Viral rhodopsins 1 are an unique family of light-gated cation channels

Nat Commun. 2020 Nov 11;11(1):5707. doi: 10.1038/s41467-020-19457-7.

Abstract

Phytoplankton is the base of the marine food chain as well as oxygen and carbon cycles and thus plays a global role in climate and ecology. Nucleocytoplasmic Large DNA Viruses that infect phytoplankton organisms and regulate the phytoplankton dynamics encompass genes of rhodopsins of two distinct families. Here, we present a functional and structural characterization of two proteins of viral rhodopsin group 1, OLPVR1 and VirChR1. Functional analysis of VirChR1 shows that it is a highly selective, Na+/K+-conducting channel and, in contrast to known cation channelrhodopsins, it is impermeable to Ca2+ ions. We show that, upon illumination, VirChR1 is able to drive neural firing. The 1.4 Å resolution structure of OLPVR1 reveals remarkable differences from the known channelrhodopsins and a unique ion-conducting pathway. Thus, viral rhodopsins 1 represent a unique, large group of light-gated channels (viral channelrhodopsins, VirChR1s). In nature, VirChR1s likely mediate phototaxis of algae enhancing the host anabolic processes to support virus reproduction, and therefore, might play a major role in global phytoplankton dynamics. Moreover, VirChR1s have unique potential for optogenetics as they lack possibly noxious Ca2+ permeability.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Calcium / metabolism
  • Cations
  • Cells, Cultured
  • Channelrhodopsins / metabolism
  • HEK293 Cells
  • Humans
  • Ion Channel Gating
  • Light
  • Neurons / metabolism
  • Phylogeny
  • Phytoplankton / virology*
  • Protein Conformation
  • Rats, Wistar
  • Rhodopsin / chemistry*
  • Rhodopsin / genetics
  • Rhodopsin / metabolism*
  • Structure-Activity Relationship
  • Viral Proteins / chemistry*
  • Viral Proteins / genetics
  • Viral Proteins / metabolism*
  • X-Ray Diffraction

Substances

  • Cations
  • Channelrhodopsins
  • Viral Proteins
  • Rhodopsin
  • Calcium