{"title":"[寄生虫抗原胞脂素P与红细胞因子P1的相互作用]。","authors":"T Hrzenjak, D Zlatko, L D Mirjana","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Glycolipid compounds causing agglutination of erythrocytes in vitro and the appearance of the anti-P-antibodies in vivo have been named P antigens. The P denotes blood group factor P, being the antigen belonging to multiple allelomorphs in the P system. Their structure has been shown to be of glycosphingolipid nature differing in number and character from carbohydrate components. It has been established that at infestations by parasites the titre of the anti-P-antibodies increases, and hydatid fluid from the cysts of Echinococcus granulosus, as well as certain tissue extracts of some helminths inhibit agglutination of the P1-erythrocytes by anti-P1--antisera. We have isolated the very polar glycolipid complex from hydatid fluid of the cysts of Echinococcus granulosus and from the tissue homogenates of some parasite helminths. We have named it as cytolipin P, designating by P its parasitic origin. The complex is immunologically active and induces cellular and humoral immune response. Having taken into account the nature of cytolipin P we investigated its biological relation to blood group P-factor. Equine, sheep and human p1-erythrocytes agglutinate the cytolipin P when the concentration of it reaches 75--100 mg%. The inhibition of agglutination was achieved by four sequential doses inducing haemagglutination with anti-P-sera when used as standards, and with human anti-P1-sera of the patients exhibiting echinococcal and ascardial positive human and animal sera. Inhibition was reached two times quicker with anticytolipin-P-sera. It would appear that in the organisms invaded by parasites the cytolipin P represents that antigenic structure which provokes the organism to produce the polyclonal anti-P-antibodies.</p>","PeriodicalId":75595,"journal":{"name":"Bilten za hematologiju i transfuziju","volume":"11 2-3","pages":"33-8"},"PeriodicalIF":0.0000,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"[Interaction of the parasitic antigen cytolipin P with erythrocyte factor P1].\",\"authors\":\"T Hrzenjak, D Zlatko, L D Mirjana\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Glycolipid compounds causing agglutination of erythrocytes in vitro and the appearance of the anti-P-antibodies in vivo have been named P antigens. The P denotes blood group factor P, being the antigen belonging to multiple allelomorphs in the P system. Their structure has been shown to be of glycosphingolipid nature differing in number and character from carbohydrate components. It has been established that at infestations by parasites the titre of the anti-P-antibodies increases, and hydatid fluid from the cysts of Echinococcus granulosus, as well as certain tissue extracts of some helminths inhibit agglutination of the P1-erythrocytes by anti-P1--antisera. We have isolated the very polar glycolipid complex from hydatid fluid of the cysts of Echinococcus granulosus and from the tissue homogenates of some parasite helminths. We have named it as cytolipin P, designating by P its parasitic origin. The complex is immunologically active and induces cellular and humoral immune response. Having taken into account the nature of cytolipin P we investigated its biological relation to blood group P-factor. Equine, sheep and human p1-erythrocytes agglutinate the cytolipin P when the concentration of it reaches 75--100 mg%. The inhibition of agglutination was achieved by four sequential doses inducing haemagglutination with anti-P-sera when used as standards, and with human anti-P1-sera of the patients exhibiting echinococcal and ascardial positive human and animal sera. Inhibition was reached two times quicker with anticytolipin-P-sera. It would appear that in the organisms invaded by parasites the cytolipin P represents that antigenic structure which provokes the organism to produce the polyclonal anti-P-antibodies.</p>\",\"PeriodicalId\":75595,\"journal\":{\"name\":\"Bilten za hematologiju i transfuziju\",\"volume\":\"11 2-3\",\"pages\":\"33-8\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1983-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Bilten za hematologiju i transfuziju\",\"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":"Bilten za hematologiju i transfuziju","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
在体外引起红细胞凝集和体内出现抗P抗体的糖脂化合物被命名为P抗原。P为血型因子P,是P系统中属于多个同形体的抗原。它们的结构已被证明具有糖鞘脂性质,在数量和性质上不同于碳水化合物成分。已经证实,在寄生虫的侵袭下,抗p抗体的滴度增加,颗粒棘球绦虫囊中的包虫液以及某些蠕虫的某些组织提取物可抑制抗p1 -抗血清对p1 -红细胞的凝集。我们从细粒棘球绦虫囊的包虫液和一些寄生虫的组织匀浆中分离出极极性糖脂复合物。我们将其命名为细胞脂素P,以P表示其寄生来源。该复合物具有免疫活性,可诱导细胞和体液免疫反应。考虑到细胞脂素P的性质,我们研究了它与血型P因子的生物学关系。马、羊和人的p1-红细胞在浓度达到75—100mg %时可凝集细胞脂素P。以抗p -血清为对照,以人抗p1 -血清为对照,以棘球蚴和蛔虫阳性的人、动物血清为对照,连续4次诱导血凝,达到抑制凝集的目的。抗细胞脂素- p -血清达到抑制效果快两倍。可见,在被寄生虫入侵的生物体中,胞脂素P代表了一种抗原结构,促使生物体产生多克隆抗P抗体。
[Interaction of the parasitic antigen cytolipin P with erythrocyte factor P1].
Glycolipid compounds causing agglutination of erythrocytes in vitro and the appearance of the anti-P-antibodies in vivo have been named P antigens. The P denotes blood group factor P, being the antigen belonging to multiple allelomorphs in the P system. Their structure has been shown to be of glycosphingolipid nature differing in number and character from carbohydrate components. It has been established that at infestations by parasites the titre of the anti-P-antibodies increases, and hydatid fluid from the cysts of Echinococcus granulosus, as well as certain tissue extracts of some helminths inhibit agglutination of the P1-erythrocytes by anti-P1--antisera. We have isolated the very polar glycolipid complex from hydatid fluid of the cysts of Echinococcus granulosus and from the tissue homogenates of some parasite helminths. We have named it as cytolipin P, designating by P its parasitic origin. The complex is immunologically active and induces cellular and humoral immune response. Having taken into account the nature of cytolipin P we investigated its biological relation to blood group P-factor. Equine, sheep and human p1-erythrocytes agglutinate the cytolipin P when the concentration of it reaches 75--100 mg%. The inhibition of agglutination was achieved by four sequential doses inducing haemagglutination with anti-P-sera when used as standards, and with human anti-P1-sera of the patients exhibiting echinococcal and ascardial positive human and animal sera. Inhibition was reached two times quicker with anticytolipin-P-sera. It would appear that in the organisms invaded by parasites the cytolipin P represents that antigenic structure which provokes the organism to produce the polyclonal anti-P-antibodies.