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首页> 外文期刊>Infection and immunity >Molecular Cloning, Biochemical Characterization, and Partial Protective Immunity of the Heme-Binding Glutathione S-Transferases from the Human Hookworm Necator americanus
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Molecular Cloning, Biochemical Characterization, and Partial Protective Immunity of the Heme-Binding Glutathione S-Transferases from the Human Hookworm Necator americanus

机译：美洲人钩虫的血红素结合型谷胱甘肽S-转移酶的分子克隆，生化特性和部分保护性免疫。

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Hookworm glutathione S-transferases (GSTs) are critical for parasite blood feeding and survival and represent potential targets for vaccination. Three cDNAs, each encoding a full-length GST protein from the human hookworm Necator americanus (and designated Na-GST-1, Na-GST-2, and Na-GST-3, respectively) were isolated from cDNA based on their sequence similarity to Ac-GST-1, a GST from the dog hookworm Ancylostoma caninum. The open reading frames of the three N. americanus GSTs each contain 206 amino acids with 51% to 69% sequence identity between each other and Ac-GST-1. Sequence alignment with GSTs from other organisms shows that the three Na-GSTs belong to a nematode-specific nu-class GST family. All three Na-GSTs, when expressed in Pichia pastoris, exhibited low lipid peroxidase and glutathione-conjugating enzymatic activities but high heme-binding capacities, and they may be involved in the detoxification and/or transport of heme. In two separate vaccine trials, recombinant Na-GST-1 formulated with Alhydrogel elicited 32 and 39% reductions in adult hookworm burdens (P < 0.05) following N. americanus larval challenge relative to the results for a group immunized with Alhydrogel alone. In contrast, no protection was observed in vaccine trials with Na-GST-2 or Na-GST-3. On the basis of these and other preclinical data, Na-GST-1 is under possible consideration for further vaccine development.
机译：钩虫谷胱甘肽 S -转移酶（GSTs）对于寄生虫的血液喂养和生存至关重要，并代表了潜在的疫苗接种目标。三个cDNA，每个cDNA编码人钩虫 Necator americanus （并命名为 Na -GST-1， Na -GST）的全长GST蛋白-2和 Na -GST-3）分别基于与狗钩虫的GST Ac -GST-1的序列相似性从cDNA中分离出来。 >犬牙垢。三个 N的开放阅读框。美洲GST分别包含206个氨基酸，与 Ac -GST-1的序列同一性为51％至69％。与来自其他生物的GST的序列比对表明，三个 Na -GST属于线虫特异性nu类GST家族。当在 Pi chia pastoris 中表达时，所有三个 Na -GST均表现出低脂质过氧化物酶和谷胱甘肽结合酶活性，但具有高血红素结合能力，并且它们可能参与血红素的排毒和/或运输。在两项单独的疫苗试验中，用Alhydrogel配制的重组 Na -GST-1引起 N后，成人钩虫负担减少了32％和39％（ P <0.05）。相对于仅用Alhydrogel免疫的组的结果而言，美洲幼虫挑战。相反，在用 Na -GST-2或 Na -GST-3进行的疫苗试验中未观察到保护作用。根据这些和其他临床前数据，可能正在考虑 Na -GST-1进一步开发疫苗。

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