Monteiro Karina M, Lorenzatto Karina R, de Lima Jeferson C, Dos Santos Guilherme B, Förster Sabine, Paludo Gabriela P, Carvalho Paulo C, Brehm Klaus, Ferreira Henrique B
Laboratório de Genômica Estrutural e Funcional, Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul (UFRGS), Porto Alegre, RS, Brazil; Departamento de Biologia Molecular e Celular, Instituto de Biociências, Centro de Biotecnologia, UFRGS, Porto Alegre, RS, Brazil.
Laboratório de Genômica Estrutural e Funcional, Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul (UFRGS), Porto Alegre, RS, Brazil; Programa de Pós-Graduação em Biologia Celular e Molecular, Centro de Biotecnologia, UFRGS, Porto Alegre, RS, Brazil.
J Proteomics. 2017 Jun 6;162:40-51. doi: 10.1016/j.jprot.2017.04.009. Epub 2017 Apr 22.
The hydatid fluid (HF) that fills Echinococcus multilocularis metacestode vesicles is a complex mixture of proteins from both parasite and host origin. Here, a LC-MS/MS approach was used to compare the HF composition of E. multilocularis H95 and G8065 isolates (EmH95 and EmG8065, respectively), which present differences in terms of growth and fertility. Overall, 446 unique proteins were identified, 392 of which (88%) were from parasite origin and 54 from culture medium. At least 256 of parasite proteins were sample exclusive, and 82 of the 136 shared proteins presented differential abundance between E. multilocularis isolates. The parasite's protein repertoires in EmH95 and EmG8065 HF samples presented qualitative and quantitative differences involving antigens, signaling proteins, proteolytic enzymes, protease inhibitors and chaperones, highlighting intraspecific singularities that could be correlated to biological features of each isolate. The repertoire of medium proteins found in the HF was also differential between isolates, and the relevance of the HF exogenous protein content for the parasite's biology is discussed. The repertoires of identified proteins also provided potential molecular markers for important biological features, such as parasite growth rate and fertility, as well potential protein targets for the development of novel diagnostic and treatment strategies for alveolar echinococcosis.
E. multilocularis metacestode infection of mammal hosts involve complex interactions mediated by excretory/secretory (ES) products. The hydatid fluid (HF) that fills the E. multilocularis metacestode vesicles contains complex repertoires of parasite ES products and host proteins that mediate important molecular interactions determinant for parasite survival and development, and, consequently, to the infection outcome. HF has been also extensively reported as the main source of proteins for the immunodiagnosis of echinococcosis. The performed proteomic analysis provided a comprehensive profiling of the HF protein composition of two E. multilocularis isolates. This allowed us to identify proteins of both parasite and exogenous (medium) origin, many of which present significant differential abundances between parasite isolates and may correlate to their differential biological features, including fertility and growth rate.
填充多房棘球绦虫幼虫囊泡的棘球蚴液（HF）是来自寄生虫和宿主的蛋白质的复杂混合物。在此，采用液相色谱-串联质谱（LC-MS/MS）方法比较了多房棘球绦虫H95和G8065分离株（分别为EmH95和EmG8065）的HF组成，这两种分离株在生长和繁殖力方面存在差异。总体而言，共鉴定出446种独特蛋白质，其中392种（88%）来自寄生虫，54种来自培养基。至少256种寄生虫蛋白质是样本特有的，136种共享蛋白质中的82种在多房棘球绦虫分离株之间呈现出丰度差异。EmH95和EmG8065 HF样本中寄生虫的蛋白质组存在定性和定量差异，涉及抗原、信号蛋白、蛋白水解酶、蛋白酶抑制剂和伴侣蛋白，突出了种内特异性，这些特异性可能与每个分离株的生物学特征相关。HF中发现的培养基蛋白质组在分离株之间也存在差异，并讨论了HF外源蛋白质含量对寄生虫生物学的相关性。鉴定出的蛋白质组还为重要生物学特征提供了潜在的分子标记，如寄生虫生长速率和繁殖力，以及为泡型棘球蚴病新型诊断和治疗策略开发提供了潜在的蛋白质靶点。
多房棘球绦虫幼虫对哺乳动物宿主的感染涉及由排泄/分泌（ES）产物介导的复杂相互作用。填充多房棘球绦虫幼虫囊泡的棘球蚴液（HF）包含寄生虫ES产物和宿主蛋白质的复杂组合，这些蛋白质介导了对寄生虫生存和发育以及感染结果起决定性作用的重要分子相互作用。HF也被广泛报道为棘球蚴病免疫诊断的主要蛋白质来源。所进行的蛋白质组学分析提供了两种多房棘球绦虫分离株HF蛋白质组成的全面概况。这使我们能够鉴定出寄生虫和外源（培养基）来源的蛋白质，其中许多在寄生虫分离株之间呈现出显著的丰度差异，并且可能与其不同的生物学特征相关，包括繁殖力和生长速率。
