We describe the identification and characterization of two new cDNAs encoding pheromone-binding proteins (PBPs) from the male antennae of Sesamia nonagrioides, a species where no PBPs have been identified to date. Because PBPs are thought to participate in the first step of odor detection in a specific manner, we focused our investigation on this olfactory protein family using reverse transcription–polymerase chain reaction strategies. The deduced amino acid sequences of SnonPBP1 and SnonPBP2 revealed mature proteins of 142 and 143 amino acids, respectively, with six cysteine residues in conserved positions relative to other known PBPs. The alignment of the two mature S. nonagrioides PBPs with other noctuid PBPs showed high sequence identity (70– 80%) with other full-length sequences from GenBank. Sequence identity between SnonPBP1 and SnonPBP2 was only 46%, suggesting that the two proteins belong to different classes of PBPs already described from the Noctuidae. Furthermore, analyses of expression patterns of SnonPBP1 and SnonPBP2 were performed by in situ hybridization on antennae of both sexes, and these studies revealed the expression of the two PBPs at the bases of olfactory sensilla (basiconica or trichodea) from both sexes. The possible binding properties of these two new PBPs are discussed according to their homologies with other known PBPs and S. nonagrioides pheromone components.
Molecular Cloning and in Situ Expression Patterns of Two New Pheromone-Binding Proteins from the Corn Stemborer Sesamia nonagrioides
DE SANTIS, FEDERICA;CONTI, Eric;
2006
Abstract
We describe the identification and characterization of two new cDNAs encoding pheromone-binding proteins (PBPs) from the male antennae of Sesamia nonagrioides, a species where no PBPs have been identified to date. Because PBPs are thought to participate in the first step of odor detection in a specific manner, we focused our investigation on this olfactory protein family using reverse transcription–polymerase chain reaction strategies. The deduced amino acid sequences of SnonPBP1 and SnonPBP2 revealed mature proteins of 142 and 143 amino acids, respectively, with six cysteine residues in conserved positions relative to other known PBPs. The alignment of the two mature S. nonagrioides PBPs with other noctuid PBPs showed high sequence identity (70– 80%) with other full-length sequences from GenBank. Sequence identity between SnonPBP1 and SnonPBP2 was only 46%, suggesting that the two proteins belong to different classes of PBPs already described from the Noctuidae. Furthermore, analyses of expression patterns of SnonPBP1 and SnonPBP2 were performed by in situ hybridization on antennae of both sexes, and these studies revealed the expression of the two PBPs at the bases of olfactory sensilla (basiconica or trichodea) from both sexes. The possible binding properties of these two new PBPs are discussed according to their homologies with other known PBPs and S. nonagrioides pheromone components.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.