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Ferric Quinate (QPLEX) inhibits the interaction of Major Outer Membrane Protein (MOMP) with the Lewis b (Leb) antigen and Limits Campylobacter colonisation in broilers (2023)
Journal Article
Okoye, J. C., Holland, A., Pitoulias, M., Paschalis, V., Piddubnyi, A., Dufailu, O. A., …Soultanos, P. (2023). Ferric Quinate (QPLEX) inhibits the interaction of Major Outer Membrane Protein (MOMP) with the Lewis b (Leb) antigen and Limits Campylobacter colonisation in broilers. Frontiers in Microbiology, 14, Article 1146418. https://doi.org/10.3389/fmicb.2023.1146418

Campylobacter jejuni colonizes hosts by interacting with Blood Group Antigens (BgAgs) on the surface of gastrointestinal epithelia. Genetic variations in BgAg expression affects host susceptibility to C. jejuni. Here, we show that the essential major... Read More about Ferric Quinate (QPLEX) inhibits the interaction of Major Outer Membrane Protein (MOMP) with the Lewis b (Leb) antigen and Limits Campylobacter colonisation in broilers.

Ferric quinate (QPLEX) inhibits the interaction of major outer membrane protein (MOMP) with the Lewis b (Leb) antigen and limits Campylobacter colonization in broilers (2023)
Journal Article
Okoye, J. C., Holland, A., Pitoulias, M., Paschalis, V., Piddubnyi, A., Dufailu, O. A., …Soultanas, P. (2023). Ferric quinate (QPLEX) inhibits the interaction of major outer membrane protein (MOMP) with the Lewis b (Leb) antigen and limits Campylobacter colonization in broilers. Frontiers in Microbiology, 14, Article 1146418. https://doi.org/10.3389/fmicb.2023.1146418

Campylobacter jejuni colonizes hosts by interacting with Blood Group Antigens (BgAgs) on the surface of gastrointestinal epithelia. Genetic variations in BgAg expression affects host susceptibility to C. jejuni. Here, we show that the essential major... Read More about Ferric quinate (QPLEX) inhibits the interaction of major outer membrane protein (MOMP) with the Lewis b (Leb) antigen and limits Campylobacter colonization in broilers.

Interaction of human HelQ with DNA polymerase delta halts DNA synthesis and stimulates DNA single-strand annealing (2023)
Journal Article
He, L., Lever, R., Cubbon, A., Tehseen, M., Jenkins, T., Nottingham, A. O., …Bolt, E. L. (2023). Interaction of human HelQ with DNA polymerase delta halts DNA synthesis and stimulates DNA single-strand annealing. Nucleic Acids Research, 51(4), 1740-1749. https://doi.org/10.1093/nar/gkad032

DNA strand breaks are repaired by DNA synthesis from an exposed DNA end paired with a homologous DNA template. DNA polymerase delta (Pol δ) catalyses DNA synthesis in multiple eukaryotic DNA break repair pathways but triggers genome instability unles... Read More about Interaction of human HelQ with DNA polymerase delta halts DNA synthesis and stimulates DNA single-strand annealing.

Ferric quinate (QPLEX) interacts with the major outer membrane protein (MOMP) of Campylobacter jejuni and enters through the porin channel into the periplasmic space (2022)
Journal Article
Okoye, J. C., Bellamy-Carter, J., Oldham, N. J., Oldfield, N. J., Mahdavi, J., & Soultanas, P. (2022). Ferric quinate (QPLEX) interacts with the major outer membrane protein (MOMP) of Campylobacter jejuni and enters through the porin channel into the periplasmic space. Computational and Structural Biotechnology Journal, 20, 5355-5363. https://doi.org/10.1016/j.csbj.2022.09.032

Ferric chelates like ferric tyrosinate (TYPLEX) and the closely related ferric quinate (QPLEX) are structural mimics of bacterial siderophores. TYPLEX has been trialled as a feed additive in farming of commercial broilers, reducing Campylobacter load... Read More about Ferric quinate (QPLEX) interacts with the major outer membrane protein (MOMP) of Campylobacter jejuni and enters through the porin channel into the periplasmic space.

The HelQ human DNA repair helicase utilizes a PWI-like domain for DNA loading through interaction with RPA, triggering DNA unwinding by the HelQ helicase core (2021)
Journal Article
Jenkins, T., Northall, S. J., Ptchelkine, D., Lever, R., Cubbon, A., Betts, H., …Bolt, E. L. (2021). The HelQ human DNA repair helicase utilizes a PWI-like domain for DNA loading through interaction with RPA, triggering DNA unwinding by the HelQ helicase core. NAR Cancer, 3(1), Article zcaa043. https://doi.org/10.1093/narcan/zcaa043

Genome instability is a characteristic enabling factor for carcinogenesis. HelQ helicase is a component of human DNA maintenance systems that prevent or reverse genome instability arising during DNA replication. Here, we provide details of the molecu... Read More about The HelQ human DNA repair helicase utilizes a PWI-like domain for DNA loading through interaction with RPA, triggering DNA unwinding by the HelQ helicase core.

DNA binding and unwinding by Hel308 helicase requires dual functions of a winged helix domain (2017)
Journal Article
Northall, S. J., Buckley, R., Jones, N., Penedo, J. C., Soultanas, P., & Bolt, E. L. (2017). DNA binding and unwinding by Hel308 helicase requires dual functions of a winged helix domain. DNA Repair, 57, https://doi.org/10.1016/j.dnarep.2017.07.005

Hel308 helicases promote genome stability linked to DNA replication in archaea, and have homologues in metazoans. In the crystal structure of archaeal Hel308 bound to a tailed DNA duplex, core helicase domains encircle single-stranded DNA (ssDNA) in... Read More about DNA binding and unwinding by Hel308 helicase requires dual functions of a winged helix domain.