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Biofluorescence

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Fluorescence is the emission of light by a molecule or an atom that has absorbed light or other electromagnetic radiation. In most cases, the emitted light has a longer wavelength, and therefore a lower photon energy, than the absorbed radiation. A perceptible example of fluorescence occurs when the absorbed radiation is in the ultraviolet region of the electromagnetic spectrum (invisible to the human eye), while the emitted light is in the visible region; this gives the fluorescent substance a distinct color that can only be seen when the substance has been exposed to UV light.

Biofluorescence is fluorescence emitted by a living organism. Biofluorescence requires an external light source and a biomolecular substance that converts absorbed light into a new one. The fluorescent substance absorbs light at one wavelength, often blue or UV, and emits at another, longer wavelength, green, red, or anything in between. In a living organism, the fluorescent agent often is a protein (or several), but it could be other biomolecules as well.

Since biofluorescence was discovered in Aequorea victoria and the green fluorescent protein structure was resolved, many other organisms have been shown to exhibit biofluorescence and many new fluorescent proteins have been discovered.[1][2][3]

Taxonomic range

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Plants

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Biofluorescence is frequent in plants, and can occur in many of their parts.[4] The biofluorescence in chlorophyll but has been studied since the 1800s.[5] Generally, chlorophyll fluoresces red,[6] and can be used as a measure of photosynthetic capabilities,[7][6] or general health.[5] After absorbing light, chlorophyll may fluoresce as part of the physiological processes involved in photosynthesis.[6]

Reproductive organs such as pollen,[8][9] anthers [9] or petals[10] may also fluoresce. These characters may produce a variety of colors depending on the pigment responsible for fluorescence.[10][8][5][9] While it is unclear what the primary function of different kinds of fluorescence are in plants,[4] reproductive characters may biofluoresce as a signal to attract pollinators,[11][9] However, biofluorescence may also attract prey in predatory plants,[12] or serve no function.[5]

Animals

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While biofluorescence was first discovered and extensively characterized in invertebrates, recent work has observed biofluorescence in many vertebrates, with discoveries of biofluorescence have been made in salamanders and frogs,[13][14][15] fish,[16][17][18] birds,[19][20][21] and mammals.[22][23][21]

Functions

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The function of biofluorescence in each case is not completely known. The fluorescent signal may play a role in inter- and intraspecific communication, such as camouflage (e.g. corals[24]), attracting mates (e.g. birds[25] and copepods[26]) and symbionts (e.g. corals[3]), or deterring predators.[26]

Other explanations are physiological, with bright color being a side-product of a defense from UV (e.g. the protein sandercyanin,[17] and UV protection of genes in pollen[9]). Bright red fluorescence in the larvae of Acropora millepora coral correlates with the activation of a diapause-like state that may aid in conserving energy and tolerating heat and other stressors during a long dispersal to novel habitats.[27]

Evolution

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Most likely biofluorescence arose multiple times by convergent evolution.[3][28] Reconstruction experiments suggest the original fluorescent protein was green, and had a simple beta-barrel shape with a chromophore hidden inside. Different colors of green fluorescent proteins (GFP), yellow, red, cyan, and amber, are determined by variations in chromophore structure. Red fluorescent proteins chromophore are the most complex and require extra maturation steps. New fluorescent proteins evolved through gene duplication and accumulation of multiple mutations which gradually changed autocatalytic functions and final chromophore structure.[28]

GFP analogs are common, but this is not the only possible structural solution for biofluorescence. In freshwater Japanese eels Anguilla japonica the unique protein UnaG fluoresces by binding bilirubin, a mechanism very distinct from that of green fluorescent protein.[16] UnaG absorbs blue light and emits green only when the complex with bilirubin is formed. This feature makes UnaG attractive for biomedical assays in exploration of bilirubin-dependent cellular processes.[29]

Another non-GFP- like fluorescent protein is a blue protein, sandercyanin, from freshwater fish walleye, Sander vitreus, in the North hemisphere. Sandercyanin is seasonally produced, with production peaking in the late summer, and is thought to be a defense against high UV. Sandercyanin binds biliverdin IXa, and together they form a tetra-homomer which absorbs UV light at 375nm and emits red light at 675nm.[17]

Two species of catsharks, Cephaloscyllium ventriosum, endemic to the eastern Pacific, and Scyliorhinus retifer, from the western Atlantic, fluoresce by a different mechanism.[18] The fluorescence is produced by brominated tryptophan-kynurenine metabolites, small aromatic compounds present in the lighter-colored regions of skin on the fish. Dermal features of the shark skin optically enhance the fluorescent signal.[18]

See also

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References

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  1. ^ Labas, Y. A.; Gurskaya, N. G.; Yanushevich, Y. G.; Fradkov, A. F.; Lukyanov, K. A.; Lukyanov, S. A.; Matz, M. V. (2002-04-02). "Diversity and evolution of the green fluorescent protein family". Proceedings of the National Academy of Sciences. 99 (7): 4256–4261. Bibcode:2002PNAS...99.4256L. doi:10.1073/pnas.062552299. ISSN 0027-8424. PMC 123635. PMID 11929996.
  2. ^ Alieva, Naila O.; Konzen, Karen A.; Field, Steven F.; Meleshkevitch, Ella A.; Hunt, Marguerite E.; Beltran-Ramirez, Victor; et al. (2008-07-16). El-Shemy, Hany A. (ed.). "Diversity and Evolution of Coral Fluorescent Proteins". PLOS ONE. 3 (7): e2680. Bibcode:2008PLoSO...3.2680A. doi:10.1371/journal.pone.0002680. ISSN 1932-6203. PMC 2481297. PMID 18648549.
  3. ^ a b c Chudakov, Dmitriy M.; Matz, Mikhail V.; Lukyanov, Sergey; Lukyanov, Konstantin A. (July 2010). "Fluorescent Proteins and Their Applications in Imaging Living Cells and Tissues". Physiological Reviews. 90 (3): 1103–1163. doi:10.1152/physrev.00038.2009. ISSN 0031-9333. PMID 20664080.
  4. ^ a b Holovachov, Oleksandr (2015-09-02). "Unseen beauty of flowers – hidden signals or spectacular by-product?". Green Letters. 19 (3): 329–331. doi:10.1080/14688417.2015.1078121. ISSN 1468-8417.
  5. ^ a b c d Lagorio, M. Gabriela; Cordon, Gabriela B.; Iriel, Analia (September 2015). "Reviewing the relevance of fluorescence in biological systems". Photochemical & Photobiological Sciences. 14 (9): 1538–1559. doi:10.1039/c5pp00122f. hdl:11336/8072. ISSN 1474-905X.
  6. ^ a b c Murchie, E.H.; Lawson, T. (October 2013). "Chlorophyll fluorescence analysis: a guide to good practice and understanding some new applications". Journal of Experimental Botany. 64 (13): 3983–3998. doi:10.1093/jxb/ert208. ISSN 1460-2431. PMID 23913954.
  7. ^ Krause, G. Heinrich; Weis, Engelbert (1984). "Chlorophyll fluorescence as a tool in plant physiology: II. Interpretation of fluorescence signals". Photosynthesis Research. 5 (2): 139–157. doi:10.1007/BF00028527. ISSN 0166-8595. PMID 24458602.
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  11. ^ Gumbert, A. (2000-06-01). "Color choices by bumble bees (Bombus terrestris): innate preferences and generalization after learning". Behavioral Ecology and Sociobiology. 48 (1): 36–43. doi:10.1007/s002650000213. ISSN 1432-0762.
  12. ^ Kurup, R.; Johnson, A. J.; Sankar, S.; Hussain, A. A.; Kumar, C. Sathish; Sabulal, B. (May 2013). Rennenberg, H. (ed.). "Fluorescent prey traps in carnivorous plants". Plant Biology. 15 (3): 611–615. Bibcode:2013PlBio..15..611K. doi:10.1111/j.1438-8677.2012.00709.x. ISSN 1435-8603. PMID 23696970.
  13. ^ Lamb, Jennifer Y.; Davis, Matthew P. (2020-02-27). "Salamanders and other amphibians are aglow with biofluorescence". Scientific Reports. 10 (1): 2821. Bibcode:2020NatSR..10.2821L. doi:10.1038/s41598-020-59528-9. ISSN 2045-2322. PMC 7046780. PMID 32108141.
  14. ^ Santa-Cruz, Roy; von May, Rudolf; Catenazzi, Alessandro; Whitcher, Courtney; López Tejeda, Evaristo; Rabosky, Daniel (2019-08-26). "A New Species of Terrestrial-Breeding Frog (Amphibia, Strabomantidae, Noblella) from the Upper Madre De Dios Watershed, Amazonian Andes and Lowlands of Southern Peru". Diversity. 11 (9): 145. doi:10.3390/d11090145. ISSN 1424-2818.
  15. ^ Whitcher, Courtney; Beaver, Lilyanne; Lemmon, Emily Moriarty (February 2024). "The effect of biofluorescence on predation upon Cope's gray treefrog: A clay model experiment". Behavioural Processes. 215: 104996. doi:10.1016/j.beproc.2024.104996.
  16. ^ a b Kumagai, Akiko; Ando, Ryoko; Miyatake, Hideyuki; Greimel, Peter; Kobayashi, Toshihide; Hirabayashi, Yoshio; et al. (June 2013). "A Bilirubin-Inducible Fluorescent Protein from Eel Muscle". Cell. 153 (7): 1602–1611. doi:10.1016/j.cell.2013.05.038. PMID 23768684.
  17. ^ a b c Ghosh, Swagatha; Yu, Chi-Li; Ferraro, Daniel J.; Sudha, Sai; Pal, Samir Kumar; Schaefer, Wayne F.; et al. (2016-10-11). "Blue protein with red fluorescence". Proceedings of the National Academy of Sciences. 113 (41): 11513–11518. Bibcode:2016PNAS..11311513G. doi:10.1073/pnas.1525622113. ISSN 0027-8424. PMC 5068307. PMID 27688756.
  18. ^ a b c Park, Hyun Bong; Lam, Yick Chong; Gaffney, Jean P.; Weaver, James C.; Krivoshik, Sara Rose; Hamchand, Randy; et al. (September 2019). "Bright Green Biofluorescence in Sharks Derives from Bromo-Kynurenine Metabolism". iScience. 19: 1291–1336. Bibcode:2019iSci...19.1291P. doi:10.1016/j.isci.2019.07.019. PMC 6831821. PMID 31402257.
  19. ^ Pearn, Sophie M.; Bennett, Andrew T.D.; Cuthill, Innes C. (2001-11-07). "Ultraviolet vision, fluorescence and mate choice in a parrot, the budgerigar Melopsittacus undulatus". Proceedings of the Royal Society of London. Series B: Biological Sciences. 268 (1482): 2273–2279. doi:10.1098/rspb.2001.1813. ISSN 0962-8452. PMC 1088876. PMID 11674876.
  20. ^ Hausmann, Franziska; Arnold, Kathryn E.; Marshall, N. Justin; Owens, Ian P. F. (2003-01-07). "Ultraviolet signals in birds are special". Proceedings of the Royal Society of London. Series B: Biological Sciences. 270 (1510): 61–67. doi:10.1098/rspb.2002.2200. ISSN 0962-8452. PMC 1691211. PMID 12590772.
  21. ^ a b Gershwin, Lisa-ann (2024-02-05). Update on fluorescent mammals and birds in Tasmania (Report). doi:10.26749/25131257.v1.
  22. ^ Anich, Paula Spaeth; Anthony, Sharon; Carlson, Michaela; Gunnelson, Adam; Kohler, Allison M.; Martin, Jonathan G.; Olson, Erik R. (2021-03-26). "Biofluorescence in the platypus ( Ornithorhynchus anatinus )". Mammalia. 85 (2): 179–181. doi:10.1515/mammalia-2020-0027. ISSN 1864-1547.
  23. ^ Olson, Erik R.; Carlson, Michaela R.; Ramanujam, V. M. Sadagopa; Sears, Lindsay; Anthony, Sharon E.; Anich, Paula Spaeth; Ramon, Leigh; Hulstrand, Alissa; Jurewicz, Michaela; Gunnelson, Adam S.; Kohler, Allison M.; Martin, Jonathan G. (2021-02-18). "Vivid biofluorescence discovered in the nocturnal Springhare (Pedetidae)". Scientific Reports. 11 (1): 4125. Bibcode:2021NatSR..11.4125O. doi:10.1038/s41598-021-83588-0. ISSN 2045-2322. PMC 7892538. PMID 33603032.
  24. ^ Matz, Mikhail V.; Marshall, N. Justin; Vorobyev, Misha (2006). "Are Corals Colorful?". Photochemistry and Photobiology. 82 (2): 345–350. doi:10.1562/2005-08-18-RA-653. ISSN 0031-8655. PMID 16613484.
  25. ^ Hausmann, Franziska; Arnold, Kathryn E.; Marshall, N. Justin; Owens, Ian P. F. (2003). "Ultraviolet signals in birds are special". Proceedings of the Royal Society of London. Series B: Biological Sciences. 270 (1510): 61–67. doi:10.1098/rspb.2002.2200. ISSN 0962-8452. PMC 1691211. PMID 12590772.
  26. ^ a b Shagin, Dmitry A.; Barsova, Ekaterina V.; Yanushevich, Yurii G.; Fradkov, Arkady F.; Lukyanov, Konstantin A.; Labas, Yulii A.; et al. (2004). "GFP-like Proteins as Ubiquitous Metazoan Superfamily: Evolution of Functional Features and Structural Complexity". Molecular Biology and Evolution. 21 (5): 841–850. doi:10.1093/molbev/msh079. ISSN 1537-1719. PMID 14963095.
  27. ^ Strader, Marie E.; Aglyamova, Galina V.; Matz, Mikhail V. (January 2016). "Red fluorescence in coral larvae is associated with a diapause-like state". Molecular Ecology. 25 (2): 559–569. Bibcode:2016MolEc..25..559S. doi:10.1111/mec.13488. ISSN 0962-1083. PMID 26600127.
  28. ^ a b Ugalde, Juan A.; Chang, Belinda S. W.; Matz, Mikhail V. (2004-09-03). "Evolution of Coral Pigments Recreated". Science. 305 (5689): 1433. doi:10.1126/science.1099597. ISSN 0036-8075. PMID 15353795.
  29. ^ Yeh, Johannes T.-H.; Nam, Kwangho; Yeh, Joshua T.-H.; Perrimon, Norbert (2017-02-08). "eUnaG: a new ligand-inducible fluorescent reporter to detect drug transporter activity in live cells". Scientific Reports. 7 (1): 41619. Bibcode:2017NatSR...741619Y. doi:10.1038/srep41619. ISSN 2045-2322. PMC 5296874. PMID 28176814.
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