病毒受体拮抗性诱获配体H9的体外活性及其对人趋化因子受体CX_3CR1的作用

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目的:来源于US28受体N末端的诱惑配体多肽H9,以阐明H9的体外活性及其对细胞表面趋化因子受体CX3CR1内化及调变研究,探讨H9对人趋化因子受体CX3CR1的作用及影响。方法:立足US28的广谱趋化因子结合活性,得到趋化因子受体拮抗性多肽H9。采用趋化抑制实验检测多肽对生理性趋化因子引起的细胞迁移活性的影响,流式细胞术方法(FCM)检测细胞内钙离子浓度变化,利用激光共聚焦显微镜和流式细胞仪分别定性、定量检测CX3CR1的内化,以阐明H9的生物活性及其对人源受体CX3CR1的作用及其机制。结果:多肽H9可以阻断受体结合生理性趋化因子形成的趋化作用,本身不引起趋化运动,不影响胞内信号转导和细胞自然活性;200 ng/mL H9在给药后的最初50min钟内能使细胞表面受体CX3CR1内化达到最大值,内化率约为70%,第100分钟,内化到细胞内的CX3CR1逐渐再循环到细胞表面。证明了H9能引起细胞表面受体CX3CR1内化,内化的受体部分再循环到细胞表面。结论:H9是一种趋化因子受体抑制短肽,影响人受体CX3CR1的内化,但内化后受体再循环到细胞表面,对人受体CX3CR1生理功能没有明显影响,可以作为特异性抗病毒多肽。 OBJECTIVE: To elucidate the in vitro activity of H9 and its effect on the internalization and modulation of cell surface chemokine receptor CX3CR1, and to explore the effect of H9 on the chemokine receptor CX3CR1 The role and influence. METHODS: Based on the broad-spectrum chemokine binding activity of US28, the chemokine receptor antagonist polypeptide H9 was obtained. The chemotactic inhibition assay was used to detect the effect of peptides on cell migration induced by physiological chemotactic factor. Flow cytometry (FCM) was used to detect the change of intracellular calcium concentration. The changes of intracellular calcium concentration were analyzed by laser confocal microscopy and flow cytometry, respectively. The internalization of CX3CR1 was quantitated to clarify the biological activity of H9 and its effect on the human receptor CX3CR1 and its mechanism. Results: Polypeptide H9 blocked the chemotactic effect of receptor binding with chemotactic factor, and did not cause chemotaxis per se. It did not affect intracellular signal transduction and cell natural activity. After administration of 200 ng / mL H9 Within the first 50 min, the internalization of CX3CR1, the cell surface receptor, reached its maximum, with an internalization rate of about 70%. The first 100 min, CX3CR1, which had been internalized into the cells, gradually re-circulated to the cell surface. It was demonstrated that H9 causes the internalization of the cell surface receptor CX3CR1 to be partially recirculated to the cell surface. CONCLUSION: H9 is a chemokine receptor inhibiting short peptide that affects the internalization of the human CX3CR1 receptor. However, the internalized receptor is recirculated to the cell surface and has no significant effect on the physiological function of human CX3CR1 receptor and may serve as a specific Sexual antiviral polypeptide.
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