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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| Veröffentlicht in: | PloS one Jg. 7; H. 4; S. e33231 |
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| Format: | Journal Article |
| Sprache: | Englisch |
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Public Library of Science
10.04.2012
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| 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. |
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| 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 |
| Author_xml | – sequence: 1 givenname: Daniel R. surname: Matthews fullname: Matthews, Daniel R. – sequence: 2 givenname: Gilbert O. surname: Fruhwirth fullname: Fruhwirth, Gilbert O. – sequence: 3 givenname: Gregory surname: Weitsman fullname: Weitsman, Gregory – sequence: 4 givenname: Leo M. surname: Carlin fullname: Carlin, Leo M. – sequence: 5 givenname: Enyinnaya surname: Ofo fullname: Ofo, Enyinnaya – sequence: 6 givenname: Melanie surname: Keppler fullname: Keppler, Melanie – sequence: 7 givenname: Paul R. surname: Barber fullname: Barber, Paul R. – sequence: 8 givenname: Iain D. C. surname: Tullis fullname: Tullis, Iain D. C. – sequence: 9 givenname: Borivoj surname: Vojnovic fullname: Vojnovic, Borivoj – sequence: 10 givenname: Tony surname: Ng fullname: Ng, Tony – sequence: 11 givenname: Simon M. surname: Ameer-Beg fullname: Ameer-Beg, Simon M. |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/22506000$$D View this record in MEDLINE/PubMed |
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| CitedBy_id | crossref_primary_10_1371_journal_pone_0110695 crossref_primary_10_1016_j_bpj_2020_11_2275 crossref_primary_10_1016_j_ab_2015_08_022 crossref_primary_10_1111_jmi_12057 crossref_primary_10_1007_s43630_021_00096_w crossref_primary_10_1002_jbio_201200185 crossref_primary_10_1038_s41467_017_01799_4 crossref_primary_10_1002_cyto_a_22616 crossref_primary_10_1111_febs_12348 crossref_primary_10_1038_s41467_021_22816_7 crossref_primary_10_1038_nrc3724 crossref_primary_10_1038_srep28186 crossref_primary_10_1517_17460441_2015_1075001 crossref_primary_10_1007_s10495_015_1120_6 |
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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 |
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| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 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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