Structure of Bombyx mori Chemosensory Protein 1 in Solution
S. Jansen1, J. Chmelík2, L. Žídek2, P. Padrta2, P. Novák2, J.-F. Picimbon1, C. Löfstedt1 and V. Sklenář2
1 Lund University, Department of Ecology, SE-22362 Lund, Sweden
2 Masaryk
University, Faculty of Science, National Centre for Biomolecular Research,
Kotlářská 2, CZ-61137 Brno, Czech Republic
xchmelik@chemi.muni.cz
In insects, two different soluble protein groups have been identified in
the antennal lymph. The first group comprises the Odorant Binding Proteins
(OBPs). These proteins are approximately 150
residues long and contain six highly conserved cysteines forming three
disulfide bridges. They are implied in the binding of pheromones and odorant
molecules. The second group is formed by Chemosensory Proteins (CSPs). CSPs are
smaller proteins of around 110 amino acids that contain only four cysteines
linked by two disulfide bridges, at different positions than those from OBPs.
Their signature motif is CX6CX18CX2C.
The
first proposed role of CSPs was based on their tissue localization. They are
mainly expressed in chemosensory sensillae in antennae, legs, proboscis and
other chemosensory organs and they have been attributed a role in carrying
chemosensory or gustatory molecules. However, no binding to taste or odor
molecules has yet been demonstrated. On the other hand, binding to pheromone
compounds and fatty acids has been shown in Mamestra
brassicae and in Apis mellifera.
Moreover, they have a role in solubilizing cuticular hydrocarbons in ants.
Thus, the role of CSPs can be extended to carrier proteins for hydrophobic
ligands.
Here
we report the determination of the structure of Bombyx mori CSP1 (BmorCSP1) by NMR. BmorCSP1 is expressed mainly in
antennae and legs and was cloned from antennal cDNA. The overall fold of
BmorCSP1 is globular and comprises six α-helices. These helices span
residues 10-14, 17-27, 35-49, 57-72, 75-85, and 92-100. The hydrophobic edges of the helices are formed mostly by leucine
and isoleucine residues and therefore well suited to constitute a binding site
for hydrophobic ligands.