Vogt R G, Rybczynski R, Lerner M R
Department of Internal Medicine, Yale University School of Medicine, New Haven, Connecticut 06510.
J Neurosci. 1991 Oct;11(10):2972-84. doi: 10.1523/JNEUROSCI.11-10-02972.1991.
Odorant-binding proteins (OBPs) are small, water-soluble proteins uniquely expressed in olfactory tissue of insects and vertebrates. OBPs are present in the aqueous fluid surrounding olfactory sensory dendrites and are thought to aid in the capture and transport of hydrophobic odorants into and through this fluid. OBPs may represent the initial biochemical recognition step in olfaction, because they transport odorants to the receptor neurons. Insect OBPs are represented by multiple classes: pheromone-binding proteins (PBPs) and general odorant-binding proteins (GOBP1 and GOBP2). PBPs associate with pheromone-sensitive neurons, while GOBPs associate with general odorant-sensitive neurons. Analysis of N-terminal amino acid sequences of 14 insect OBPs isolated from six species indicated that the PBPs were variable and the GOBPs were highly conserved. However, inferred properties of these proteins were based only on partial sequence data. We now report the full-length sequences of a GOBP1 and GOBP2 from the moth Manduca sexta and compare these sequences with those of PBPs from three species, including M. sexta, Antheraea polyphemus, and A. pernyi. We also compare these with a GOBP2 of A. pernyi, previously identified only as a novel OBP. These comparisons fully support our N-terminal analysis. The signal peptide sequences of seven insect OBPs reveal conserved sequences within OBP classes, but not between OBP classes even within the same animal species. This suggests that multiple OBPs may be coexpressed in the same cell type, but differentially processed in a class-specific manner. Properties of the GOBPs suggest that general olfaction is broadly receptive at the periphery. Properties of the PBPs suggest that pheromone olfaction is discriminatory at the periphery, and that the initial biochemical steps in pheromone detection may play an active role in odor perception.
气味结合蛋白(OBP)是一类小分子水溶性蛋白,在昆虫和脊椎动物的嗅觉组织中特异性表达。OBP存在于嗅觉感觉树突周围的水性液体中,被认为有助于捕获和运输疏水性气味分子进入并穿过这种液体。OBP可能代表嗅觉中的初始生化识别步骤,因为它们将气味分子运输到受体神经元。昆虫OBP有多个类别:性信息素结合蛋白(PBP)和普通气味结合蛋白(GOBP1和GOBP2)。PBP与性信息素敏感神经元相关,而GOBP与普通气味敏感神经元相关。对从六个物种中分离出的14种昆虫OBP的N端氨基酸序列分析表明,PBP具有变异性,而GOBP高度保守。然而,这些蛋白质的推断特性仅基于部分序列数据。我们现在报告了烟草天蛾的GOBP1和GOBP2的全长序列,并将这些序列与包括烟草天蛾、多音大蚕蛾和柞蚕在内的三个物种的PBP序列进行了比较。我们还将它们与柞蚕的GOBP2进行了比较,柞蚕的GOBP2之前仅被鉴定为一种新型OBP。这些比较完全支持了我们的N端分析。七种昆虫OBP的信号肽序列揭示了OBP类别内的保守序列,但即使在同一动物物种内,不同OBP类别之间也没有保守序列。这表明多种OBP可能在同一细胞类型中共表达,但以类别特异性方式进行差异加工。GOBP的特性表明,普通嗅觉在外周具有广泛的接受性。PBP的特性表明,性信息素嗅觉在外周具有辨别性,并且性信息素检测中的初始生化步骤可能在气味感知中发挥积极作用。