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首页> 外文期刊>Biotechnology Advances: An International Review Journal >Hookworm SCP/TAPS protein structure - a key to understanding host-parasite interactions and developing new interventions.
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Hookworm SCP/TAPS protein structure - a key to understanding host-parasite interactions and developing new interventions.

机译：钩虫SCP / TAPS蛋白结构-了解宿主-寄生虫相互作用和开发新干预措施的关键。

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摘要

SCP/TAPS proteins are a diverse family of molecules in eukaryotes, including parasites. Despite their abundant occurrence in parasite secretomes, very little is known about their functions in parasitic nematodes, including blood-feeding hookworms. Current information indicates that SCP/TAPS proteins (called Ancylostoma-secreted proteins, ASPs) of the canine hookworm, Ancylostoma caninum, represent at least three distinct groups of proteins. This information, combined with comparative modelling, indicates that all known ASPs have an equatorial groove that binds extended structures, such as peptides or glycans. To elucidate structure-function relationships, we explored the three-dimensional crystal structure of an ASP (called Ac-ASP-7), which is highly up-regulated in expression in the transition of A. caninum larvae from a free-living to a parasitic stage. The topology of the N-terminal domain is consistent with pathogenesis-related proteins, and the C-terminal extension that resembles the fold of the Hinge domain. By anomalous diffraction, we identified a new metal binding site in the C-terminal extension of the protein. Ac-ASP-7 is in a monomer-dimer equilibrium, and crystal-packing analysis identified a dimeric structure which might resemble the homo-dimer in solution. The dimer interaction interface includes a novel binding site for divalent metal ions, and is proposed to serve as a binding site for proteins involved in the parasite-host interplay at the molecular level. Understanding this interplay and the integration of structural and functional data could lead to the design of new approaches for the control of parasitic diseases, with biotechnological outcomes.Digital Object Identifier http://dx.doi.org/10.1016/j.biotechadv.2011.11.002
机译：SCP / TAPS蛋白是真核生物（包括寄生虫）中的各种分子家族。尽管它们在寄生虫的分泌组中大量存在，但对其在寄生线虫（包括吸血钩虫）中的功能了解甚少。当前信息表明，犬钩虫的SCP / TAPS蛋白（称为“ Ancylostoma”分泌蛋白，ASP）代表至少三个不同的蛋白组。该信息与比较建模相结合，表明所有已知的ASP均具有与扩展结构（例如肽或聚糖）结合的赤道凹槽。为了阐明结构与功能的关系，我们探索了ASP的三维晶体结构（称为 Ac -ASP-7），该结构在 A过渡过程中的表达高度上调。犬幼虫从自由生活到寄生虫阶段。 N末端结构域的拓扑结构与致病相关蛋白一致，C末端延伸类似于Hinge结构域的折叠。通过异常衍射，我们在蛋白质的C端延伸中发现了一个新的金属结合位点。 Ac -ASP-7处于单体二聚体平衡状态，晶体堆积分析确定了可能类似于溶液中均二聚体的二聚体结构。二聚体相互作用界面包括用于二价金属离子的新结合位点，并且被提议用作在分子水平上参与寄生虫-宿主相互作用的蛋白质的结合位点。了解这种相互作用以及结构和功能数据的整合可能会导致设计出具有生物技术成果的控制寄生虫病的新方法。数字对象标识符http://dx.doi.org/10.1016/j.biotechadv.2011.11 .002

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