Abstract
In this review we present the developmental, histological, evolutionary and functional properties of insect chemosensory proteins (CSPs) in insect species. CSPs are small globular proteins folded like a prism and notoriously known for their complex and arguably obscure function(s), particularly in pheromone olfaction. Here, we focus on direct functional consequences on protein function depending on duplication, expression and RNA editing. The result of our analysis is important for understanding the significance of RNA-editing on functionality of CSP genes, particularly in the brain tissue.
Highlights
We propose that Chemosensory Proteins (CSPs) play a key role in activating the omega6 fatty acid pathway, which is necessary to produce diacylglycerol (DAG) that will in turn activate phospholipase kinase C and phosphorylation of many various different proteins (Figure 6) [56]
We attempt to engage in an understanding of their neofunctionalization or ability to interact with lipids and fatty acids for neuroplasticity
The biochemical mechanisms of CSPs in the resistance against insecticide has not been fully investigated, a role of CSPs at different levels of the insect immunological defense is strongly supported by the ability of whitefly CSP1s to interact with lipids, while whitefly CSP2s and CSP3s have the ability to interact directly with specific xenobiotic compounds such as cinnamaldehydes from plant oils [15]
Summary
Chemosensory proteins are a class of small (10–12 kDa) soluble proteins reported for the first time by Nomura et al (1982) as an up-regulated factor in the regenerating legs of Periplaneta americana [1]. RNA and protein editing could account for the theoretical problem of CSPs interacting with a million or trillion possible ligands, referring not necessarily to the olfactory receptor combinatorial coding theory, but to the recognition, transport and degradation of an enormous amount of potential toxicants and/or all the lipid metabolites that are necessary to activate nuclear receptors, trigger enzymes in different reactions of a chain and/or regulate gene expression in various cellular physiological systems (Figure 1) All of these complementary mechanisms would enable the CSPs to be malleable, i.e., to have a sequence that can be recoded in order to orientate the protein to a new function. It is a hypothesis that is largely compatible with the existence of CSPs in different levels within many various kingdoms that contain organisms with cell walls, i.e., arthropods, bacteria, insects and plants [20,28,29,30]
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