Major venom proteins of the fire ant Solenopsis invicta

insights into possible pheromone-binding function from mass spectrometric analysis

T. Das, I. Alabi, M. Colley, F. Yan, W. Griffith, S. Bach, Susan E Weintraub, R. Renthal

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Proteins in the venom of the fire ant Solenopsis invicta have been suggested to function in pheromone binding. Venom from queens and workers contains different isoforms of these proteins, consistent with the differing pheromones they secrete, but questions remain about the venom protein composition and glandular source. We found that the queen venom contains a previously uncharacterized pheromone-binding protein paralogue known as Sol i 2X1. Using imaging mass spectrometry, we located the main venom proteins in the poison sac, implying that pheromones might have to compete with venom alkaloids for binding. Using the known structure of the worker venom protein Sol i 2w, we generated three-dimensional homology models of the worker venom protein Sol i 4.02, and of the two main venom proteins in queens and female alates, Sol i 2q and Sol i 2X1. Surprisingly, the models show that the proteins have relatively small internal hydrophobic binding pockets that are blocked by about 10 amino acids of the C-terminal region. For these proteins to function as carriers of hydrophobic ligands, a conformational change would be required to displace the C-terminal region, somewhat like the mechanism known to occur in the silk moth pheromone-binding protein.

Original languageEnglish (US)
Pages (from-to)505-511
Number of pages7
JournalInsect Molecular Biology
Volume27
Issue number4
DOIs
StatePublished - Aug 1 2018

Fingerprint

Ant Venoms
fire ants
Solenopsis invicta
Pheromones
Venoms
venoms
pheromones
Polymethyl Methacrylate
Proteins
proteins
queen insects
Carrier Proteins
binding proteins
Silk
Moths
protein isoforms
Poisons
Alkaloids
protein composition
silk

Keywords

  • imaging mass spectrometry
  • pheromone-binding proteins
  • venom proteins

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Insect Science

Cite this

Major venom proteins of the fire ant Solenopsis invicta : insights into possible pheromone-binding function from mass spectrometric analysis. / Das, T.; Alabi, I.; Colley, M.; Yan, F.; Griffith, W.; Bach, S.; Weintraub, Susan E; Renthal, R.

In: Insect Molecular Biology, Vol. 27, No. 4, 01.08.2018, p. 505-511.

Research output: Contribution to journalArticle

Das, T. ; Alabi, I. ; Colley, M. ; Yan, F. ; Griffith, W. ; Bach, S. ; Weintraub, Susan E ; Renthal, R. / Major venom proteins of the fire ant Solenopsis invicta : insights into possible pheromone-binding function from mass spectrometric analysis. In: Insect Molecular Biology. 2018 ; Vol. 27, No. 4. pp. 505-511.
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