scholarly journals On the occurrence of cytochrome P450 in viruses

2019 ◽  
Vol 116 (25) ◽  
pp. 12343-12352 ◽  
Author(s):  
David C. Lamb ◽  
Alec H. Follmer ◽  
Jared V. Goldstone ◽  
David R. Nelson ◽  
Andrew G. Warrilow ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Acanthamoeba Castellanii ◽  
Giant Virus ◽  
Gene Products ◽  
Cytochrome P450 Reductase ◽  
P450 Gene ◽  
Redox Partners ◽  
Genes Encoding ◽  
Giant Viruses ◽  
And Function

Genes encoding cytochrome P450 (CYP; P450) enzymes occur widely in the Archaea, Bacteria, and Eukarya, where they play important roles in metabolism of endogenous regulatory molecules and exogenous chemicals. We now report that genes for multiple and unique P450s occur commonly in giant viruses in the Mimiviridae, Pandoraviridae, and other families in the proposed order Megavirales. P450 genes were also identified in a herpesvirus (Ranid herpesvirus 3) and a phage (Mycobacterium phage Adler). The Adler phage P450 was classified as CYP102L1, and the crystal structure of the open form was solved at 2.5 Å. Genes encoding known redox partners for P450s (cytochrome P450 reductase, ferredoxin and ferredoxin reductase, and flavodoxin and flavodoxin reductase) were not found in any viral genome so far described, implying that host redox partners may drive viral P450 activities. Giant virus P450 proteins share no more than 25% identity with the P450 gene products we identified in Acanthamoeba castellanii, an amoeba host for many giant viruses. Thus, the origin of the unique P450 genes in giant viruses remains unknown. If giant virus P450 genes were acquired from a host, we suggest it could have been from an as yet unknown and possibly ancient host. These studies expand the horizon in the evolution and diversity of the enormously important P450 superfamily. Determining the origin and function of P450s in giant viruses may help to discern the origin of the giant viruses themselves.

scholarly journals Polyphenols as Food Supplement Improved Food Consumption and Longevity of Honey Bees (Apis mellifera) Intoxicated by Pesticide Thiacloprid

Insects ◽  
2021 ◽  
Vol 12 (7) ◽  
pp. 572
Author(s):  
Marian Hýbl ◽  
Petr Mráz ◽  
Jan Šipoš ◽  
Irena Hoštičková ◽  
Andrea Bohatá ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Food Consumption ◽  
Honey Bees ◽  
Food Supplement ◽  
Cytochrome P450 Enzyme ◽  
P450 Gene ◽  
Genes Encoding ◽  
The Impact ◽  
Bee Colonies

Malnutrition is one of the main problems related to the global mass collapse of honey bee colonies, because in honey bees, malnutrition is associated with deterioration of the immune system and increased pesticide susceptibility. Another important cause of mass bee colonies losses is the use of pesticides. Therefore, the goal of this study was to verify the influence of polyphenols on longevity, food consumption, and cytochrome P450 gene expression in worker bees intoxicated by thiacloprid. The tests were carried out in vitro under artificial conditions (caged bees). A conclusively lower mortality rate and, in parallel, a higher average food intake, were observed in intoxicated bees treated using a mixture of phenolic acids and flavonoids compared to untreated intoxicated bees. This was probably caused by increased detoxification capacity caused by increased expression level of genes encoding the cytochrome P450 enzyme in the bees. Therefore, the addition of polyphenols into bee nutrition is probably able to positively affect the detoxification capacity of bees, which is often reduced by the impact of malnutrition resulting from degradation of the environment and common beekeeping management.

scholarly journals Beta sheet 2–alpha helix C loop of cytochrome P450 reductase serves as a docking site for redox partners

2010 ◽  
Vol 1804 (6) ◽  
pp. 1285-1293 ◽  
Author(s):  
Hyun-Hee Jang ◽  
Arvind P. Jamakhandi ◽  
Shane Z. Sullivan ◽  
Chul-Ho Yun ◽  
Paul F. Hollenberg ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Alpha Helix ◽  
Docking Site ◽  
Cytochrome P450 Reductase ◽  
Beta Sheet ◽  
P450 Reductase ◽  
Redox Partners

scholarly journals In-depth study of Mollivirus sibericum, a new 30,000-y-old giant virus infecting Acanthamoeba

2015 ◽  
Vol 112 (38) ◽  
pp. E5327-E5335 ◽  
Author(s):  
Matthieu Legendre ◽  
Audrey Lartigue ◽  
Lionel Bertaux ◽  
Sandra Jeudy ◽  
Julia Bartoli ◽  
...  
Keyword(s):  
Global Warming ◽  
Gene Transfer ◽  
Horizontal Gene Transfer ◽  
Ribosomal Proteins ◽  
Acanthamoeba Castellanii ◽  
Giant Virus ◽  
Metagenomic Analysis ◽  
Dna Viruses ◽  
Depth Study ◽  
Giant Viruses

Acanthamoeba species are infected by the largest known DNA viruses. These include icosahedral Mimiviruses, amphora-shaped Pandoraviruses, and Pithovirus sibericum, the latter one isolated from 30,000-y-old permafrost. Mollivirus sibericum, a fourth type of giant virus, was isolated from the same permafrost sample. Its approximately spherical virion (0.6-µm diameter) encloses a 651-kb GC-rich genome encoding 523 proteins of which 64% are ORFans; 16% have their closest homolog in Pandoraviruses and 10% in Acanthamoeba castellanii probably through horizontal gene transfer. The Mollivirus nucleocytoplasmic replication cycle was analyzed using a combination of “omic” approaches that revealed how the virus highjacks its host machinery to actively replicate. Surprisingly, the host’s ribosomal proteins are packaged in the virion. Metagenomic analysis of the permafrost sample uncovered the presence of both viruses, yet in very low amount. The fact that two different viruses retain their infectivity in prehistorical permafrost layers should be of concern in a context of global warming. Giant viruses’ diversity remains to be fully explored.

scholarly journals Probing the Role of the Hinge Segment of Cytochrome P450 Oxidoreductase in the Interaction with Cytochrome P450

2018 ◽  
Vol 19 (12) ◽  
pp. 3914 ◽  
Author(s):  
Diana Campelo ◽  
Francisco Esteves ◽  
Bernardo Brito Palma ◽  
Bruno Costa Gomes ◽  
José Rueff ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Cytochrome B5 ◽  
Cytochrome P450s ◽  
Cytochrome P450 Reductase ◽  
Redox Partner ◽  
Redox Partners ◽  
Cytochrome P450 Oxidoreductase ◽  
Experimental Approaches ◽  
Menten Kinetic

NADPH-cytochrome P450 reductase (CPR) is the unique redox partner of microsomal cytochrome P450s (CYPs). CPR exists in a conformational equilibrium between open and closed conformations throughout its electron transfer (ET) function. Previously, we have shown that electrostatic and flexibility properties of the hinge segment of CPR are critical for ET. Three mutants of human CPR were studied (S243P, I245P and R246A) and combined with representative human drug-metabolizing CYPs (isoforms 1A2, 2A6 and 3A4). To probe the effect of these hinge mutations different experimental approaches were employed: CYP bioactivation capacity of pre-carcinogens, enzyme kinetic analysis, and effect of the ionic strength and cytochrome b5 (CYB5) on CYP activity. The hinge mutations influenced the bioactivation of pre-carcinogens, which seemed CYP isoform and substrate dependent. The deviations of Michaelis-Menten kinetic parameters uncovered tend to confirm this discrepancy, which was confirmed by CYP and hinge mutant specific salt/activity profiles. CPR/CYB5 competition experiments indicated a less important role of affinity in CPR/CYP interaction. Overall, our data suggest that the highly flexible hinge of CPR is responsible for the existence of a conformational aggregate of different open CPR conformers enabling ET-interaction with structural varied redox partners.

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