利什曼原虫冠蛋白和Arp2/3复合体序列结构比对后鞭毛蛋白预测。

M. P. Costa, H. Ribeiro, A. Pacheco, D. Pinheiro, M. Kamimura, R. Araujo-Filho, D. M. de Oliveira
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引用次数: 1

摘要

利什曼原虫是一种单鞭毛原虫,其鞭毛在运动中起着关键作用,是寄生虫迁移、入侵和在宿主组织上停留所必需的。肌动蛋白是主要的细胞骨架蛋白,而在运动和进入宿主细胞过程中,寄生虫肌动蛋白和肌动蛋白运动相关蛋白的聚合和解聚可能是成功感染的关键事件。为了寻找参与利什曼原虫鞭毛活性的肌动蛋白相互作用蛋白(AIPs)的基因组和/或蛋白质组学证据,我们应用计算工具(隐马尔可夫模型、Viterbi算法和比较建模)对利什曼原虫的AIPs(如冠状蛋白和Arp2/3复合体蛋白)进行了详细的序列-结构-功能分析,推断其生物学意义。冠状蛋白和Arp2/3复合体蛋白是巨噬细胞吞噬寄生虫后吞噬体形成的两个重要元素。本文的研究结果首次提供了利什曼冠状蛋白和Arp2/3基因及其基因产物的综合生物信息学分析,对这些重要的肌动蛋白调节蛋白的基因组标注做出了直接贡献,这些蛋白尚未在鞭毛虫锥虫中进行适当的体外鉴定,以确定其推测的毒力。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Flagellar proteins prediction after sequence-structure alignments of coronin and Arp2/3 complex in Leishmania spp.
Leishmania are uniflagellate protozoa, whose flagellum plays a key role in motility, being essential for parasite migration, invasion and persistence on host tissues. Actin is the major cytoskeleton protein, while polymerization and depolymerization of parasite actin and actin motor-associated proteins during both processes of motility and host cell entry might be key events for successful infection. In search for genomic and/or proteomic evidences of actin-interacting proteins (AIPs) involved in flagellar activities of Leishmania spp., we have applied computational tools (hidden Markov models, Viterbi algorithm and comparative modeling) to infer biological meaning through detailed sequence-structural-functional analyses on Leishmania AIPs, such as coronin and Arp2/3 complex proteins, two important elements on phagosome formation after parasite phagocytosis by macrophages. Results presented here provide the first integrated bioinformatics analyses of Leishmania coronin and Arp2/3 genes and their gene products, a direct contribution to genome annotation of these important actin-regulating proteins yet to be properly in vitro characterized in flagellate trypanosomatids towards their putative virulence.
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