一种胸腺肽的结构和功能被恶性疟原虫肽所模仿

P. Dubois , M. Dardenne , T. Fandeur , O. Mercereau-Puijalon , D. Mattei , B. Müller-Hill , T. Blisnick , L. Pereira da Silva
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引用次数: 10

摘要

许多恶性疟原虫抗原含有重复的氨基酸序列。两种血期抗原Pf11-1和Pf332在我们的实验室中被鉴定为具有高交叉反应性,定义了一个交叉反应抗原家族。在本报告中,我们发现氨基酸序列同源性可能解释了这些交叉反应性,但它们延伸到宿主的多肽,即胸腺蛋白酶-α1 (t -α1)。在鸡和猴中培养的抗合成Pf11-1肽的血清与合成的t - α1发生交叉反应。合成的Pf11-1和Pf332肽具有t - α1的部分生物活性。这些结果讨论了疟疾寄生虫为逃避宿主免疫反应而设计的机制。
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Structure and function of a thymic peptide is mimicked by Plasmodium falciparum peptides

Numerous Plasmodium falciparum antigens contain repetitive amino acid sequences. Two blood stage antigens, Pf11-1 and Pf332, were characterized in our laboratories and present high cross-reactivities, defining a family of cross-reacting antigens. In this report, we show that amino acid sequence homologies might explain these cross-reactivities, but that they extend to polypeptides from the host, namely thymosin-α1 (Tα1). An antiserum raised in chickens and Saimiri monkeys against the synthetic Pf11-1 peptide cross-reacts with synthetic Tα1. Synthetic Pf11-1 and Pf332 peptides share some of the biological activities of Tα1. These results are discussed with respect to the mechanisms devised by malaria parasites for escape from the host immune response.

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