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红细胞结合实验显示,疟原虫 knowlesi 趋化因子结合蛋白与人 Fy 红细胞的结合能力高于 Fy 红细胞。

Erythrocyte-binding assays reveal higher binding of Plasmodium knowlesi Duffy binding protein to human Fy erythrocytes than to Fy erythrocytes.

机构信息

Department of Parasitology, Faculty of Medicine, University of Malaya, Kuala Lumpur, Malaysia.

出版信息

Parasit Vectors. 2018 Sep 26;11(1):527. doi: 10.1186/s13071-018-3118-8.

Abstract

BACKGROUND

The merozoite of the zoonotic Plasmodium knowlesi invades human erythrocytes via the binding of its Duffy binding protein (PkDBPαII) to the Duffy antigen on the eythrocytes. The Duffy antigen has two immunologically distinct forms, Fy and Fy. In this study, the erythrocyte-binding assay was used to quantitatively determine and compare the binding level of PkDBPαII to Fy and Fy human erythrocytes.

RESULTS

In the erythrocyte-binding assay, binding level was determined by scoring the number of rosettes that were formed by erythrocytes surrounding transfected mammalian COS-7 cells which expressed PkDBPαII. The assay result revealed a significant difference in the binding level. The number of rosettes scored for Fy was 1.64-fold higher than that of Fy (155.50 ± 34.32 and 94.75 ± 23.16 rosettes, respectively; t = -2.935, P = 0.026).

CONCLUSIONS

The erythrocyte-binding assay provided a simple approach to quantitatively determine the binding level of PkDBPαII to the erythrocyte Duffy antigen. Using this assay, PkDBPαII was found to display higher binding to Fy erythrocytes than to Fy erythrocytes.

摘要

背景

动物源性疟原虫 knowlesi 的裂殖子通过其 Duffy 结合蛋白(PkDBPαII)与红细胞上的 Duffy 抗原结合来入侵人类红细胞。Duffy 抗原有两种免疫上不同的形式,Fy 和 Fy。在这项研究中,使用红细胞结合测定法来定量确定和比较 PkDBPαII 与 Fy 和 Fy 人类红细胞的结合水平。

结果

在红细胞结合测定法中,通过对围绕表达 PkDBPαII 的转染哺乳动物 COS-7 细胞形成的红细胞玫瑰花环的数量进行评分来确定结合水平。测定结果显示结合水平存在显著差异。Fy 评分的玫瑰花环数量是 Fy 的 1.64 倍(分别为 155.50 ± 34.32 和 94.75 ± 23.16 个玫瑰花环;t = -2.935,P = 0.026)。

结论

红细胞结合测定法为定量确定 PkDBPαII 与红细胞 Duffy 抗原的结合水平提供了一种简单的方法。使用该测定法,发现 PkDBPαII 与 Fy 红细胞的结合水平高于与 Fy 红细胞的结合水平。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4854/6158824/c2bda5a55432/13071_2018_3118_Fig1_HTML.jpg

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