Functional characterization of Aquaporin-like genes in the human bed bug Cimex lectularius

Sci Rep. 2017 Jun 12;7(1):3214. doi: 10.1038/s41598-017-03157-2.

Abstract

The bed bug Cimex lectularius is a blood-feeding re-emerging annoyance pest insect that has the ability to transmit Trypanosoma cruzi under experimental laboratory conditions. Aquaporins (AQPs) are water channel proteins that are essential in biological organisms. C. lectularius are constantly exposed to water-related stress, suggesting that AQPs may offer novel control avenues. We identified and cloned four AQPs from C. lectularius, assessed tissue and lifestage-specific expression, and characterized biochemical functions in vitro and in vivo. We identified an efficient water-specific AQP (ClAQP1), two aquaglyceroporins (ClGlp1 and ClGlp2) and a homolog of Drosophila melanogaster big brain (ClBib). ClGlp1 was only functional when co-expressed with the water-specific AQP. Simultaneous RNAi gene silencing of ClAQP1 and ClGlp1 significantly reduced water and urea excretion post blood feeding. The Bib homologue was enriched in embryos, exclusively expressed in ovaries, and when silenced, dramatically increased bug fecundity. Our data demonstrate that AQPs have critical roles in excretion, water homeostasis and reproduction in C. lectularius, and could be potential targets for control in this notorious pest.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Aquaporins / classification
  • Aquaporins / genetics*
  • Aquaporins / metabolism
  • Bedbugs / genetics*
  • Bedbugs / growth & development
  • Bedbugs / metabolism
  • Female
  • Fertility / genetics
  • Gene Expression Profiling*
  • Humans
  • Insect Proteins / genetics*
  • Insect Proteins / metabolism
  • Male
  • Oocytes / metabolism
  • Phylogeny
  • Protein Isoforms / genetics
  • Protein Isoforms / metabolism
  • RNA Interference
  • Water / metabolism
  • Xenopus laevis

Substances

  • Aquaporins
  • Insect Proteins
  • Protein Isoforms
  • Water