Evolution of Protein Physical Structures in Insect Chemosensory Systems

Picimbon, Jean-François

doi:10.1007/978-3-030-05165-5_10

Cited by 16 publications

(51 citation statements)

References 149 publications

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“…The folded shape of BmorCSP4 and a number of 11 new protein foldings (11 variants) can be generated from gene splicing. (3) The primary transcripts that are a faithful copy of the gene and variant mRNAs are all subject to further typo RNA editing, resulting in an increased number of genetic variants and protein subtypes [13,[16][17][18][19][20]. Each mRNA is subject to mutations (A-to-G, A-to-U, C-to-A, C-to-U, G-to-A, G-to-U and/or U-to-C) depending on external conditions (cold/hot temperature, humidity and/or exposure to xenobiotic insecticides).…”

Section: A Very Ancient Malleable Proteinmentioning

confidence: 99%

“…The Leucine-Glutamate-Glycine-Lysine (LeuGluGlyLys) motif changes to Phenylalanine-Glutamate-Serine-Glutamate-Lysine-Lysine (PheGluSerGluLysLys) in the C-terminal tail. A Glycine residue (Gly) is inserted next to Cysteine at position 29, 55 or both [13,14,16,17,19,20]. Protein structures are generated by BmorCSP4 templates in SWISS-MODEL using the X-ray crystal structure of MbraCSPA6 (1kx9.1.A) as a reference model [7,18].…”

Section: A Very Ancient Malleable Proteinmentioning

confidence: 99%

“…In particular, we attempt to provide a comprehensive theoretical framework to explore the question of whether different edited versions of a protein such as CSP can be produced to cope with a wide variety of ligands, such as lipids and fatty acids, as well as drug compounds, insecticides and other xenobiotics. 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].…”

Section: A Very Ancient Malleable Proteinmentioning

confidence: 99%

“…The CSP gene family is not specific to insects and other arthropod classes [20,[28][29][30]. The existence of CSP in microbes cannot be a controversial issue.…”

Section: Csps and Cell Evolutionmentioning

confidence: 99%

“…Very surprisingly, the very same proteins (BmorCSP2 and BmorCSP6) were found in Bombyx and in multi-species in bacteria. BmorCSPs were found not only in bacterial germs of the genus Acinetobacter, but also in E. coli [20,30,31]. This is an intriguing discovery to discuss function and evolution in the CSP gene family.…”

Section: Csps and Cell Evolutionmentioning

confidence: 99%

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Comprehensive History of CSP Genes: Evolution, Phylogenetic Distribution and Functions

Liu

Xuan

Rajashekar

et al. 2020

Genes

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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.

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Section: A Very Ancient Malleable Proteinmentioning

confidence: 99%

Section: A Very Ancient Malleable Proteinmentioning

confidence: 99%

Section: A Very Ancient Malleable Proteinmentioning

confidence: 99%

“…The CSP gene family is not specific to insects and other arthropod classes [20,[28][29][30]. The existence of CSP in microbes cannot be a controversial issue.…”

Section: Csps and Cell Evolutionmentioning

confidence: 99%

Section: Csps and Cell Evolutionmentioning

confidence: 99%

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Comprehensive History of CSP Genes: Evolution, Phylogenetic Distribution and Functions

Liu

Xuan

Rajashekar

et al. 2020

Genes

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Functional and evolutionary characterization of chemosensory protein CSP2 in the whitefly, Bemisia tabaci

Li¹,

Dewer

Du³

et al. 2020

Pest Management Science

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BACKGROUND: Chemosensory proteins (CSPs) are thought to play essential roles in insect chemical communication, but their exact physiological functions remain unclear. RESULTS: In this study, we investigated the functions of the CSP2 gene in the whitefly Bemisia tabaci using protein expression and the binding affinity spectrum of CSP2 to different types of odor molecules. Moreover, the evolutionary characteristics of the CSP2 gene were studied. The data obtained using binding assay showed that the CSP2 protein can bind to a broad range of plant volatiles including the homoterpene (E)-3,8-dimethyl-1,4,7-nonatriene (DMNT) and its analogs. In addition, using a behavioral experimental approach we identified that DMNT can repel the selection and oviposition of B. tabaci. Furthermore, protein structure modeling, molecular docking analyses and a functional mutation experiment were carried out resulting in the final identification of key amino acid residue Y11, which displayed important roles in the binding of CSP2 to DMNT. The results also showed that Y11 is located in the pocket region where CSP2 has a pi-alkyl interaction with DMNT. Meanwhile, comparative and evolutionary analyses indicated that CSP2 shared a high sequence similarity with CSPs of other insect family members such as Sternorrhyncha and Auchenorrhyncha including aphids, whiteflies and planthoppers. CONCLUSION: These results suggested that CSP2 likely contributes to mediating responses of B. tabaci to plant volatiles, which may play a pivotal role in its feeding and oviposition preferences. Moreover, these findings could provide key information for exploring efficiency monitoring and integrated pest management strategies of B. tabaci.

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Lactobacillus for ribosome peptide editing cancer

Yue

Picimbon

2023

Clin Transl Oncol

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This study reviews newly discovered insect peptide point mutations as new possible cancer research targets. To interpret newly discovered peptide point mutations in insects as new possible cancer research targets, we focused on the numerous peptide changes found in the ‘CSP’ family on the sex pheromone gland of the female silkworm moth Bombyx mori . We predict that the Bombyx peptide modifications will have a significant effect on cancer CUP (cancers of unknown primary) therapy and that bacterial peptide editing techniques, specifically Lactobacillus combined to CRISPR, will be used to regulate ribosomes and treat cancer in humans.

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Evolution of Protein Physical Structures in Insect Chemosensory Systems

Cited by 16 publications

References 149 publications

Comprehensive History of CSP Genes: Evolution, Phylogenetic Distribution and Functions

Comprehensive History of CSP Genes: Evolution, Phylogenetic Distribution and Functions

Functional and evolutionary characterization of chemosensory protein CSP2 in the whitefly, Bemisia tabaci

Lactobacillus for ribosome peptide editing cancer

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