Candidate pheromone binding proteins of the silkmoth Bombyx mori.
Pheromone reception is thought to be mediated by pheromone binding proteins (PBPs) in the aqueous lymph of the antennal sensilla. Recent studies have shown that the only known PBP of Bombyx mori (BmorPBP1) appears to be specifically tuned to bombykol but not to bombykal, raising the question of whether additional subtypes may exist. We have identified two novel genes, which encode candidate PBPs (BmorPBP2, BmorPBP3). Comparison with PBPs from various moth species have revealed a high degree of sequence identity and the three BmorPBP-subtypes can be assigned to distinct groups within the moth PBP family. In situ hybridization revealed that BmorPBP2 and BmorPBP3 are expressed only in relatively few cells compared to the number of cells expressing BmorPBP1. Double-labeling experiments have shown that the two novel BmorPBPs are expressed in the same cells but are not co-expressed with BmorPBP1. Furthermore, unlike BmorPBP1, cells expressing the newly identified PBPs did not surround neurons containing the BmOR-1 receptor. The results indicate that BmorPBP2 and BmorPBP3 are located in sensilla types, which are different from the long sensilla trichodea.
Forstner
Maike
M
Institute of Physiology (230), University of Hohenheim, Garbenstrasse 30, 70599 Stuttgart, Germany.
Gohl
Thomas
T
Breer
Heinz
H
Krieger
Jürgen
J
D000595:Amino Acid Sequence; D000818:Animals; D012831:Bombyx / Q000235:genetics*; D002352:Carrier Proteins / Q000235:genetics*; D018076:DNA, Complementary / Q000032:analysis; D005260:Female; D017344:Genes, Insect; D017403:In Situ Hybridization; D019476:Insect Proteins / Q000235:genetics*; D008297:Male; D008969:Molecular Sequence Data; D020133:Reverse Transcriptase Polymerase Chain Reaction; D017386:Sequence Homology, Amino Acid
D002352:Carrier Proteins; D018076:DNA, Complementary; D019476:Insect Proteins; C403713:pheromone binding protein, insect