Tools
Tools
Rose, Clair 
ORCID: https://orcid.org/0000-0001-7782-5359, Praulins, Giorgi, Armstrong, Stuart D., Casas-Sanchez, Aitor ORCID: https://orcid.org/0000-0001-5237-1223, Davis, Jem, Molyneux, Gemma, YuntaYanes, Cristina, Stead, Zenaida, Prescott, Mark, Perally, Samirah, Rutter, Anne, Makepeace, Benjamin L., LaCourse, James ORCID: https://orcid.org/0000-0001-9261-7136 and Acosta Serrano, Alvaro ORCID: https://orcid.org/0000-0002-2576-7959
(2019)
'Characterisation of a novel glycosylated glutathione transferase of Onchocerca ochengi, closest relative of the human river blindness parasite'. Parasitology, Vol 146, Issue 14, pp. 1773-1784.
|
Text
characterisation_of_a_novel_glycosylated_glutathione_transferase_accepted.pdf - Accepted Version Download (1MB) | Preview |
|
|
Text
Parasitology_LaCourse_InPress_2019.pdf - Published Version Available under License Creative Commons Attribution. Download (781kB) | Preview |
Abstract
Filarial nematodes possess glutathione transferases (GSTs), ubiquitous enzymes with potential to detoxify xenobiotic and endogenous substrates, and modulate the host immune system, which may aid worm infection establishment, maintenance and survival in the host. Here we have identified and characterised a sigma class glycosylated GST (OoGST1), from the cattle-infective filarial nematode Onchocerca ochengi, which is homologous (99% amino acid identity) with an immunodominant GST and potential vaccine candidate from the human parasite, O. volvulus, (OvGST1b). O. ochengi native GSTs were purified using a two-step affinity chromatography approach, resolved by 2D and 1D SDS-PAGE and subjected to enzymic deglycosylation revealing the existence of at least four glycoforms. A combination of lectin-blotting and mass spectrometry (MS) analyses of the released N-glycans indicated that OoGST1 contained mainly oligomannose Man5GlcNAc2 structure, but also hybrid- and larger oligommanose-type glycans in a lower proportion. Furthermore, purified OoGST1 showed prostaglandin synthase activity as confirmed by Liquid Chromatography (LC)/MS following a coupled-enzyme assay. This is only the second reported and characterised glycosylated GST and our study highlights its potential role in host-parasite interactions and use in the study of human onchocerciasis.
| Item Type: | Article |
|---|---|
| Subjects: | QU Biochemistry > Enzymes > QU 141 Transferases WC Communicable Diseases > Tropical and Parasitic Diseases > WC 695 Parasitic diseases (General) WC Communicable Diseases > Tropical and Parasitic Diseases > WC 850 Nematode infections (General) WC Communicable Diseases > Tropical and Parasitic Diseases > WC 885 Onchocerciasis |
| Faculty: Department: | Biological Sciences > Department of Tropical Disease Biology Biological Sciences > Vector Biology Department Education |
| Digital Object Identifer (DOI): | https://doi.org/10.1017/S0031182019000763 |
| Depositing User: | Stacy Murtagh |
| Date Deposited: | 14 Jun 2019 10:18 |
| Last Modified: | 23 Jan 2020 12:27 |
| URI: | https://archive.lstmed.ac.uk/id/eprint/11040 |
Statistics
Actions (login required)
 |
Edit Item |