Apolipophorin-III-like protein expressed in the antenna of the red imported fire ant, Solenopsis invicta Buren (Hymenoptera: Formicidae)

• Published in: Archives of insect biochemistry and physiology 2004-11, Vol.57 (3), p.101-110
• Main Authors: Guntur, K.V.P, Velasquez, D, Chadwell, L, Carroll, C, Weintraub, S, Cassill, J.A, Renthal, R
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; amino acid sequences; Animals; antennae; Ants - genetics; Ants - metabolism; apolipophorin; Apolipoproteins - genetics; Apolipoproteins - metabolism; Base Sequence; binding proteins; complementary DNA; DNA Primers; Electrophoresis, Gel, Two-Dimensional; encapsulins; fire ants; Formicidae; insect pheromones; insect proteins; lipid-binding proteins; Male; males; Mass Spectrometry; Molecular Sequence Data; nucleotide sequences; olfaction; Organophosphorus Compounds; pheromone-binding proteins; Reverse Transcriptase Polymerase Chain Reaction; Sense Organs - metabolism; Sequence Alignment; Sequence Analysis, DNA; Solenopsis invicta
• ISSN: 0739-4462; 1520-6327
• DOI: 10.1002/arch.20019

Antennal proteins of the male 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.