Visual tuning in the flashlight fish Anomalops katoptron to detect blue, bioluminescent light

PLoS One. 2018 Jul 11;13(7):e0198765. doi: 10.1371/journal.pone.0198765. eCollection 2018.

Abstract

Bioluminescence is a fascinating phenomenon and can be found in many different organisms including fish. It has been suggested that bioluminescence is used for example for defense, prey attraction, and for intraspecific communication to attract for example sexual partners. The flashlight fish, Anomalops katoptron (A. katoptron), is a nocturnal fish that produces bioluminescence and lives in shallow waters, which makes it ideal for laboratory studies. In order to understand A. katoptron's ability to detect bioluminescent light (480 to 490 nm) at night, we characterized the visual system adaptation of A. katoptron using phylogenetic, electrophysiological and behavioral studies. We found that the retinae of A. katoptron contain rods and sparse cones. A. katoptron retinae express two main visual pigments, rhodopsin (RH1), and to a lesser extent, rhodopsin-like opsin (RH2). Interestingly, recombinant RH1 and RH2 are maximally sensitive to a wavelength of approximately 490 nm light (λmax), which correspond to the spectral peak of in vivo electroretinogram (ERG) measurements. In addition, behavioral assays revealed that A. katoptron is attracted by low intensity blue but not red light. Collectively, our results suggest that the A. katoptron visual system is optimized to detect blue light in the frequency range of its own bioluminescence and residual starlight.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptation, Physiological*
  • Amino Acid Sequence
  • Animals
  • Electroretinography
  • Fish Proteins / genetics*
  • Fish Proteins / metabolism
  • Fishes
  • Gene Expression
  • HEK293 Cells
  • Humans
  • Light
  • Luminescence
  • Luminescent Measurements / methods
  • Opsins / genetics*
  • Opsins / metabolism
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Retinal Cone Photoreceptor Cells / cytology
  • Retinal Cone Photoreceptor Cells / physiology*
  • Retinal Rod Photoreceptor Cells / cytology
  • Retinal Rod Photoreceptor Cells / physiology*
  • Rhodopsin / genetics*
  • Rhodopsin / metabolism
  • Sequence Alignment
  • Sequence Homology, Amino Acid

Substances

  • Fish Proteins
  • Opsins
  • Recombinant Proteins
  • Rhodopsin

Grants and funding

MD was supported by Hans-Böckler Foundation. MN and MDM (5806/1-2 and 5806/2-1) were funded by the German Science Foundation (DFG). This work was supported by funds from the Ruhr University of Bochum, Germany and by Deutsche Forschungsgemeinschaft (DFG) grants He2471/18-1 Priority Program (SPP1926).