A Multi-Functional Imaging Approach to High-Content Protein Interaction Screening

Functional imaging can provide a level of quantification that is not possible in what might be termed traditional high-content screening. This is due to the fact that the current state-of-the-art high-content screening systems take the approach of scaling-up single cell assays, and are therefore bas...

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Vydáno v:PloS one Ročník 7; číslo 4; s. e33231
Hlavní autoři: Matthews, Daniel R., Fruhwirth, Gilbert O., Weitsman, Gregory, Carlin, Leo M., Ofo, Enyinnaya, Keppler, Melanie, Barber, Paul R., Tullis, Iain D. C., Vojnovic, Borivoj, Ng, Tony, Ameer-Beg, Simon M.
Médium: Journal Article
Jazyk:angličtina
Vydáno: United States Public Library of Science 10.04.2012
Public Library of Science (PLoS)
Témata:
Amino acids
Analytical chemistry
Anisotropy
Assaying
Biology
Biophysics
Biosensing Techniques - instrumentation
Biosensing Techniques - methods
Biosensors
Cancer
Cdc42 protein
Cell Line, Tumor
Chemokines
CXCR4 protein
Data analysis
Detection equipment
Energy transfer
Fluorescence
Fluorescence Polarization - instrumentation
Fluorescence Polarization - methods
Fluorescence resonance energy transfer
Fluorescence Resonance Energy Transfer - instrumentation
Fluorescence Resonance Energy Transfer - methods
Green Fluorescent Proteins - chemistry
Humans
Image processing
Information processing
Instrumentation
Internalization
Lifetime
Luminescent Proteins - chemistry
Medical imaging
Microscopy
Oncology
Photons
Physics
Protein interaction
Protein Interaction Domains and Motifs
Protein-protein interactions
Proteins
Proteins - chemistry
Receptors, CXCR4 - chemistry
Recipes
Red Fluorescent Protein
Scaling
Screening
Sensitivity and Specificity
Small Molecule Libraries - chemistry
Studies
Time correlation functions
United Kingdom > UK
United States > US
ISSN:1932-6203, 1932-6203
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Abstract Functional imaging can provide a level of quantification that is not possible in what might be termed traditional high-content screening. This is due to the fact that the current state-of-the-art high-content screening systems take the approach of scaling-up single cell assays, and are therefore based on essentially pictorial measures as assay indicators. Such phenotypic analyses have become extremely sophisticated, advancing screening enormously, but this approach can still be somewhat subjective. We describe the development, and validation, of a prototype high-content screening platform that combines steady-state fluorescence anisotropy imaging with fluorescence lifetime imaging (FLIM). This functional approach allows objective, quantitative screening of small molecule libraries in protein-protein interaction assays. We discuss the development of the instrumentation, the process by which information on fluorescence resonance energy transfer (FRET) can be extracted from wide-field, acceptor fluorescence anisotropy imaging and cross-checking of this modality using lifetime imaging by time-correlated single-photon counting. Imaging of cells expressing protein constructs where eGFP and mRFP1 are linked with amino-acid chains of various lengths (7, 19 and 32 amino acids) shows the two methodologies to be highly correlated. We validate our approach using a small-scale inhibitor screen of a Cdc42 FRET biosensor probe expressed in epidermoid cancer cells (A431) in a 96 microwell-plate format. We also show that acceptor fluorescence anisotropy can be used to measure variations in hetero-FRET in protein-protein interactions. We demonstrate this using a screen of inhibitors of internalization of the transmembrane receptor, CXCR4. These assays enable us to demonstrate all the capabilities of the instrument, image processing and analytical techniques that have been developed. Direct correlation between acceptor anisotropy and donor FLIM is observed for FRET assays, providing an opportunity to rapidly screen proteins, interacting on the nano-meter scale, using wide-field imaging.
AbstractList Functional imaging can provide a level of quantification that is not possible in what might be termed traditional high-content screening. This is due to the fact that the current state-of-the-art high-content screening systems take the approach of scaling-up single cell assays, and are therefore based on essentially pictorial measures as assay indicators. Such phenotypic analyses have become extremely sophisticated, advancing screening enormously, but this approach can still be somewhat subjective. We describe the development, and validation, of a prototype high-content screening platform that combines steady-state fluorescence anisotropy imaging with fluorescence lifetime imaging (FLIM). This functional approach allows objective, quantitative screening of small molecule libraries in protein-protein interaction assays. We discuss the development of the instrumentation, the process by which information on fluorescence resonance energy transfer (FRET) can be extracted from wide-field, acceptor fluorescence anisotropy imaging and cross-checking of this modality using lifetime imaging by time-correlated single-photon counting. Imaging of cells expressing protein constructs where eGFP and mRFP1 are linked with amino-acid chains of various lengths (7, 19 and 32 amino acids) shows the two methodologies to be highly correlated. We validate our approach using a small-scale inhibitor screen of a Cdc42 FRET biosensor probe expressed in epidermoid cancer cells (A431) in a 96 microwell-plate format. We also show that acceptor fluorescence anisotropy can be used to measure variations in hetero-FRET in protein-protein interactions. We demonstrate this using a screen of inhibitors of internalization of the transmembrane receptor, CXCR4. These assays enable us to demonstrate all the capabilities of the instrument, image processing and analytical techniques that have been developed. Direct correlation between acceptor anisotropy and donor FLIM is observed for FRET assays, providing an opportunity to rapidly screen proteins, interacting on the nano-meter scale, using wide-field imaging.
Functional imaging can provide a level of quantification that is not possible in what might be termed traditional high-content screening. This is due to the fact that the current state-of-the-art high-content screening systems take the approach of scaling-up single cell assays, and are therefore based on essentially pictorial measures as assay indicators. Such phenotypic analyses have become extremely sophisticated, advancing screening enormously, but this approach can still be somewhat subjective. We describe the development, and validation, of a prototype high-content screening platform that combines steady-state fluorescence anisotropy imaging with fluorescence lifetime imaging (FLIM). This functional approach allows objective, quantitative screening of small molecule libraries in protein-protein interaction assays. We discuss the development of the instrumentation, the process by which information on fluorescence resonance energy transfer (FRET) can be extracted from wide-field, acceptor fluorescence anisotropy imaging and cross-checking of this modality using lifetime imaging by time-correlated single-photon counting. Imaging of cells expressing protein constructs where eGFP and mRFP1 are linked with amino-acid chains of various lengths (7, 19 and 32 amino acids) shows the two methodologies to be highly correlated. We validate our approach using a small-scale inhibitor screen of a Cdc42 FRET biosensor probe expressed in epidermoid cancer cells (A431) in a 96 microwell-plate format. We also show that acceptor fluorescence anisotropy can be used to measure variations in hetero-FRET in protein-protein interactions. We demonstrate this using a screen of inhibitors of internalization of the transmembrane receptor, CXCR4. These assays enable us to demonstrate all the capabilities of the instrument, image processing and analytical techniques that have been developed. Direct correlation between acceptor anisotropy and donor FLIM is observed for FRET assays, providing an opportunity to rapidly screen proteins, interacting on the nano-meter scale, using wide-field imaging.Functional imaging can provide a level of quantification that is not possible in what might be termed traditional high-content screening. This is due to the fact that the current state-of-the-art high-content screening systems take the approach of scaling-up single cell assays, and are therefore based on essentially pictorial measures as assay indicators. Such phenotypic analyses have become extremely sophisticated, advancing screening enormously, but this approach can still be somewhat subjective. We describe the development, and validation, of a prototype high-content screening platform that combines steady-state fluorescence anisotropy imaging with fluorescence lifetime imaging (FLIM). This functional approach allows objective, quantitative screening of small molecule libraries in protein-protein interaction assays. We discuss the development of the instrumentation, the process by which information on fluorescence resonance energy transfer (FRET) can be extracted from wide-field, acceptor fluorescence anisotropy imaging and cross-checking of this modality using lifetime imaging by time-correlated single-photon counting. Imaging of cells expressing protein constructs where eGFP and mRFP1 are linked with amino-acid chains of various lengths (7, 19 and 32 amino acids) shows the two methodologies to be highly correlated. We validate our approach using a small-scale inhibitor screen of a Cdc42 FRET biosensor probe expressed in epidermoid cancer cells (A431) in a 96 microwell-plate format. We also show that acceptor fluorescence anisotropy can be used to measure variations in hetero-FRET in protein-protein interactions. We demonstrate this using a screen of inhibitors of internalization of the transmembrane receptor, CXCR4. These assays enable us to demonstrate all the capabilities of the instrument, image processing and analytical techniques that have been developed. Direct correlation between acceptor anisotropy and donor FLIM is observed for FRET assays, providing an opportunity to rapidly screen proteins, interacting on the nano-meter scale, using wide-field imaging.
Audience Academic
Author Weitsman, Gregory
Keppler, Melanie
Carlin, Leo M.
Barber, Paul R.
Ofo, Enyinnaya
Tullis, Iain D. C.
Vojnovic, Borivoj
Matthews, Daniel R.
Ameer-Beg, Simon M.
Ng, Tony
Fruhwirth, Gilbert O.
AuthorAffiliation 2 Gray Institute for Radiation Oncology and Biology, Department of Oncology, University of Oxford, Oxford, United Kingdom
1 Division of Cancer Studies, Randall Division of Cell and Molecular Biophysics, King’s College London, London, United Kingdom
Aligarh Muslim University, India
AuthorAffiliation_xml – name: 1 Division of Cancer Studies, Randall Division of Cell and Molecular Biophysics, King’s College London, London, United Kingdom
– name: 2 Gray Institute for Radiation Oncology and Biology, Department of Oncology, University of Oxford, Oxford, United Kingdom
– name: Aligarh Muslim University, India
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/22506000$$D View this record in MEDLINE/PubMed
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ContentType Journal Article
Copyright COPYRIGHT 2012 Public Library of Science
2012 Matthews et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
Matthews et al. 2012
Copyright_xml – notice: COPYRIGHT 2012 Public Library of Science
– notice: 2012 Matthews et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
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Conceived and designed the experiments: SMA TN DRM. Performed the experiments: DRM GOF GW LMC EO. Analyzed the data: DRM SMA. Contributed reagents/materials/analysis tools: MK PB IT BV. Wrote the paper: DRM SMA.
Current address: Centre for Molecular & Cellular Biology of Inflammation, King’s College London, London, United Kingdom
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SubjectTerms Amino acids
Analytical chemistry
Anisotropy
Assaying
Biology
Biophysics
Biosensing Techniques - instrumentation
Biosensing Techniques - methods
Biosensors
Cancer
Cdc42 protein
Cell Line, Tumor
Chemokines
CXCR4 protein
Data analysis
Detection equipment
Energy transfer
Fluorescence
Fluorescence Polarization - instrumentation
Fluorescence Polarization - methods
Fluorescence resonance energy transfer
Fluorescence Resonance Energy Transfer - instrumentation
Fluorescence Resonance Energy Transfer - methods
Green Fluorescent Proteins - chemistry
Humans
Image processing
Information processing
Instrumentation
Internalization
Lifetime
Luminescent Proteins - chemistry
Medical imaging
Microscopy
Oncology
Photons
Physics
Protein interaction
Protein Interaction Domains and Motifs
Protein-protein interactions
Proteins
Proteins - chemistry
Receptors, CXCR4 - chemistry
Recipes
Red Fluorescent Protein
Scaling
Screening
Sensitivity and Specificity
Small Molecule Libraries - chemistry
Studies
Time correlation functions
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Title A Multi-Functional Imaging Approach to High-Content Protein Interaction Screening
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