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Purification and molecular cloning of chemosensory proteins from Bombyx mori

✍ Scribed by Jean-François Picimbon; Karen Dietrich; Sergio Angeli; Andrea Scaloni; Jürgen Krieger; Heinz Breer; Paolo Pelosi

Publisher
John Wiley and Sons
Year
2000
Tongue
English
Weight
158 KB
Volume
44
Category
Article
ISSN
0739-4462

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✦ Synopsis

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 a-helical foldings at conserved positions and a reduced hydrophobicity with respect to this novel family of chemosensory proteins. Arch. Insect Biochem. Physiol. 44:120-129, 2000.

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