Protein that makes sense in the Argentine ant
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With a protein-based approach, we have identified and cloned the cDNA encoding a chemosensory protein (LhumCSP) in the Argentine ant, Linepithema humile. The open reading frame of the cloned cDNA encoded a signal peptide (20 residues), and a mature protein (pI 4.62) of 106 amino acid residues. The calculated molecular mass (12,453 Da) was in agreement with the molecular mass measured by on-line chromatography–electrospray ionization mass spectrometry (12,448 Da), given the formation of two disulfide bridges. LhumCSP shared sequence similarity with various CSPs, particularly those identified and/or cloned from moth species. Also, LhumCSP showed the hallmark of the chemosensory proteins, i.e., four well conserved cysteine residues. The antennal protein was not detected in non-olfactory tissues (leg and thorax) contrary to a putative pheromone-binding protein isolated from the thorax of the red imported fire ant, Solenopsis invicta. In addition, these findings suggest that, as in Orthopterans and Phasmids, the protein that makes sense in the Argentine ant is not an odorant-binding protein, but rather a chemosensory protein.
KeywordsMolecular Mass Disulfide Cysteine Residue Ionization Mass Spectrometry Disulfide Bridge
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