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174 results on '"Loveridge, E. Joel"'

1. Identification of the odorant binding proteins of Western Flower Thrips ( Frankliniella occidentalis ), characterization and binding analysis of FoccOBP3 with molecular modelling, molecular dynamics simulations and a confirmatory field trial

Author

Zafar, Zeeshan, primary, Wood, Martyn J., additional, Fatima, Sidra, additional, Bhatti, Muhammad Faraz, additional, Shah, Farooq A., additional, Saud, Zack, additional, Loveridge, E. Joel, additional, Karaca, Ismail, additional, and Butt, Tariq M., additional

Published
2024
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2. A residue-free approach to water disinfection using catalytic in situ generation of reactive oxygen species

Author

Richards, Thomas, Harrhy, Jonathan H., Lewis, Richard J., Howe, Alexander G. R., Suldecki, Grzegorz M., Folli, Andrea, Morgan, David J., Davies, Thomas E., Loveridge, E. Joel, Crole, David A., Edwards, Jennifer K., Gaskin, Paul, Kiely, Christopher J., He, Qian, Murphy, Damien M., Maillard, Jean-Yves, Freakley, Simon J., and Hutchings, Graham J.

Published
2021
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4. Evaluation of Metarhizium brunneum- and Metarhizium-Derived VOCs as Dual-Active Biostimulants and Pest Repellents in a Wireworm-Infested Potato Field

Author

Wood, Martyn J., primary, Kortsinoglou, Alexandra M., additional, Bull, James C., additional, Eastwood, Daniel C., additional, Kouvelis, Vassili N., additional, Bourdon, Pierre A., additional, Loveridge, E. Joel, additional, Mathias, Stephen, additional, Meyrick, Abigail, additional, Midthassel, Audun, additional, Myrta, Arben, additional, and Butt, Tariq, additional

Published
2023
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13. Fungal bioremediation of polyethylene: Challenges and perspectives.

Author

Cowan, Andrew R., Costanzo, Chiara M., Benham, Robert, Loveridge, E. Joel, and Moody, Suzy C.

Subjects
FUNGAL remediation, POLLUTANTS, POLYETHYLENE, PLASTIC scrap, WASTE recycling, PLASTICS, MARINE debris
Abstract

Plastics have become ubiquitous in both their adoption as materials and as environmental contaminants. Widespread pollution of these versatile, man‐made and largely petroleum‐derived polymers has resulted from their long‐term mass production, inappropriate disposal and inadequate end of life management. Polyethylene (PE) is at the forefront of this problem, accounting for one‐third of plastic demand in Europe in part due to its extensive use in packaging. Current recycling and incineration processes do not represent sustainable solutions to tackle plastic waste, especially once it becomes littered, and the development of new waste‐management and remediation technologies are needed. Mycoremediation (fungal‐based biodegradation) of PE has been the topic of several studies over the last two decades. The utility of these studies is limited by an inconclusive definition of biodegradation and a lack of knowledge regarding the biological systems responsible. This review highlights relevant features of fungi as potential bioremediation agents, before discussing the evidence for fungal biodegradation of both high‐ and low‐density PE. An up‐to‐date perspective on mycoremediation as a future solution to PE waste is provided. [ABSTRACT FROM AUTHOR]

Published
2022
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15. TCR-induced alteration of primary MHC peptide anchor residue

Author

Madura, Florian, Rizkallah, Pierre J., Legut, Mateusz, Holland, Christopher J., Fuller, Anna, Bulek, Anna, Schauenburg, Andrea J., Trimby, Andrew, Hopkins, Jade R., Wells, Stephen A., Godkin, Andrew, Miles, John J., Sami, Malkit, Li, Yi, Liddy, Nathaniel, Jakobsen, Bent K., Loveridge, E. Joel, Cole, David K., and Sewell, Andrew K.

Abstract

The HLA‐A*02:01‐restricted decapeptide EAAGIGILTV, derived from melanoma antigen recognized by T‐cells‐1 (MART‐1) protein, represents one of the best‐studied tumor associated T‐cell epitopes, but clinical results targeting this peptide have been disappointing. This limitation may reflect the dominance of the nonapeptide, AAGIGILTV, at the melanoma cell surface. The decapeptide and nonapeptide are presented in distinct conformations by HLA‐A*02:01 and TCRs from clinically relevant T‐cell clones recognize the nonapeptide poorly. Here, we studied the MEL5 TCR that potently recognizes the nonapeptide. The structure of the MEL5‐HLA‐A*02:01‐AAGIGILTV complex revealed an induced fit mechanism of antigen recognition involving altered peptide–MHC anchoring. This “flexing” at the TCR–peptide–MHC interface to accommodate the peptide antigen explains previously observed incongruences in this well‐studied system and has important implications for future therapeutic approaches. Finally, this study expands upon the mechanisms by which molecular plasticity can influence antigen recognition by T cells.

Published
2019

16. Reclassification of the specialized metabolite producer Pseudomonas mesoacidophila ATCC 31433 as a member of the Burkholderia cepacia complex

Author

Loveridge, E Joel, Jones, Cerith, Bull, Matthew J, Moody, Suzy C, Kahl, Małgorzata W, Khan, Zainab, Neilson, Louis, Tomeva, Marina, Adams, Sarah E, Wood, Andrew C, Rodriguez-Martin, Daniel, Pinel, Ingrid, Parkhill, Julian, Mahenthiralingam, Eshwar, Crosby, John, Loveridge, E Joel [0000-0002-8528-4019], Jones, Cerith [0000-0001-6275-0235], Parkhill, Julian [0000-0002-7069-5958], Mahenthiralingam, Eshwar [0000-0001-9014-3790], and Apollo - University of Cambridge Repository

Subjects
DNA, Bacterial, Identification, Genome, antibiotic resistance, Antibiotic resistance, Bulgecin, Burkholderia cepacia complex, Gene Expression Regulation, Bacterial, Q1, Biosynthesis, Anti-Bacterial Agents, Antibacterial, Metal resistance, antibacterial, Pseudomonas, Drug Resistance, Bacterial, identification, bulgecin, biosynthesis, genome, metal resistance, biological, Genome, Bacterial, Phylogeny
Abstract

Pseudomonas mesoacidophila ATCC 31433 is a Gram-negative bacterium, first isolated from Japanese soil samples, that produces the monobactam isosulfazecin and the β-lactam-potentiating bulgecins. To characterize the biosynthetic potential of P. mesoacidophila ATCC 31433, its complete genome was determined using single-molecule real-time DNA sequence analysis. The 7.8-Mb genome comprised four replicons, three chromosomal (each encoding rRNA) and one plasmid. Phylogenetic analysis demonstrated that P. mesoacidophila ATCC 31433 was misclassified at the time of its deposition and is a member of the Burkholderia cepacia complex, most closely related to Burkholderia ubonensis The sequenced genome shows considerable additional biosynthetic potential; known gene clusters for malleilactone, ornibactin, isosulfazecin, alkylhydroxyquinoline, and pyrrolnitrin biosynthesis and several uncharacterized biosynthetic gene clusters for polyketides, nonribosomal peptides, and other metabolites were identified. Furthermore, P. mesoacidophila ATCC 31433 harbors many genes associated with environmental resilience and antibiotic resistance and was resistant to a range of antibiotics and metal ions. In summary, this bioactive strain should be designated B. cepacia complex strain ATCC 31433, pending further detailed taxonomic characterization.IMPORTANCE This work reports the complete genome sequence of Pseudomonas mesoacidophila ATCC 31433, a known producer of bioactive compounds. Large numbers of both known and novel biosynthetic gene clusters were identified, indicating that P. mesoacidophila ATCC 31433 is an untapped resource for discovery of novel bioactive compounds. Phylogenetic analysis demonstrated that P. mesoacidophila ATCC 31433 is in fact a member of the Burkholderia cepacia complex, most closely related to the species Burkholderia ubonensis Further investigation of the classification and biosynthetic potential of P. mesoacidophila ATCC 31433 is warranted.

Published
2017

17. Chemoenzymatic assembly of isotopically labeled folates

Author

Angelastro, Antonio, Dawson, William M., Luk, Louis Y.P., Loveridge, E. Joel, and Allemann, Rudolf K.

Abstract

Pterin-containing natural products have diverse functions in life, but an efficient and easy scheme for their in vitro synthesis is not available. Here we report a chemoenzymatic 14-step, one-pot synthesis that can be used to generate 13C- and 15N-labeled dihydrofolates (H2F) from glucose, guanine, and p-aminobenzoyl-l-glutamic acid. This synthesis stands out from previous approaches to produce H2F in that the average yield of each step is >91% and it requires only a single purification step. The use of a one-pot reaction allowed us to overcome potential problems with individual steps during the synthesis. The availability of labeled dihydrofolates allowed the measurement of heavy-atom isotope effects for the reaction catalyzed by the drug target dihydrofolate reductase and established that protonation at N5 of H2F and hydride transfer to C6 occur in a stepwise mechanism. This chemoenzymatic pterin synthesis can be applied to the efficient production of other folates and a range of other natural compounds with applications in nutritional, medical, and cell-biological research.

Published
2017

18. The temperature dependence of the kinetic isotope effects of dihydrofolate reductase from Thermotoga maritima is influenced by intersubunit interactions

Author

Loveridge, E. Joel and Allemann, Rudolf K.

Subjects
Dihydrofolate reductase -- Research, Chemical reaction, Rate of -- Research, Biological sciences, Chemistry
Abstract

The role of the salt bridges in the dimerization and thermal stability of dihydrofolate reductase from the hyperthermophile Thermotoga maritima (TmDHFR) is studied by generating a series of variants in which the residues are exchanged for residues whose side chains bear the opposite charge. The results have shown that although the rate of dihydrofolate reduction by TmDHFR is not affected by the loss of the K129-E136-E138 salt bridges, changes to the temperature dependence of the kinetic isotope effect on hydride transfer are observed.

Published
2010

19. Solvent effects on catalysis by Escherichia coli dihydrofolate reductase

Author

Loveridge, E. Joel, Tey, Lai-Hock, and Allemann, Rudolf K.

Subjects
Chemical reaction, Rate of -- Analysis, Escherichia coli -- Physiological aspects, Solvation -- Analysis, Dihydrofolate reductase -- Chemical properties, Chemistry
Abstract

The article discusses the mechanisms, as well as the kinetics associated with the reaction catalyzed by dihydrofolate reductase obtained from Escherichia coli. The various effects of solvent composition on the temperature dependency of the various kinetic parameters are also explained.

Published
2010

20. Effect of dimerization on the stability and catalytic activity of dihydrofolate reductase from the hyperthermophile Thermotoga maritima

Author

Loveridge, E. Joel, Rodriguez, Robert J., Swanwick, Richard S., and Allemann, Rudolf K.

Subjects
Amino acids -- Chemical properties, Amino acids -- Structure, Hyperthermophiles -- Research, Dihydrofolate reductase -- Research, Biological sciences, Chemistry
Abstract

The generation of a variant of dihydrofolate reductase (DHFR) from Thermotoga maritima, TmDHFR-V11D, in which a single amino acid replacement is sufficient to favor the monomeric form of the enzyme in the presence of the nondenaturing zwitterionic detergent 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate is reported. The reduced catalytic activity of TmDHFR relative to the monomeric Escherichia coli enzyme is not caused by rigidity resulting from dimerization, but is a subtle consequence of the sequence and structure of its subunits, which appear to have evolved to permit thermostability at the expense of catalysis.

Published
2009

21. Different reaction mechanisms for mesophilic and thermophilic dihydrofolate reductases

Author

Loveridge, E. Joel, Behiry, Enas M., Swanwick, Richard S., and Allemann, Rudolf K.

Subjects
Escherichia coli -- Physiological aspects, Isotopes -- Chemical properties, Oxidoreductases -- Chemical properties, Oxidoreductases -- Structure, Chemistry
Abstract

Solvent kinetic isotope effects are described for two dihydrofolate reductases, namely the monomers, mesophilic enzymes from Escherichia coli (EcDHFR) and the dimeric, thermophilic enzyme from Thermotoga maritime (TmDHFR). The reduced reaction rates of TmDHFR is due to its quaternary structure, which is needed for increased thermostability but which also prevents active modulation of the reactivity of the active site bound substrate observed in EcDHFR.

Published
2009

24. CYP105-diverse structures, functions and roles in an intriguing family of enzymes in 'Streptomyces'

Author

Moody, Suzy C and Loveridge, E Joel

Subjects
biological
Abstract

The cytochromes P450 (CYP or P450) are a large superfamily of haem-containing enzymes found in all domains of life. They catalyse a variety of complex reactions, predominantly mixed-function oxidations, often displaying highly regio- and/or stereospecific chemistry. In streptomycetes, they are predominantly associated with secondary metabolite biosynthetic pathways or with xenobiotic catabolism. Homologues of one family, CYP105, have been found in all Streptomyces species thus far sequenced. This review looks at the diverse biological functions of CYP105s and the biosynthetic/catabolic pathways they are associated with. Examples are presented showing a range of biotransformative abilities and different contexts. As biocatalysts capable of some remarkable chemistry, CYP105s have great biotechnological potential and merit detailed study. Recent developments in biotechnological applications which utilize CYP105s are described, alongside a brief overview of the benefits and drawbacks of using P450s in commercial applications. The role of CYP105s in vivo is in many cases undefined and provides a rich source for further investigation into the functions these enzymes fulfil and the metabolic pathways they participate in, in the natural environment.

Published
2014

39. Aliphatic 1H, 13C and 15N chemical shift assignments of dihydrofolate reductase from the psychropiezophile Moritella profunda in complex with NADP+ and folate

Author

Loveridge, E. Joel, primary, Matthews, Stella M., additional, Williams, Christopher, additional, Whittaker, Sara B.-M., additional, Günther, Ulrich L., additional, Evans, Rhiannon M., additional, Dawson, William M., additional, Crump, Matthew P., additional, and Allemann, Rudolf K., additional

Published
2012
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41. The Role of Large-Scale Motions in Catalysis by Dihydrofolate Reductase

Author

Loveridge, E. Joel, primary, Tey, Lai-Hock, additional, Behiry, Enas M., additional, Dawson, William M., additional, Evans, Rhiannon M., additional, Whittaker, Sara B.-M., additional, Günther, Ulrich L., additional, Williams, Christopher, additional, Crump, Matthew P., additional, and Allemann, Rudolf K., additional

Published
2011
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