Apterous A modulates wing size, bristle formation and patterning in Nilaparvata lugens

Sci Rep. 2015 May 21:5:10526. doi: 10.1038/srep10526.

Abstract

Apterous A (apA), a member of the LIM-homeobox gene family, plays a critical role in the development of wing. The achaete-scute Complex (AS-C) encodes basic helix-loop-helix (bHLH) transcription factors and functions in bristle development. In the present study, we cloned apA (NlapA) and an achaete-scute homologue (NlASH) from N. lugens. Levels of NlapA and NlASH were higher in nymphs than adults, with particularly high expression in the thorax of nymphs. NlapA expressed more highly in nymphs of the macropterous strain (MS) than those of the brachypterous strain (BS) at 2(nd) and 4(th) instar. Knockdown of NlapA and NlASH in vivo generated similar phenotypic defects in the wing (loss-of-bristles, twisted or erect wing). Silencing of NlapA in nymphs of MS led to decreased wing size in adults. Moreover, depletion of NlapA suppressed expression of NlDl, Nlsal, Nlser, Nlvg and Nlwg, both in MS and BS, but induced differential responses of Nlubx and Nlnotch expression between MS and BS. Notably, expression of NlASH was regulated by NlapA. These results collectively indicate that NlapA is an upstream modulator of wing size, bristle formation and patterning. Further studies on DNA-protein and protein-protein interactions are required to elucidate NlapA-mediated regulation of wing development.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cloning, Molecular
  • Hemiptera / metabolism*
  • Homeodomain Proteins / antagonists & inhibitors
  • Homeodomain Proteins / genetics
  • Homeodomain Proteins / metabolism*
  • Insect Proteins / antagonists & inhibitors
  • Insect Proteins / genetics
  • Insect Proteins / metabolism*
  • RNA Interference
  • RNA, Double-Stranded / metabolism
  • Real-Time Polymerase Chain Reaction
  • Transcriptome
  • Wings, Animal / anatomy & histology
  • Wings, Animal / physiology*

Substances

  • Homeodomain Proteins
  • Insect Proteins
  • RNA, Double-Stranded