Destabilization of target-sensitive immunoliposomes by antigen binding--a rapid assay for virus.

Destabilization of target-sensitive immunoliposomes by antigen binding--a rapid assay for virus.
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通过抗原结合使靶标敏感的免疫脂质体不稳定——病毒的快速检测。

DOI:
10.1016/s0006-291x(86)80585-x
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发表时间:
1986
影响因子:
3.1
通讯作者:
Huang,L
Huang,L
中科院分区:
生物学4区
文献类型:
--
作者:
Ho,RJ;Rouse,BT;Huang,L

文献摘要

被引文献

相似文献

Interactions of antibody stabilized phosphatidylethanolamine (PE) immunoliposomes with Herpes Simplex virus (HSV) and virus infected cells were studied by detecting the immune-dependent lysis of liposomes. Employing PE immunoliposomes bearing anti-HSV glycoprotein D (gD) IgG, immune-specificity of these liposomes were documented by the sole ability of HSV and the HSV-infected L cells to induce immunoliposome lysis. In addition, inhibition of PE immunoliposome lysis by free anti-gD IgG, but not anti-HSV glycoprotein B IgG, indicated the target antigen specificity of these immunoliposomes. Based on these observations, alkaline phosphatase encapsulated PE liposomes were used to directly detect HSV in fluid phase. This immunoliposome assay which does not require washing was shown to be very rapid and sensitive: 35pfu of HSV-1 in 5ul could be detected within 1.5hr.