Platyhelminth Venom Allergen-Like (VAL) proteins: revealing structural diversity, class-specific features and biological associations across the phylum.

Platyhelminth Venom Allergen-Like (VAL) proteins: revealing structural diversity, class-specific features and biological associations across the phylum.
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DOI:
10.1017/s0031182012000704
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发表时间:
2012-09
期刊:
影响因子:
2.4
通讯作者:
Hoffmann KF
Hoffmann KF
中科院分区:
医学2区
文献类型:
--
作者:
Chalmers IW;Hoffmann KF

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在扁形动物感染期间,寄生虫会释放多种蛋白质来帮助入侵、开始进食、促进适应并介导宿主免疫反应的调节。这些蛋白质中包括毒液过敏原样 (VAL) 家族,它是较大的精子涂层蛋白/Tpx-1/Ag5/PR-1/Sc7 (SCP/TAPS) 超家族的一部分。为了探索该蛋白家族在扁形动物发育和宿主相互作用过程中的重要性,我们系统地总结了迄今为止所有已发表的 VAL 蛋白家族的蛋白质组学、基因组学和免疫学研究。通过进行新的基因组和转录组学分析,从所有 4 个传统分类纲(吸虫纲、绦虫纲、单殖纲和涡虫纲)物种中鉴定出 200 多种 VAL 蛋白 (228),我们进一步扩展了与扁形动物门 VAL 多样性相关的知识。随后的系统发育和三级结构分析揭示了几个类特异性 VAL 特征,这可能表明该蛋白家族介导的一系列作用。我们对扁形动物 VAL 的全面分析为理解该蛋白质家族的多样性提供了统一的概要,并为启动这些神秘成员的未来功能表征提供了坚实的背景。
During platyhelminth infection, a cocktail of proteins is released by the parasite to aid invasion, initiate feeding, facilitate adaptation and mediate modulation of the host immune response. Included amongst these proteins is the Venom Allergen-Like (VAL) family, part of the larger sperm coating protein/Tpx-1/Ag5/PR-1/Sc7 (SCP/TAPS) superfamily. To explore the significance of this protein family during Platyhelminthes development and host interactions, we systematically summarize all published proteomic, genomic and immunological investigations of the VAL protein family to date. By conducting new genomic and transcriptomic interrogations to identify over 200 VAL proteins (228) from species in all 4 traditional taxonomic classes (Trematoda, Cestoda, Monogenea and Turbellaria), we further expand our knowledge related to platyhelminth VAL diversity across the phylum. Subsequent phylogenetic and tertiary structural analyses reveal several class-specific VAL features, which likely indicate a range of roles mediated by this protein family. Our comprehensive analysis of platyhelminth VALs represents a unifying synopsis for understanding diversity within this protein family and a firm context in which to initiate future functional characterization of these enigmatic members.