Author
Listed:
- Dan Yu
(University of California
Cardiovascular Research Institute, University of California)
- William Clay Gustafson
(Helen Diller Family Comprehensive Cancer Center, University of California)
- Chun Han
(Cardiovascular Research Institute, University of California
University of California
University of California)
- Céline Lafaye
(Université Grenoble Alpes, Institut de Biologie Structurale (IBS)
CNRS, IBS
CEA, DSV, IBS)
- Marjolaine Noirclerc-Savoye
(Université Grenoble Alpes, Institut de Biologie Structurale (IBS)
CNRS, IBS
CEA, DSV, IBS)
- Woo-Ping Ge
(Cardiovascular Research Institute, University of California
University of California
University of California)
- Desiree A. Thayer
(Cardiovascular Research Institute, University of California
University of California
University of California)
- Hai Huang
(Cardiovascular Research Institute, University of California
University of California)
- Thomas B. Kornberg
(Cardiovascular Research Institute, University of California
University of California)
- Antoine Royant
(Université Grenoble Alpes, Institut de Biologie Structurale (IBS)
CNRS, IBS
CEA, DSV, IBS
European Synchrotron Radiation Facility)
- Lily Yeh Jan
(Cardiovascular Research Institute, University of California
University of California
University of California
Howard Hughes Medical Institute, University of California)
- Yuh Nung Jan
(Cardiovascular Research Institute, University of California
University of California
University of California
Howard Hughes Medical Institute, University of California)
- William A. Weiss
(Helen Diller Family Comprehensive Cancer Center, University of California
Brain Tumor Research Center, University of California)
- Xiaokun Shu
(University of California
Cardiovascular Research Institute, University of California)
Abstract
Infrared fluorescent proteins (IFPs) are ideal for in vivo imaging, and monomeric versions of these proteins can be advantageous as protein tags or for sensor development. In contrast to GFP, which requires only molecular oxygen for chromophore maturation, phytochrome-derived IFPs incorporate biliverdin (BV) as the chromophore. However, BV varies in concentration in different cells and organisms. Here we engineered cells to express the haeme oxygenase responsible for BV biosynthesis and a brighter monomeric IFP mutant (IFP2.0). Together, these tools improve the imaging capabilities of IFP2.0 compared with monomeric IFP1.4 and dimeric iRFP. By targeting IFP2.0 to the plasma membrane, we demonstrate robust labelling of neuronal processes in Drosophila larvae. We also show that this strategy improves the sensitivity when imaging brain tumours in whole mice. Our work shows promise in the application of IFPs for protein labelling and in vivo imaging.
Suggested Citation
Dan Yu & William Clay Gustafson & Chun Han & Céline Lafaye & Marjolaine Noirclerc-Savoye & Woo-Ping Ge & Desiree A. Thayer & Hai Huang & Thomas B. Kornberg & Antoine Royant & Lily Yeh Jan & Yuh Nung J, 2014.
"An improved monomeric infrared fluorescent protein for neuronal and tumour brain imaging,"
Nature Communications, Nature, vol. 5(1), pages 1-7, May.
Handle:
RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms4626
DOI: 10.1038/ncomms4626
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