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首页> 外文期刊>Vaccine >Specific erythrocyte binding capacity and biological activity of Plasmodium falciparum-derived rhoptry-associated protein 1 peptides
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Specific erythrocyte binding capacity and biological activity of Plasmodium falciparum-derived rhoptry-associated protein 1 peptides

机译:恶性疟原虫衍生的rhoptry相关蛋白1肽的特异性红细胞结合能力和生物学活性

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摘要

Rhoptry-associated protein 1 (RAP1) is a merozoite antigen within Plasmodium falciparum rhoptries as yet having no specific function described for it. Synthetic peptides spanning the RAP1 sequence were tested in erythrocyte binding assays to identify possible RAP1 functional regions. Five high activity binding peptides (HABPs) were identified; 26201, 26202, 26203 and 26204 spanned residues C-461-K-540 within RAP1 Cys region, whilst 26188 (T-201-Y-220) was located in p67 amino terminal. The results showed that peptide binding was saturable, some HABPs inhibited in vitro merozoite invasion and specifically bound to a 72 kDa protein in red blood cell membrane. HABP possible function in merozoite invasion of erythrocytes is also discussed
机译:Rhoptry相关蛋白1(RAP1)是恶性疟原虫rhoptries中的裂殖子抗原,但尚未对其进行描述。在红细胞结合测定中测试了跨越RAP1序列的合成肽,以鉴定可能的RAP1功能区。鉴定了五种高活性结合肽(HABP)。 26201、26202、26203和26204跨越RAP1 Cys区域内的残基C-461-K-540,而26188(T-201-Y-220)位于p67氨基末端。结果表明,肽结合是可饱和的,一些HABPs抑制了体外裂殖子的入侵,并特异性结合了红细胞膜中的72kDa蛋白。还讨论了HABP在裂殖子入侵红细胞中的可能功能

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