Rapid Biodegradation of the Herbicide 2,4-Dichlorophenoxyacetic Acid by <i>Cupriavidus gilardii</i> T-1

Wu, Xiangwei; Wang, Wenbo; Liu, Junwei; Pan, Dandan; Tu, Xiao-Hui; Lv, Pei; Wang, Yi; Cao, Haiqun; Wang, Yawen; Hua, Rimao

doi:10.1021/acs.jafc.7b00544

Cited by 49 publications

(30 citation statements)

References 45 publications

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“…Since then, C. gilardii has been isolated from multiple ecological niches, including untreated drinking water (5), urban pond water (6), agricultural soil (7), soil contaminated with heavy metals (8), soil containing natural asphalt (9), plants (10), and human clinical samples (11–17). At the environmental and biotechnological levels, this organism has gained attention because of its potential role as an indicator of heavy metal contamination (8), as well as its ability to degrade herbicides (7) and other toxic hydrocarbons, such as naphthenic acids (9).…”

Section: Introductionmentioning

confidence: 99%

Comparative Genomics Reveals a Well-Conserved Intrinsic Resistome in the Emerging Multidrug-Resistant Pathogen Cupriavidus gilardii

Ruiz

McCarley

Espejo

et al. 2019

mSphere

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The Gram-negative bacterium Cupriavidus gilardii is an emerging multidrug-resistant pathogen found in many environments. However, little is known about this species or its antibiotic resistance mechanisms. We used biochemical tests, antibiotic susceptibility experiments, and whole-genome sequencing to characterize an environmental C. gilardii isolate. Like clinical isolates, this isolate was resistant to meropenem, gentamicin, and other antibiotics. Resistance to these antibiotics appeared to be related to the large number of intrinsic antibiotic resistance genes found in this isolate. As determined by comparative genomics, this resistome was also well conserved in the only two other C. gilardii strains sequenced to date. The intrinsic resistome of C. gilardii did not include the colistin resistance gene mcr-5, which was in a transposon present only in one strain. The intrinsic resistome of C. gilardii was comprised of (i) many multidrug efflux pumps, such as a homolog of the Pseudomonas aeruginosa MexAB-OprM pump that may be involved in resistance to meropenem, other β-lactams, and aminoglycosides; (ii) a novel β-lactamase (OXA-837) that decreases susceptibility to ampicillin but not to other β-lactams tested; (iii) a new aminoglycoside 3-N-acetyltransferase [AAC(3)-IVb, AacC10] that decreases susceptibility to gentamicin and tobramycin; and (iv) a novel partially conserved aminoglycoside 3ʺ-adenylyltransferase [ANT(3ʺ)-Ib, AadA32] that decreases susceptibility to spectinomycin and streptomycin. These findings provide the first mechanistic insight into the intrinsic resistance of C. gilardii to multiple antibiotics and its ability to become resistant to an increasing number of drugs during therapy. IMPORTANCE Cupriavidus gilardii is a bacterium that is gaining increasing attention both as an infectious agent and because of its potential use in the detoxification of toxic compounds and other biotechnological applications. In recent years, however, there has been an increasing number of reported infections, some of them fatal, caused by C. gilardii. These infections are hard to treat because this bacterium is naturally resistant to many antibiotics, including last-resort antibiotics, such as carbapenems. Moreover, this bacterium often becomes resistant to additional antibiotics during therapy. However, little is known about C. gilardii and its antibiotic resistance mechanisms. The significance of our research is in providing, for the first time, whole-genome information about the natural antibiotic resistance genes found in this bacterium and their conservation among different C. gilardii strains. This information may provide new insights into the appropriate use of antibiotics in combating infections caused by this emerging pathogen.

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Section: Introductionmentioning

confidence: 99%

Comparative Genomics Reveals a Well-Conserved Intrinsic Resistome in the Emerging Multidrug-Resistant Pathogen Cupriavidus gilardii

Ruiz

McCarley

Espejo

et al. 2019

mSphere

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“…However, only a few of these methods conform to the Food and Agriculture Organization’s (FAO) requirement that the reduction of AFB1 is achieved while maintaining the nutritional value without residual toxicity or modifying the food or feed properties [6,7]. Biological degradation has proven to be an efficient, safe, and feasible method for AFB1 removal because its raw materials are non-polluting, highly specific, mild, and environmentally friendly; this process also discourages toxin regeneration [8,9,10].…”

Section: Introductionmentioning

confidence: 99%

Effective Biodegradation of Aflatoxin B1 Using the Bacillus licheniformis (BL010) Strain

Wang

Zhang

Yan

et al. 2018

Toxins

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Aflatoxin B1 (AFB1), a pollutant of agricultural products, has attracted considerable attention in recent years, due to its potential impact on health. In the present study, Bacillus licheniformis (BL010) was demonstrated to efficiently degrade AFB1, reducing over 89.1% of the toxin content within 120 h. A crude enzyme solution of BL010 exhibited the highest degradation level (97.3%) after three induction periods. However, uninduced BL010 bacteria was not capable of reducing AFB1. Furthermore, high performance liquid chromatography (HPLC) analysis showed that while a cell-free extract caused a significant decrease in AFB1 content (93.6%, p < 0.05), cell culture fluid treatment did not significantly degrade AFB1. The biotransformation products of AFB1 were detected and further identified by quadrupole time-of-flight liquid chromatography–mass spectrometry (LC-Q-TOF/MS); these corresponded to a molecular formula of C12H14O4. A sequence analysis of whole BL010 genes with a bioinformatics approach identified the secondary structures of two degrading enzymes (Chia010 and Lac010), providing an important basis for subsequent homology modeling and functional predictions.

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“…Until now, most of the reports describing microbial degradation of 2,4-D with the involvement of particular enzymes have concerned bacterial activity. Cupriavidus gilardii T-1 degraded 2,4-D to 2,4-DCP by a cleavage of the ether bond and then into 3,5-dichlorocatechol via hydroxylation, followed by ortho-cleavage to form cis-2-dichlorodiene lactone (Wu et al 2017 ). The compound 2,4-D was degraded by the following fungal strains: Cunninghamella elegans , C. echinulata , Rhizoctonia solani , Verticillium lecanii , Penicillium chrysogenum , Aspergillus penicillioides , Eupenicillium sp .…”

Section: Discussionmentioning

confidence: 99%

Elimination and detoxification of 2,4-D by Umbelopsis isabellina with the involvement of cytochrome P450

Nykiel-Szymańska

Stolarek

Bernat

2017

Environ Sci Pollut Res

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The chemical 2,4-dichlorophenoxyacetic acid (2,4-D) is used in agriculture as a herbicide. Its intensive use has an adverse effect on the environment. This study involved examining the degradation of 2,4-D compound by the filamentous fungus Umbelopsis isabellina. After 5 days of incubation, 98% of the herbicide (added at 25 mg L−1) was found to be removed. The elimination of 2,4-D by U. isabellina was connected with the formation of 2,4-dichlorophenol (2,4-DCP), which resulted in a 60% decrease in the sample toxicity toward Artemia franciscana larvae. The metabolism of 2,4-D was inhibited by the addition of metyrapone, a known cytochrome P450 inhibitor. It provides evidence that cytochrome P450 system is involved in 2,4-D metabolism in U. isabellina.

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Rapid Biodegradation of the Herbicide 2,4-Dichlorophenoxyacetic Acid by Cupriavidus gilardii T-1

Cited by 49 publications

References 45 publications

Comparative Genomics Reveals a Well-Conserved Intrinsic Resistome in the Emerging Multidrug-Resistant Pathogen Cupriavidus gilardii

Comparative Genomics Reveals a Well-Conserved Intrinsic Resistome in the Emerging Multidrug-Resistant Pathogen Cupriavidus gilardii

Effective Biodegradation of Aflatoxin B1 Using the Bacillus licheniformis (BL010) Strain

Elimination and detoxification of 2,4-D by Umbelopsis isabellina with the involvement of cytochrome P450

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