Abstract

Hygrosensation is an essential sensory modality that is used to find sources of moisture. Hygroreception allows animals to avoid desiccation, an existential threat that is increasing with climate change. Humidity response, however, remains poorly understood. Here we find that humidity-detecting sensilla in the Drosophila antenna express and rely on a small protein, Obp59a. Mutants lacking this protein are defective in three hygrosensory behaviors, one operating over seconds, one over minutes, and one over hours. Remarkably, loss of Obp59a and humidity response leads to an increase in desiccation resistance. Obp59a is an exceptionally well-conserved, highly localized, and abundantly expressed member of a large family of secreted proteins. Antennal Obps have long been believed to transport hydrophobic odorants, and a role in hygroreception was unexpected. The results enhance our understanding of hygroreception, Obp function, and desiccation resistance, a process that is critical to insect survival.

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All data generated or analysed during this study are included in the manuscript and supporting files.

Article and author information

Author details

  1. Jennifer S Sun

    Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven, United States
    Competing interests
    The authors declare that no competing interests exist.
    ORCID icon "This ORCID iD identifies the author of this article:" 0000-0002-4274-0504
  2. Nikki K Larter

    Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven, United States
    Competing interests
    The authors declare that no competing interests exist.
    ORCID icon "This ORCID iD identifies the author of this article:" 0000-0002-1938-1929
  3. J Sebastian Chahda

    Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, United States
    Competing interests
    The authors declare that no competing interests exist.
  4. Douglas Rioux

    Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, United States
    Competing interests
    The authors declare that no competing interests exist.
  5. Ankita Gumaste

    Interdepartmental Neuroscience Program, Yale University, New Haven, United States
    Competing interests
    The authors declare that no competing interests exist.
  6. John R Carlson

    Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven, United States
    For correspondence
    john.carlson@yale.edu
    Competing interests
    The authors declare that no competing interests exist.
    ORCID icon "This ORCID iD identifies the author of this article:" 0000-0002-0244-5180

Funding

Dwight N. and Noyes D. Clark Scholarship Fund

  • Jennifer S Sun

P.E.O. Scholar Award

  • Jennifer S Sun

National Science Foundation (Graduate Research Fellowship Program)

  • Jennifer S Sun
  • Nikki K Larter

National Institutes of Health (National Research Service Award)

  • J Sebastian Chahda

National Institutes of Health (T32 GM007499)

  • Jennifer S Sun

National Institutes of Health (U01 Al15648-02)

  • John R Carlson

National Institutes of Health (RO1s)

  • John R Carlson

The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.

Reviewing Editor

  1. Leslie C Griffith, Brandeis University, United States

Version history

  1. Received: June 15, 2018
  2. Accepted: September 18, 2018
  3. Accepted Manuscript published: September 19, 2018 (version 1)
  4. Version of Record published: October 16, 2018 (version 2)

Copyright

© 2018, Sun et al.

This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.

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  1. Jennifer S Sun
  2. Nikki K Larter
  3. J Sebastian Chahda
  4. Douglas Rioux
  5. Ankita Gumaste
  6. John R Carlson
(2018)
Humidity response depends on the small soluble protein Obp59a in Drosophila
eLife 7:e39249.
https://doi.org/10.7554/eLife.39249

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https://doi.org/10.7554/eLife.39249