TY - JOUR
T1 - Soluble proteins from chemosensory organs of Eurycantha calcarata (Insects, Phasmatodea)
AU - Marchese, Silvana
AU - Angeli, Sergio
AU - Andolfo, Annapaola
AU - Scaloni, Andrea
AU - Brandazza, Anna
AU - Mazza, Mario
AU - Picimbon, Jean François
AU - Leal, Walter S.
AU - Pelosi, Paolo
PY - 2000
Y1 - 2000
N2 - 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 posttranslational 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. (C) 2000 Elsevier Science Ltd.
AB - 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 posttranslational 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. (C) 2000 Elsevier Science Ltd.
KW - Chemosensory proteins
KW - Eurycantha calcarata
KW - Odorant-binding proteins
KW - Phasmids
KW - RACE
KW - Sequence analysis
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U2 - 10.1016/S0965-1748(00)00084-9
DO - 10.1016/S0965-1748(00)00084-9
M3 - Article
C2 - 10989296
AN - SCOPUS:0033809025
VL - 30
SP - 1091
EP - 1098
JO - Insect Biochemistry and Molecular Biology
JF - Insect Biochemistry and Molecular Biology
SN - 0965-1748
IS - 11
ER -