Soto M, Requena J M, Quijada L, Angel S O, Gomez L C, Guzman F, Patarroyo M E, Alonso C
Centro de Biología Molecular Severo Ochoa, Universidad Autónoma de Madrid, Cantoblanco, Spain.
Clin Exp Immunol. 1995 May;100(2):246-52. doi: 10.1111/j.1365-2249.1995.tb03661.x.
In this work we show that in the sera from dogs naturally infected with the protozoan parasite Leishmania infantum there are antibodies that react specifically against the parasite acidic ribosomal proteins LiP2a and LiP2b, and that each one of the Leishmania P proteins elicits a specific humoral immune response. Using synthetic peptides, the antigenic epitope of these proteins has been mapped in a single region located adjacent to the C-terminal domain highly conserved among the eukaryotic P proteins. The anti-P antibodies elicited during the Leishmania infection do not recognize the conserved C-terminal domain of the parasite P proteins, in contrast with the findings reported in Chagas' disease or systemic lupus erythematosus. The antigenic epitopes of the LiP2a and LiP2b are almost identical in amino acid sequence. No reactivity against Trypanosoma cruzi and human P proteins was found in sera from L. infantum-infected dogs.
在本研究中，我们发现，在自然感染原生动物寄生虫婴儿利什曼原虫的犬类血清中，存在能与该寄生虫酸性核糖体蛋白LiP2a和LiP2b发生特异性反应的抗体，且利什曼原虫的每种P蛋白都会引发特定的体液免疫反应。利用合成肽，这些蛋白的抗原表位已被定位在一个与真核生物P蛋白中高度保守的C端结构域相邻的单一区域。与恰加斯病或系统性红斑狼疮的报道结果相反，利什曼原虫感染期间产生的抗P抗体不能识别寄生虫P蛋白的保守C端结构域。LiP2a和LiP2b的抗原表位在氨基酸序列上几乎相同。在感染婴儿利什曼原虫的犬类血清中，未发现与克氏锥虫和人类P蛋白的反应性。
