Abstract
Antennal proteins of the mole fire ant (Solenopsis invicta) were analyzed by two-dimensional gel electrophoresis, with the objective of identifying pheromone-binding proteins, which have not previously been found in ant antennae. The major low-molecular weight protein found in the male fire ant antenna was subjected to Edman degradation to determine the N-terminal amino acid sequence. Degenerate PCR primers based on this sequence were used to obtain a cDNA sequence corresponding to the full-length protein sequence. In-gel trypsin digestion followed by MALDI-TOF mass spectrometry and HPLC-ESI/MS/MS demonstrated that the protein gel spot contained only the protein corresponding to the cDNA sequence obtained by PCR. The sequence is similar to apolipophorin-III, an exchangeable lipid-binding protein. Fire ant apolipophorin-III is expressed in the antenna as well as the head, thorax and abdomen.
Original language | English (US) |
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Pages (from-to) | 101-110 |
Number of pages | 10 |
Journal | Archives of Insect Biochemistry and Physiology |
Volume | 57 |
Issue number | 3 |
DOIs | |
State | Published - Nov 2004 |
Keywords
- Apolipophorin
- Encapsulins
- Moss spectrometry
- Olfoction
- Pheromone-binding proteins
ASJC Scopus subject areas
- Insect Science
- Physiology
- Biochemistry