Chemosensory Proteins: A Versatile Binding Family
Chemosensory Proteins (CSPs), a family of small soluble polypeptides, own their name to their highly abundant expression in chemosensory organs of insects. However, CSPs are extremely versatile and perform different tasks in chemical communication, but also in unrelated functions, such as development and insecticide resistance. Their multifunction is certainly linked to their simple structure and easy refolding.
In insect chemoreception, they may perform functions similar to OBPs (Odorant-binding Proteins), another class of soluble polypeptides able to bind pheromones and odorants. Both families of proteins are reported to play roles in detecting and releasing semiochemicals with specific tasks according to species. In the first part of this review, after a brief historical introduction on their discovery, we describe structural aspects and binding properties of CSPs and compare such features with those of OBPs. Evolutionary aspects are also discussed with attention on the expansion of the CSP family across insect orders and species. The second part is focused on CSPs expressed in non-sensory organs and their possible physiological functions. Most of these proteins have been reported in pheromone glands, where they likely assist the release of chemical messages in the environment. Other functions have been reported in relation to solubilization of essential nutrients during feeding, embryo development and regeneration of amputated limbs, as well as resistance to insecticides. Finally, given the compact structure and stability of CSPs, their potential uses as biosensing elements, scavengers for noxious compounds and reservoirs for slow release of fragrances and other volatiles are proposed and discussed.
- Free JB (1987) Pheromones of social bees. Cornell University Press, Ithaca, p 218Google Scholar
- Larisika M, Kotlowski C, Steininger C, Mastrogiacomo R, Pelosi P, Schutz S, Peteu SF, Kleber C, Reiner-Rozman C, Nowak C, Knoll W (2015) Electronic olfactory sensor based on A. mellifera odorant-binding protein 14 on a reduced graphene oxide field-effect transistor. Angew Chemie Int Ed 54:13245–13248CrossRefGoogle Scholar
- Liu GX, Ma H, Xie H, Xuan N, Guo X, Fan Z, Rajashekar B, Arnaud P, Offmann B, Picimbon JF (2016) Biotype characterization, developmental profiling, insecticide response and binding property of Bemisia tabaci chemosensory proteins: role of CSP in insect defense. PLoS One 11:e0154706CrossRefPubMedPubMedCentralGoogle Scholar
- Mastrobuoni G, Qiao H, Iovinella I, Sagona S, Niccolini A, Boscaro F, Caputo B, Orejuela MR, dellaTorre A, Kempa S, Felicioli A, Pelosi P, Moneti G, Dani FR (2013) A proteomic investigation of soluble olfactory proteins in Anopheles gambiae. PLoS One 8:e75162CrossRefPubMedPubMedCentralGoogle Scholar
- Missbach C, Vogel H, Hansson BS, Groβe-Wilde E (2015) Identification of odorant binding proteins and chemosensory proteins in antennal transcriptomes of the jumping bristletail Lepismachilis y-signata and the firebrat Thermobia domestica: evidence for an independent OBP-OR origin. Chem Senses 40:615–626CrossRefPubMedGoogle Scholar
- Renthal R, Manghnani L, Bernal S, Qu Y, Griffith WP, Lohmeyer K, Guerrero FD, Borges LMF, Pérez de León A (2017) The chemosensory appendage proteome of Amblyomma americanum (Acari: Ixodidae) reveals putative odorant-binding and other chemoreception-related proteins. Insect Sci 24:730–742CrossRefPubMedGoogle Scholar
- Sun YF, De Biasio F, Qiao HL, Iovinella I, Yang SX, Ling Y, Riviello L, Battaglia D, Falabella P, Yang XL, Pelosi P (2012a) Two odorant-binding proteins mediate the behavioural response of aphids to the alarm pheromone (E)-ß-farnesene and structural analogues. PLoS One 7:e32759CrossRefPubMedPubMedCentralGoogle Scholar
- Sun M, Liu Y, Walker WB, Liu C, Lin K, Gu S, Zhang Y, Zhou J, Wang G (2013) Identification and characterization of pheromone receptors and interplay between receptors and pheromone binding proteins in the diamondback moth, Plutella xyllostella. PLoS One 8:e62098CrossRefPubMedPubMedCentralGoogle Scholar
- Werren JH et al. (2010) Functional and evolutionary insights from the genomes of three parasitoid Nasonia species. Science 327:343–348Google Scholar
- Zhou XH, Ban LP, Iovinella I, Zhao LJ, Gao Q, Felicioli A, Sagona S, Pieraccini G, Pelosi P, Zhang L, Dani FR (2013) Diversity, abundance and sex-specific expression of chemosensory proteins in the reproductive organs of the locust Locusta migratoria manilensis. Biol Chem 394:43–54CrossRefPubMedGoogle Scholar