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172 results for “P450”
Data from: Genetic mapping identifies a major locus spanning P450 clusters associated with pyrethroid resistance in kdr-free Anopheles arabiensis from Chad
Prevention of malaria transmission throughout much of Africa is dependent on bednets that are impregnated with pyrethroid insecticides. Anopheles arabiensis is the major malaria vector in Chad and efforts to control this vector are threatened by the emergence of pyrethroid resistance. WHO bioassays revealed that An. arabiensis from Ndjamena is resistant to pyrethroids and dichlorodiphenyltrichloroethane (DDT) but fully susceptible to carbamates and organophosphates. No 1014F or 1014S kdr alleles were detected in this population. To determine the mechanisms that are responsible for resistance, genetic crosses were established between the Ndja strain and an insecticide susceptible population from Mozambique. Resistance was inherited as an autosomal trait and quantitative trait locus (QTL) mapping identified a single major locus on chromosome 2R, which explained 24.4% of the variance in resistance. This QTL is enriched in P450 genes including 25 cytochrome P450s in total. One of these, Cyp6p4 is 22-fold upregulated in the Ndja strain compared with the susceptible. Piperonyl butoxide (PBO) synergist and biochemical assays further support a role for P450s in conferring pyrethroid resistance in this population.
Data from: Cytochrome P450 diversification and hostplant utilization patterns in specialist and generalist moths: birth, death, and adaptation
Across insect genomes, the size of the cytochrome P450 monooxygenase (CYP) gene superfamily varies widely. CYPome size variation has been attributed to reciprocal adaptive radiations in insect detoxification genes in response to plant biosynthetic gene radiations driven by coevolution between herbivores and their chemically defended hostplants. Alternatively, variation in CYPome size may be due to random "birth and death" processes, whereby exponential increase via gene duplications is limited by random decay via gene death or transition via divergence. We examined CYPome diversification in the genomes of seven Lepidoptera species varying in host breadth from monophagous (Bombyx mori) to highly polyphagous (Amyelois transitella). CYPome size largely reflects the size of Clan 3, the clan associated with xenobiotic detoxification, and to some extent phylogenetic age. Consistently across genomes, families CYP6, CYP9, and CYP321 are most diverse and CYP6AB, CYP6AE, CYP6B, CYP9A, and CYP9G are most diverse among subfamilies. Higher gene number in subfamilies is due to duplications occurring primarily after speciation and specialization ("P450 blooms"), and the genes are arranged in clusters, indicative of active duplicating loci. In the parsnip webworm, Depressaria pastinacella, gene expression levels in large subfamilies are high relative to smaller subfamilies. Functional and phylogenetic data suggest a correlation between highly dynamic loci (reflective of extensive gene duplication, functionalization, and in some cases loss) and the ability of enzymes encoded by these genes to metabolize hostplant defenses, consistent with an adaptive, nonrandom process driven by ecological interactions.
Data from: Positional cloning of rp2 QTL associates the P450 genes CYP6Z1, CYP6Z3 and CYP6M7 with pyrethroid resistance in the malaria vector Anopheles funestus
Pyrethroid resistance in Anopheles funestus is threatening malaria control in Africa. Elucidation of underlying resistance mechanisms is crucial to improve the success of future control programs. A positional cloning approach was used to identify genes conferring resistance in the uncharacterised rp2 QTL previously detected in this vector using F6 Advanced Intercross Lines (AIL). A 113 kb BAC clone spanning rp2 was identified and sequenced revealing a cluster of fifteen P450 genes and one salivary protein gene (SG7-2). Contrary to An. gambiae, AfCYP6M1 is triplicated in An. funestus while AgCYP6Z2 ortholog is absent. 565 new SNPs were identified for genetic mapping from rp2 P450s and other genes revealing high genetic polymorphisms with 1 SNP every 36bp. A significant genotype/phenotype association was detected for rp2 P450s but not for a cluster of cuticular protein genes previously associated with resistance in An. gambiae. QTL mapping using F6 AIL confirms the rp2 QTL with an increase logarithm of odds (LOD) score of 5. Multiplex gene expression profiling of 15 P450s and other genes around rp2 followed by individual validation using qRT-PCR indicated a significant over-expression in the resistant FUMOZ-R strain of the P450s AfCYP6Z1, AfCYP6Z3, AfCYP6M7 and the glutathione-s-transferase GSTe2 with respective fold-change of 11.2, 6.3, 5.5 and 2.8. Polymorphisms analysis of AfCYP6Z1 and AfCYP6Z3 identified amino acid changes potentially associated with resistance further indicating that these genes are controlling the pyrethroid resistance explained by the rp2 QTL. The characterisation of this rp2 QTL significantly improves our understanding of resistance mechanisms in An. funestus.
Fig. 8 in Development of an efficient transient expression system for Siraitia grosvenorii fruit and functional characterization of two NADPH-cytochrome P450 reductases
Fig. 8. HPLC chromatogram of the mogrol standard and Agrobacterium-mediated transient expression of fruit harbouring pTRV-SgCPRs and pTRV-0 at 24 h after agroinfiltration.
Fig. 9 in Development of an efficient transient expression system for Siraitia grosvenorii fruit and functional characterization of two NADPH-cytochrome P450 reductases
Fig. 9. (A) Mogrol content in the S. grosvenorii fruit harbouring PBI121, PBI121-SgCPR1, and PBI121-SgCPR2. (B) MIIE content in the S. grosvenorii fruit harbouring PBI121, PBI121-SgCPR1, and PBI121-SgCPR2. (C) MIII content in the S. grosvenorii fruit harbouring PBI121, PBI121-SgCPR1, and PBI121-SgCPR2. (D) Accumulation of mogrol in the S. grosvenorii fruit harbouring pTRV, pTRV-SgCPR1, and pTRV-SgCPR2. (E) Accumulation of MII in the S. grosvenorii fruit harbouring pTRV, pTRV- SgCPR1, and pTRV-SgCPR2. (F) Accumulation of MIII in the S. grosvenorii fruit harbouring pTRV, pTRV-SgCPR1, and pTRV-SgCPR2. The values are the mean ± SD of three independent biological replicates.
Fig. 7 in Development of an efficient transient expression system for Siraitia grosvenorii fruit and functional characterization of two NADPH-cytochrome P450 reductases
Fig. 7. HPLC chromatogram of the mogrol standard and Agrobacterium-mediated transient expression of fruit harbouring PBI121-SgCPRs and PBI121 at 24 h after agroinfiltration.
Fig. 2 in Development of an efficient transient expression system for Siraitia grosvenorii fruit and functional characterization of two NADPH-cytochrome P450 reductases
Fig. 2. (A) Cloning of full-length and specific fragments of the SgCPR1 and SgCPR2 genes from S. grosvenorii cDNA. M, marker (2000 bp). The fulllength SgCPR1 and SgCPR2 genes are shown in red brackets, whereas the blue arrow indicates the specific fragments of the SgCPR1 and SgCPR2 genes. (B) Vector map of PBI121. (C) Construction of PBI12- SgCPR recombinant plasmids with the GUS marker and CaMV35S promoter. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
Fig. 5 in Development of an efficient transient expression system for Siraitia grosvenorii fruit and functional characterization of two NADPH-cytochrome P450 reductases
Fig. 5. qRT-PCR analysis of SgCPR1 and SgCPR2 in fruit after infiltration (at t = 0 h). Relative expression levels were normalized to t = 0 h. (A) Relative transcript levels of SgCPR1 in fruit harbouring PBI121- SgCPR1 and PBI121. (B) SgCPR2 gene expression levels in fruit harbouring PBI121 and PBI121-SgCPR2. (C) Relative expression levels of SgCPR1 in fruit harbouring pTRV-SgCPR1 and pTRV-0. (D) Expression levels of SgCPR2 in fruit harbouring pTRV-SgCPR2 and pTRV-0. The relative expression levels normalized to the level of the SgUBQ gene. All the data are shown as means±SDs. * indicates significant differences at p <0.05 (LSD test).
Fig. 3 in Development of an efficient transient expression system for Siraitia grosvenorii fruit and functional characterization of two NADPH-cytochrome P450 reductases
Fig. 3. (A) Selective nucleotide sequences for VIGS in S. grosvenorii, which were inserted into EcoRI and BamHI. (B) pTRV2-SgCPR recombinant plasmid construction.
Fig. 1 in Development of an efficient transient expression system for Siraitia grosvenorii fruit and functional characterization of two NADPH-cytochrome P450 reductases
Fig. 1. The mogroside biosynthetic pathway in S. grosvenorii. The blue box on the left shows the generation of mogrol, which is a unique nonglycosylated tetra-hydroxycucurbitane in S. grosvenorii. The red box on the right represents a series of glycosylation reactions. The enzyme names are abbreviated as follows: SgSQE, squalene epoxidase; SgCS, cucurbitadienol synthase; SgEPH, epoxide hydrolase; SgCYP450, cytochrome P450 monooxygenase; SgCPR, NADPHcytochrome P450 reductase; SgUGT, UDP-glucosyltransferase. Among these, the candidate SgCPRs are highlighted in red. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
Fig. 6 in Development of an efficient transient expression system for Siraitia grosvenorii fruit and functional characterization of two NADPH-cytochrome P450 reductases
Fig. 6. Accumulation of MIII and MIIE. (A) Total ion chromatograms of ten standard mixtures determined by LC-MS/MS. Among these, the retention times of MIII and MIIE were 10.01 and 12.09 min, respectively. (B) Extracted ion chromatograms of the sample. The red arrow indicates the Q1/Q3 mass chromatograms of MIII, which are in the red box. The Q1/Q3 mass chromatograms of MIIE are shown in the blue box, as indicated by the blue arrow. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
Fig. 4 in Development of an efficient transient expression system for Siraitia grosvenorii fruit and functional characterization of two NADPH-cytochrome P450 reductases
Fig. 4. Histochemical GUS assay of transient expression in S. grosvenorii. GUS expression was detected in fruit but not in CK or leaves.
Fig. 6 in Cytochrome P450 catalyses the 29-carboxyl group formation of celastrol
Fig. 6. Molecular docking and mutagenesis assay of TwCYP712K1 from T. wilfordii. (a) Molecular docking of TwCYP712K1 with friedelin and the amino acid residues in the active site that were selected for mutagenesis. Friedelin (yellow); haem (green with red and blue). (b) The active site of TwCYP712K1 is shown as a cartoon and surface model. (c) The production of 29- hydroxyfriedelan-3-one in yeast harbour TwCYP712K1 or its mutants. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)
Fig. 5 in Cytochrome P450 catalyses the 29-carboxyl group formation of celastrol
Fig. 5. The role of TwCYP712K1 in celastrol biosynthesis. (a) Network of differentially expressed CYP450s and TwOSC involved in the biosynthesis of celastrol. Transcripts are represented by circles and metabolites by squares and edges are drawn when the linear correlation coefficient is> 0.7 in that tissues. The size of each circle represents the amount of expression of the gene. The pie chart shows the ratio of gene accumulation expression in different tissues. Colour key: the root was represented by purple, the stem periderm by orange, leaves by green, the stem vascular bundle by blue and flowers by red. (b) Relative expression of TwCYP712K1 in RNAi suspension cells and control suspension cells. (c) Relative expression of TwCYP712K1 in the overexpression suspension cells and control suspension cells. (d) Celastrol content in the RNAi suspension cells, overexpression suspension cells and their control suspension cells. Student's t-test was used to test for significant differences in gene expression levels and celastrol levels between the control group and experimental group. The data represent the average ± SD of at least three independent lines of suspension cells. CK, control group; OE, overexpression group; and RI, RNA interference group. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)
Fig. 4 in Cytochrome P450 catalyses the 29-carboxyl group formation of celastrol
Fig. 4. Gas chromatography-mass spectrometry (GC-MS) analysis of the products in yeast strains harbouring TwCYP712K1 from T. wilfordii. (a) Gas chromatographymass spectrometry (GC-MS) analysis of the products in yeast strains harbouring TwCYP712K1 from T. wilfordii. Peak 1, friedelin; Peak 2, 29-hydroxyfriedelan-3-one; Peak 4, polpunonic acid. (b) The reaction catalysed by TwCYP712K1. TIC, Total Ion Chromatography; EIC, Extracted Ion Chromatogram.
Fig. 3 in Cytochrome P450 catalyses the 29-carboxyl group formation of celastrol
Fig. 3. Phylogenetic tree of candidate P450s from T. wilfordii. The maximum-likelihood method was used to construct this tree with 1000 replicate bootstrap supports.
Fig. 2 in Cytochrome P450 catalyses the 29-carboxyl group formation of celastrol
Fig. 2. Hierarchical clustering of RNA-Seq expression data and heat map depicting the expression profile of candidate P450 genes. (a) The gene expression of candidate P450 genes in different tissues of T. wilfordii. (b) The gene expression of candidate P450 genes in MeJA-induced suspension cells of T. wilfordii. Colour key: candidate CYP72 family genes (blue), candidate CYP450 genes showing specific expression in the root and induced by MeJA (red), and other candidate CYP450 genes with high expression levels in the root and TwOSC1-3 (black). RX, root xylem; RP, root phloem; RB, root periderm; PS, stem vascular bundle; SB, stem periderm; F, Flowers; and L, Leaves. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)
Fig. 1 in Cytochrome P450 catalyses the 29-carboxyl group formation of celastrol
Fig. 1. The proposed carboxyl group formation of celastrol at the C-29 position and carboxyl group formation of β-amyrin at C-30 position by other cytochrome P450s. The red dashed arrows indicate one or multiple proposed step reactions, and the black solid arrow indicates a biosynthetic reaction catalysed by known CYP450 genes. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)
Fig. 7 in P450 variations bifurcate the early terpene indole alkaloid pathway in Catharanthus roseus and Camptotheca acuminata
Fig. 7. Molecular models of Catharanthus CYP72A1 and Camptotheca CYP72A564 and CYP72A565. (A) Backbone overlays of Catharanthus CYP72A1 and Camptotheca CYP72A564 and CYP72A565 models are shown with the alpha-carbon RMSD amongst CYP72A1, CYP72A564 and CYP72A565 depicted from green (0.0 Å) to yellow (3.0 Å) to red (4.5 Å). (B) SRS regions in CYP72A proteins shown with predicted substrate contact residues (gray fill). (C) Identical versus (D) different side chain residues predicted within 4.5 Å of loganin (aqua) docked in Catharanthus CYP72A1 (blue) and loganic acid (gray) docked in Camptotheca CYP72A564 (orange). (E) Identical versus (F) different side chain residues predicted within 4.5 Å of loganin (aqua) docked in Catharanthus CYP72A1 (blue) and loganic acid (gray) docked in Camptotheca CYP72A565 (rose).
Fig. 5 in P450 variations bifurcate the early terpene indole alkaloid pathway in Catharanthus roseus and Camptotheca acuminata
Fig. 5. Area of loganic acid, loganin and products from in vitro reconstitution assays conducted with full-length Camptotheca His6-tagged CPR1. Integrated areas from LC-MS analyses of purified His6-tagged CYP72A proteins reconstituted with full-length His6-tagged Caa CPR1 are shown for no NADPH (gray) and plus NADPH (gray slashed) reactions.
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