插入外膜蛋白LamB的克氏锥虫表面糖蛋白衍生肽介导大肠杆菌与HeLa细胞的黏附。
Adhesion of Escherichia coli to HeLa cells mediated by Trypanosoma cruzi surface glycoprotein-derived peptides inserted in the outer membrane protein LamB.
作者信息
Pereira C M, Favoreto S, da Silveira J F, Yoshida N, Castilho B A
机构信息
Departamento de Microbiologia, Imunologia e Parasitologia, Escola Paulista de Medicina, Universidade Federal de São Paulo, São Paulo, SP, 04023-062, Brazil.
出版信息
Infect Immun. 1999 Sep;67(9):4908-11. doi: 10.1128/IAI.67.9.4908-4911.1999.
Abstract
Peptides derived from the surface glycoprotein gp82 of Trypanosoma cruzi, previously implicated in the parasite's invasion of host cells, were expressed as fusions to the protein LamB of Escherichia coli in a region known to be exposed on the cell surface. Bacteria expressing these proteins adhered to HeLa cells in a manner that mimics the pattern of parasite invasion of mammalian cells. Purified LamB fusion proteins were shown to bind to HeLa cells and to inhibit infection by T. cruzi, supporting the notion that these gp82-derived peptides can mediate interaction of the parasite with its host.
摘要
克氏锥虫表面糖蛋白gp82衍生的肽段，此前被认为与寄生虫对宿主细胞的入侵有关，这些肽段在已知暴露于细胞表面的区域作为大肠杆菌蛋白LamB的融合蛋白表达。表达这些蛋白的细菌以模仿寄生虫入侵哺乳动物细胞模式的方式黏附于HeLa细胞。纯化的LamB融合蛋白显示可与HeLa细胞结合并抑制克氏锥虫的感染，这支持了这些gp82衍生肽段可介导寄生虫与其宿主相互作用的观点。
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