Destabilization of target-sensitive immunoliposomes by antigen binding--a rapid assay for virus |
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| Authors: | R J Ho B T Rouse L Huang |
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| Institution: | 1. Chemistry of Interfaces, Luleå University of Technology, SE-97187 Luleå, Sweden;2. Kazan State Medical University, 420012 Kazan, Russia;3. Kazan Federal University, 420008 Kazan, Russia;4. Zavoisky Physical-Technical Institute, FRC Kazan Scientific Center, Russian Academy of Sciences, 420029 Kazan, Russia;5. Department of Physics, Warwick University, Coventry CV4 7AL, UK;1. Chemistry of Interfaces, Luleå University of Technology, SE-97187 Luleå, Sweden;2. Kazan State Medical University, 420012 Kazan, Russia;3. Institute of Physics, Kazan Federal University, 420008 Kazan, Russia;4. Department of Physics, Warwick University, Coventry CV47AL, UK;1. Chemistry of Interfaces, Luleå University of Technology, SE-97187 Luleå, Sweden;2. Institute of Physics, Kazan Federal University, 420008 Kazan, Russia;3. Department of Physics, Warwick University, Coventry CV4 7AL, UK |
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| Abstract: | 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 phosphate 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. |
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