暴露于卡氏假单胞菌的大鼠血清抗体识别。这种重组蛋白的生产应该允许更详细地研究这种重要的机会性感染的宿主-寄生虫关系。
Expression cloning of Pneumocystis carinii antigens.
We undertook expression cloning of Pneumocystis carinii antigens to overcome the difficulties encountered in purification of these antigens. Using monoclonal antibodies to the P. carinii gp120 antigen and polyclonal rabbit antiserum to rat-derived P. carinii, we have isolated cDNA clones encoding immunoreactive moieties. A cDNA clone encoding the 3' portion of a 45-55 kDa antigen of rat-derived P. carinii, was the most abundant clone isolated. The peptide encoded by this cDNA has a novel sequence with a repeated motif rich in glutamic acid residues. Affinity-purified antibodies to this peptide reacted with the 45-55 kDa band of rat-derived P. carinii. The fusion protein was recognized by serum antibodies from rats with natural exposure to P. carinii. The production of this recombinant protein should allow more detailed studies of the host-parasite relationship of this important opportunistic infection.
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