Cytochrome P450 monooxygenase genes in the wild silkworm, Bombyx mandarina

Wild (Bombyx mandarina) and domestic silkworms (B. mori) are good models for investigating insect domestication, as 5000 years of artificial breeding and selection have resulted in significant differences between B. mandarina and B. mori. In this study, we improved the genome assemblies to the chromosome level and updated the protein-coding gene annotations for B. mandarina. Based on this updated genome, we identified 68 cytochrome P450 genes in B. mandarina. The cytochrome P450 repository in B. mandarina is smaller than in B. mori. Certain currently unknown key genes, rather than gene number, are critical for insecticide resistance in B. mandarina, which shows greater resistance to insecticides than B. mori. Based on the physical maps of B. mandarina, we located 66 cytochrome P450s on 18 different chromosomes, and 27 of the cytochrome P450 genes were concentrated into seven clusters. KEGG enrichment analysis of the P450 genes revealed the involvement of cytochrome P450 genes in hormone biosynthesis. Analyses of the silk gland transcriptome identified candidate cytochrome P450 genes (CYP306A) involved in ecdysteroidogenesis and insecticide metabolism in B. mandarina.

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Molecular evolution of a cytochrome P450 for the synthesis of potential antidepressant (2R,6R)-hydroxynorketamine

Chemical Communications ◽

10.1039/d0cc06729f ◽

2021 ◽

Author(s):

Ansgar Bokel ◽

Michael C. Hutter ◽

Vlada B. Urlacher

Keyword(s):

Cytochrome P450 ◽

Molecular Evolution ◽

Cytochrome P450 Monooxygenase ◽

P450 Monooxygenase ◽

Effective Synthesis

Engineered cytochrome P450 monooxygenase CYP154E1 enables the effective synthesis of the potential antidepressant (2R,6R)-hydroxynorketamine via N-demethylation and regio- and stereoselective hydroxylation of (R)-ketamine.

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Genomic and transcriptomic insights into the cytochrome P450 monooxygenase gene repertoire in the rice pest brown planthopper,Nilaparvata lugens

10.1603/ice.2016.108969 ◽

2016 ◽

Author(s):

Yanyuan Bao

Keyword(s):

Cytochrome P450 ◽

Brown Planthopper ◽

Nilaparvata Lugens ◽

Cytochrome P450 Monooxygenase ◽

Gene Repertoire ◽

P450 Monooxygenase ◽

Monooxygenase Gene ◽

Rice Pest

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First Time Ever: Cytochrome P450 Genes Discovered in Virus

Microbe Magazine ◽

10.1128/microbe.4.421.1 ◽

2009 ◽

Vol 4 (9) ◽

pp. 421-421

Keyword(s):

Cytochrome P450 ◽

Cytochrome P450 Genes ◽

First Time

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Escalation of Pyrethroid Resistance in the Malaria Vector Anopheles funestus Induces a Loss of Efficacy of Piperonyl Butoxide–Based Insecticide-Treated Nets in Mozambique

The Journal of Infectious Diseases ◽

10.1093/infdis/jiz139 ◽

2019 ◽

Vol 220 (3) ◽

pp. 467-475 ◽

Cited By ~ 16

Author(s):

Jacob M Riveron ◽

Silvie Huijben ◽

Williams Tchapga ◽

Magellan Tchouakui ◽

Murielle J Wondji ◽

...

Keyword(s):

Cytochrome P450 ◽

Pyrethroid Resistance ◽

Anopheles Funestus ◽

Resistance Mechanisms ◽

Piperonyl Butoxide ◽

Insecticide Treated Nets ◽

Molecular Analyses ◽

Cytochrome P450 Genes ◽

High Degree ◽

Long Lasting Insecticidal Nets

Abstract Background Insecticide resistance poses a serious threat to insecticide-based interventions in Africa. There is a fear that resistance escalation could jeopardize malaria control efforts. Monitoring of cases of aggravation of resistance intensity and its impact on the efficacy of control tools is crucial to predict consequences of resistance. Methods The resistance levels of an Anopheles funestus population from Palmeira, southern Mozambique, were characterized and their impact on the efficacy of various insecticide-treated nets established. Results A dramatic loss of efficacy of all long-lasting insecticidal nets (LLINs), including piperonyl butoxide (PBO)–based nets (Olyset Plus), was observed. This An. funestus population consistently (2016, 2017, and 2018) exhibited a high degree of pyrethroid resistance. Molecular analyses revealed that this resistance escalation was associated with a massive overexpression of the duplicated cytochrome P450 genes CYP6P9a and CYP6P9b, and also the fixation of the resistance CYP6P9a_R allele in this population in 2016 (100%) in contrast to 2002 (5%). However, the low recovery of susceptibility after PBO synergist assay suggests that other resistance mechanisms could be involved. Conclusions The loss of efficacy of pyrethroid-based LLINs with and without PBO is a concern for the effectiveness of insecticide-based interventions, and action should be taken to prevent the spread of such super-resistance.

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Cytochrome P450 Monooxygenase-Mediated Metabolic Utilization of Benzo[a]Pyrene by Aspergillus Species

mBio ◽

10.1128/mbio.00558-19 ◽

2019 ◽

Vol 10 (3) ◽

Cited By ~ 3

Author(s):

Erin M. Ostrem Loss ◽

Mi-Kyung Lee ◽

Ming-Yueh Wu ◽

Julia Martien ◽

Wanping Chen ◽

...

Keyword(s):

Cytochrome P450 ◽

Environmental Pollutants ◽

Energy Generation ◽

Fungal Species ◽

Metabolic Changes ◽

Cytochrome P450 Monooxygenase ◽

Cellular Growth ◽

P450 Monooxygenase ◽

Content Type ◽

Fundamental Knowledge

ABSTRACT Soil-dwelling fungal species possess the versatile metabolic capability to degrade complex organic compounds that are toxic to humans, yet the mechanisms they employ remain largely unknown. Benzo[a]pyrene (BaP) is a pervasive carcinogenic contaminant, posing a significant concern for human health. Here, we report that several Aspergillus species are capable of degrading BaP. Exposing Aspergillus nidulans cells to BaP results in transcriptomic and metabolic changes associated with cellular growth and energy generation, implying that the fungus utilizes BaP as a growth substrate. Importantly, we identify and characterize the conserved bapA gene encoding a cytochrome P450 monooxygenase that is necessary for the metabolic utilization of BaP in Aspergillus. We further demonstrate that the fungal NF-κB-type velvet regulators VeA and VelB are required for proper expression of bapA in response to nutrient limitation and BaP degradation in A. nidulans. Our study illuminates fundamental knowledge of fungal BaP metabolism and provides novel insights into enhancing bioremediation potential. IMPORTANCE We are increasingly exposed to environmental pollutants, including the carcinogen benzo[a]pyrene (BaP), which has prompted extensive research into human metabolism of toxicants. However, little is known about metabolic mechanisms employed by fungi that are able to use some toxic pollutants as the substrates for growth, leaving innocuous by-products. This study systemically demonstrates that a common soil-dwelling fungus is able to use benzo[a]pyrene as food, which results in expression and metabolic changes associated with growth and energy generation. Importantly, this study reveals key components of the metabolic utilization of BaP, notably a cytochrome P450 monooxygenase and the fungal NF-κB-type transcriptional regulators. Our study advances fundamental knowledge of fungal BaP metabolism and provides novel insight into designing and implementing enhanced bioremediation strategies.

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Chromosomal assembly of the nuclear genome of the endosymbiont-bearing trypanosomatid Angomonas deanei

G3 Genes|Genome|Genetics ◽

10.1093/g3journal/jkaa018 ◽

2021 ◽

Vol 11 (1) ◽

Author(s):

John W Davey ◽

Carolina M C Catta-Preta ◽

Sally James ◽

Sarah Forrester ◽

Maria Cristina M Motta ◽

...

Keyword(s):

Chromosome Number ◽

Noncoding Rnas ◽

Nuclear Genome ◽

Supernumerary Chromosome ◽

Ribosomal Rnas ◽

Protein Coding ◽

Transfer Rnas ◽

Protein Coding Genes ◽

Oxford Nanopore ◽

Genome Assemblies

Abstract Angomonas deanei is an endosymbiont-bearing trypanosomatid with several highly fragmented genome assemblies and unknown chromosome number. We present an assembly of the A. deanei nuclear genome based on Oxford Nanopore sequence that resolves into 29 complete or close-to-complete chromosomes. The assembly has several previously unknown special features; it has a supernumerary chromosome, a chromosome with a 340-kb inversion, and there is a translocation between two chromosomes. We also present an updated annotation of the chromosomal genome with 10,365 protein-coding genes, 59 transfer RNAs, 26 ribosomal RNAs, and 62 noncoding RNAs.

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In Silico Structural Modeling and Analysis of Interactions of Tremellomycetes Cytochrome P450 Monooxygenases CYP51s with Substrates and Azoles

International Journal of Molecular Sciences ◽

10.3390/ijms22157811 ◽

2021 ◽

Vol 22 (15) ◽

pp. 7811

Author(s):

Olufunmilayo Olukemi Akapo ◽

Joanna M. Macnar ◽

Justyna D. Kryś ◽

Puleng Rosinah Syed ◽

Khajamohiddin Syed ◽

...

Keyword(s):

Cytochrome P450 ◽

Structural Analysis ◽

In Silico ◽

Web Application ◽

Cytochrome P450 Monooxygenases ◽

Agglomerative Clustering ◽

Ligand Complex ◽

P450 Monooxygenase ◽

Study Results

Cytochrome P450 monooxygenase CYP51 (sterol 14α-demethylase) is a well-known target of the azole drug fluconazole for treating cryptococcosis, a life-threatening fungal infection in immune-compromised patients in poor countries. Studies indicate that mutations in CYP51 confer fluconazole resistance on cryptococcal species. Despite the importance of CYP51 in these species, few studies on the structural analysis of CYP51 and its interactions with different azole drugs have been reported. We therefore performed in silico structural analysis of 11 CYP51s from cryptococcal species and other Tremellomycetes. Interactions of 11 CYP51s with nine ligands (three substrates and six azoles) performed by Rosetta docking using 10,000 combinations for each of the CYP51-ligand complex (11 CYP51s × 9 ligands = 99 complexes) and hierarchical agglomerative clustering were used for selecting the complexes. A web application for visualization of CYP51s’ interactions with ligands was developed (http://bioshell.pl/azoledocking/). The study results indicated that Tremellomycetes CYP51s have a high preference for itraconazole, corroborating the in vitro effectiveness of itraconazole compared to fluconazole. Amino acids interacting with different ligands were found to be conserved across CYP51s, indicating that the procedure employed in this study is accurate and can be automated for studying P450-ligand interactions to cater for the growing number of P450s.

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