Purification and molecular cloning of chemosensory proteins from Bombyx mori.
Soluble low molecular weight acidic proteins are suspected to transport stimulus molecules to the sensory neurons within insect sensilla. From the antennae of Bombyx mori, we have purified and sequenced a protein (BmorCSP1) bearing sequence similarity to a class of soluble chemosensory proteins recently discovered in several orders of insects. Based on its N-terminal sequence, the cDNA encoding this protein has been amplified and cloned. Differential screening of a B. mori antennal cDNA library led to the identification of a second gene encoding a related protein (BmorCSP2), sharing 35-40% identity to BmorCSP1 and chemosensory proteins from other species. The predicted secondary structures of moth's, chemosensory proteins comprise alpha-helical foldings at conserved positions and a reduced hydrophobicity with respect to this novel family of chemosensory proteins.
Picimbon
J F
JF
Institut für Physiologie, Universität Hohenheim, Stuttgart, Germany. jfp@uni-hohenheim.de
Dietrich
K
K
Angeli
S
S
Scaloni
A
A
Krieger
J
J
Breer
H
H
Pelosi
P
P
D000595:Amino Acid Sequence; D000818:Animals; D012831:Bombyx / Q000737:chemistry / Q000235:genetics*; D003001:Cloning, Molecular; D017344:Genes, Insect; D019476:Insect Proteins / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D008969:Molecular Sequence Data; D009475:Neurons, Afferent / Q000737:chemistry*; D014018:Tissue Distribution; D014020:Tissue Extracts
C412286:CSP1 protein, Bombyx mori; C412285:CSP2 protein, Bombyx mori; D019476:Insect Proteins; D014020:Tissue Extracts