Literature DB >> 10989296

Soluble proteins from chemosensory organs of Eurycantha calcarata (Insects, Phasmatodea).

S Marchese1, S Angeli, A Andolfo, A Scaloni, A Brandazza, M Mazza, J Picimbon, W S Leal, P Pelosi.   

Abstract

Three related nucleotide sequences, encoding mature proteins of 108-113 amino acids, have been obtained from antennal cDNA of the Phasmid Eurycantha calcarata. Among these, one is also expressed in the tarsi as demonstrated by N-terminal sequence and mass spectrometric analyses of protein samples isolated from both organs. PCR experiments performed with specific primers, showed that this species is also expressed in the mouth organs and in the cuticle, while the other two are antennal specific. All three isoforms are similar to Drosophila OS-D and other proteins reported in several insect orders, but one of them is significantly different from the other two. The best conserved elements are the N-terminal region and the four cysteine residues. Accurate ESMS measurements indicated that all cysteines are involved in two disulphide bonds and ruled out the occurrence of additional post-translational modifications. Polyclonal antibodies, raised against the purified protein, did not react with proteins of the same class expressed in another Phasmid species, Carausius morosus, and in the orthopteran Schistocerca gregaria, nor did antibodies against these proteins recognise those of E. calcarata.

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Year:  2000        PMID: 10989296     DOI: 10.1016/s0965-1748(00)00084-9

Source DB:  PubMed          Journal:  Insect Biochem Mol Biol        ISSN: 0965-1748            Impact factor:   4.714


  18 in total

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10.  Molecular cloning, expression and molecular modeling of chemosensory protein from Spodoptera litura and its binding properties with Rhodojaponin III.

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