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一种引发溶细胞抗体的克氏锥虫膜糖蛋白的纯化

Purification of a Trypanosoma cruzi membrane glycoprotein which elicits lytic antibodies.

作者信息

Norris K A, Harth G, So M

机构信息

Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, California 92037.

出版信息

Infect Immun. 1989 Aug;57(8):2372-7. doi: 10.1128/iai.57.8.2372-2377.1989.

Abstract

Recent studies on the humoral immune response to Trypanosoma cruzi have shown that antibodies which are able to bind living parasites and lyse them in conjunction with complement are associated with host protection. Antibodies which support complement-mediated lysis (CML) of trypomastigotes are elicited as a result of an active infection and not after immunization with killed parasites. In spite of the requirement for immune antibodies, lysis proceeds mainly via the alternative complement pathway. We have purified a 160-kilodalton (kDa) glycoprotein from T. cruzi metacyclic trypomastigotes which appears to be a specific target for lytic antibodies. Rabbit antiserum to the purified 160-kDa protein was prepared, and we have determined that these antibodies will support CML of tissue-culture-derived trypomastigotes. The percentage of killing (65 to 70%) was consistent among three different T. cruzi strains tested. In order to examine the specificity of antibody-dependent CML, antibodies to T. cruzi neuraminidase, an unrelated trypomastigote membrane glycoprotein, were tested in the CML, assays and were not found lytic. Viable trypomastigotes bound anti-160-kDa antibodies uniformly as demonstrated by immunofluorescence, whereas antineuraminidase antibodies were extensively capped. The 160-kDa glycoprotein is specifically produced in infectious trypomastigotes (tissue culture derived and metacyclic) and was not detected in epimastigotes or amastigotes. The identification of the 160-kDa glycoprotein as a specific target for lytic antibodies, as well as its expression only in the infectious stage of the parasite, suggests an important role for this protein in eliciting host immunity.

摘要

最近关于克氏锥虫体液免疫反应的研究表明,能够结合活寄生虫并与补体协同使其溶解的抗体与宿主保护相关。支持锥鞭毛体补体介导溶解(CML)的抗体是由主动感染引发的,而非用灭活寄生虫免疫后产生。尽管需要免疫抗体,但溶解主要通过替代补体途径进行。我们从克氏锥虫循环后期锥鞭毛体中纯化出一种160千道尔顿(kDa)的糖蛋白,它似乎是溶细胞抗体的特异性靶标。制备了针对纯化的160-kDa蛋白的兔抗血清,并且我们已确定这些抗体将支持组织培养来源的锥鞭毛体的CML。在所测试的三种不同克氏锥虫菌株中,杀伤百分比(65%至70%)是一致的。为了检测抗体依赖性CML的特异性,在CML试验中测试了针对克氏锥虫神经氨酸酶(一种不相关的锥鞭毛体膜糖蛋白)的抗体,未发现其具有溶细胞作用。通过免疫荧光证明,活的锥鞭毛体均匀地结合抗160-kDa抗体,而抗神经氨酸酶抗体则广泛形成帽状。160-kDa糖蛋白在感染性锥鞭毛体(组织培养来源和循环后期)中特异性产生,在无鞭毛体或前鞭毛体中未检测到。将160-kDa糖蛋白鉴定为溶细胞抗体的特异性靶标,以及其仅在寄生虫感染阶段的表达,表明该蛋白在引发宿主免疫中起重要作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/28e8/313457/4b051bf4b8c8/iai00068-0120-a.jpg

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