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. 2014 Oct 13;9(10):e109590. doi: 10.1371/journal.pone.0109590

Figure 2. Alignment of insect sNPF sequences.

Figure 2

A. The unique amino acid sequence of the S. invicta short neuropeptide F active peptide(s) is compared to those of other insect species. Aligned sNPF sequences are from (top to bottom): three ant species Solin (Solenopsis invicta KJ812404), Acrec (Acromyrmex echinatior EGI59536.1), and Camfl (Camponotus floridanus EFN66516.1); the honey bee, Apime (Apis mellifera XP_003250155.1); a basal ant, Harsa (Harpegnathos saltator EFN85447.1); the locust, Schgr (Schistocerca gregaria AHH85823.1); the flour beetle, Trica (Tribolium castaneum EEZ97763.1); dipterans, Anoga (Anopheles gambiae ABD96048.1), Aedae (Aedes aegypti ABE72968.1), and Drome (Drosophila melanogaster AAN11060.1); the brown planthopper, Nillu (Nilaparvata lugens BAO00976.1), and three lepidopterans, Helar (Helicoverpa armigera AGH25568.1), Danpl (Danaus plexippus EHJ63336.1), and Bommo (Bombyx mori NP_001127729.1). Identical amino acid residues are shaded black. In the alignment, active peptides corresponding to the location of S. invicta sNPFs are underlined with a solid line, and additional orthologous peptides encoded in cDNAs from other species are underlined with dashed lines. Arrowheads indicate the predicted post-translational cleavage sites for processing the prepropeptide to active peptide(s). B. Alignment of partial sNPF nucleotide sequences encoding the active peptide in four ant species. Identical nucleotides are shaded black. Amino acid residues for the active sNPF peptide (shaded gray) are in the middle of the respective codon; for S. invicta are at the top and for the other three ant species, at the bottom. The arrowhead indicates a transversion from C to G in the codon first position in S. invicta resulting in Ala (A), and not Pro (P) as in other ants, and the insertion of six additional nucleotides also extends the peptide length. There is a conservative replacement of R for H in S. invicta and F (TTT or TTC) is replaced with Y (TAC). The sequence for C-terminal α-amidation of Y or F is X-Gly-basic residue (R), and Gly provides the nitrogen for the same [70].