Soluble proteins of chemical communication in the social wasp Polistes dominulus

被引:159
作者
Calvello, M
Guerra, N
Brandazza, A
D'Ambrosio, C
Scaloni, A
Dani, FR
Turillazzi, S
Pelosi, P
机构
[1] Dipartimento Chim & Biotecnol Agrarie, I-56124 Pisa, Italy
[2] CNR, ISPAAM, Prote & Mass Spectrometry Lab, Naples, Italy
[3] Univ Florence, Dipartimento Biol Anim & Genet, I-50121 Florence, Italy
关键词
odorant-binding protein; chemosensory protein; chemical communication; fluorescence binding assay; N-phenyl-1-naphthylamine; oleoamide; Polistes dominulus;
D O I
10.1007/s00018-003-3186-5
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Members of the odorant-binding protein (OBP) and chemosensory protein (CSP) families were identified and characterised in the sensory tissues of the social wasp Polistes dominulus (Hymenoptera: Vespidae). Unlike most insects so far investigated, OBPs were detected in antennae, legs and wings, while CSPs appeared to be preferentially expressed in the antennae. The OBP is very different from the homologous proteins of other Hymenopteran species, with around 20 % of identical residues, while the CSP appears to be much better conserved. Both OBP and CSP, not showing other post-translational modifications apart from disulphide bridges, were expressed with high yields in a bacterial system. Cysteine pairing in the recombinant and native proteins follows the classical arrangements described for other members of these classes of proteins. OBPs isolated from the wings were found to be associated with a number of long-chain aliphatic amides and other small organic molecules. Binding of these ligands and other related compounds was measured for both recombinant OBP and CSP.
引用
收藏
页码:1933 / 1943
页数:11
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