Upconversion fluorescence resonance energy transfer biosensor for sensitive detection of human immunodeficiency virus antibodies in human serum

2014 ◽  
Vol 50 (36) ◽  
pp. 4759-4762 ◽  
Author(s):  
Yan-Mei Wu ◽  
Yao Cen ◽  
Li-Jiao Huang ◽  
Ru-Qin Yu ◽  
Xia Chu
Keyword(s):  
Human Immunodeficiency Virus ◽  
Energy Transfer ◽  
Human Serum ◽  
Fluorescence Resonance Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Selective Determination ◽  
Immunodeficiency Virus ◽  
Hiv Antibodies

An upconversion FRET-based biosensor has been developed for the sensitive and selective determination of HIV antibodies in human serum.

scholarly journals Quantitative Fluorescence Resonance Energy Transfer Microscopy Analysis of the Human Immunodeficiency Virus Type 1 Gag-Gag Interaction: Relative Contributions of the CA and NC Domains and Membrane Binding

2009 ◽  
Vol 83 (14) ◽  
pp. 7322-7336 ◽  
Author(s):  
Ian B. Hogue ◽  
Adam Hoppe ◽  
Akira Ono
Keyword(s):  
Human Immunodeficiency Virus ◽  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Membrane Binding ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Immunodeficiency Virus

ABSTRACT The human immunodeficiency virus type 1 structural polyprotein Pr55Gag is necessary and sufficient for the assembly of virus-like particles on cellular membranes. Previous studies demonstrated the importance of the capsid C-terminal domain (CA-CTD), nucleocapsid (NC), and membrane association in Gag-Gag interactions, but the relationships between these factors remain unclear. In this study, we systematically altered the CA-CTD, NC, and the ability to bind membrane to determine the relative contributions of, and interplay between, these factors. To directly measure Gag-Gag interactions, we utilized chimeric Gag-fluorescent protein fusion constructs and a fluorescence resonance energy transfer (FRET) stoichiometry method. We found that the CA-CTD is essential for Gag-Gag interactions at the plasma membrane, as the disruption of the CA-CTD has severe impacts on FRET. Data from experiments in which wild-type (WT) and CA-CTD mutant Gag molecules are coexpressed support the idea that the CA-CTD dimerization interface consists of two reciprocal interactions. Mutations in NC have less-severe impacts on FRET between normally myristoylated Gag proteins than do CA-CTD mutations. Notably, when nonmyristoylated Gag interacts with WT Gag, NC is essential for FRET despite the presence of the CA-CTD. In contrast, constitutively enhanced membrane binding eliminates the need for NC to produce a WT level of FRET. These results from cell-based experiments suggest a model in which both membrane binding and NC-RNA interactions serve similar scaffolding functions so that one can functionally compensate for a defect in the other.

Fluorescence resonance energy transfer-based ratiometric fluorescent assay for highly sensitive and selective determination of sulfide anions

The Analyst ◽  
2015 ◽  
Vol 140 (19) ◽  
pp. 6711-6719 ◽  
Author(s):  
Meijuan Liang ◽  
Yonglei Chen ◽  
Haijuan Zhang ◽  
Xiaoying Niu ◽  
Laifang Xu ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Ratiometric Fluorescence ◽  
Fluorescent Assay ◽  
Selective Determination ◽  
Highly Sensitive ◽  
Fluorescence Resonance

A novel and effective ratiometric fluorescence strategy was developed for rapidly, sensitively and selectively probing sulfide anions (S2−).

scholarly journals Structural Determination of Lipid-bound ApoA-I Using Fluorescence Resonance Energy Transfer

2000 ◽  
Vol 275 (47) ◽  
pp. 37048-37054 ◽  
Author(s):  
Hui-hua Li ◽  
Douglas S. Lyles ◽  
Michael J. Thomas ◽  
Wei Pan ◽  
Mary G. Sorci-Thomas
Keyword(s):  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Structural Determination ◽  
Fluorescence Resonance

A paper-supported sandwich immunosensor based on upconversion luminescence resonance energy transfer for the visual and quantitative determination of a cancer biomarker in human serum

The Analyst ◽  
2020 ◽  
Vol 145 (12) ◽  
pp. 4181-4187 ◽  
Author(s):  
Mengyuan He ◽  
Ning Shang ◽  
Lin Shen ◽  
Zhihong Liu
Keyword(s):  
Energy Transfer ◽  
Quantitative Determination ◽  
Human Serum ◽  
Upconversion Luminescence ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Cancer Biomarker

A portable and sensitive paper-supported sandwich immunosensor based on UC-FRET was developed for the visual and quantitative determination of CEA.

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