A dominance of Mu class glutathione transferases within the equine tapeworm Anoplocephala perfoliata
The most common equine tapeworm, Anoplocephala perfoliata, has often been neglected amongst molecular investigations and has been faced with limited treatment options. However, the recent release of a transcriptome dataset has now provided opportunities for in-depth analysis of A. perfoliata protein...
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Cambridge University Press
2024-03-01
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Series: | Parasitology |
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Online Access: | https://www.cambridge.org/core/product/identifier/S0031182024000015/type/journal_article |
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author | Holly M. Northcote Boontarikaan Wititkornkul David J. Cutress Nathan D. Allen Peter M. Brophy Ruth E. Wonfor Russell M. Morphew |
author_facet | Holly M. Northcote Boontarikaan Wititkornkul David J. Cutress Nathan D. Allen Peter M. Brophy Ruth E. Wonfor Russell M. Morphew |
author_sort | Holly M. Northcote |
collection | DOAJ |
description | The most common equine tapeworm, Anoplocephala perfoliata, has often been neglected amongst molecular investigations and has been faced with limited treatment options. However, the recent release of a transcriptome dataset has now provided opportunities for in-depth analysis of A. perfoliata protein expression. Here, global, and sub-proteomic approaches were utilized to provide a comprehensive characterization of the A. perfoliata soluble glutathione transferases (GST) (ApGST). Utilizing both bioinformatics and gel-based proteomics, GeLC and 2D-SDS PAGE, the A. perfoliata ‘GST-ome’ was observed to be dominated with Mu class GST representatives. In addition, both Sigma and Omega class GSTs were identified, albeit to a lesser extent and absent from affinity chromatography approaches. Moreover, 51 ApGSTs were localized across somatic (47 GSTs), extracellular vesicles (EVs) (Whole: 1 GST, Surface: 2 GSTs) and EV depleted excretory secretory product (ESP) (9 GSTs) proteomes. In related helminths, GSTs have shown promise as novel anthelmintic or vaccine targets for improved helminth control. Thus, provides potential targets for understanding A. perfoliata novel infection mechanisms, host–parasite relationships and anthelmintic treatments. |
first_indexed | 2024-03-08T08:51:03Z |
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id | doaj.art-2329217313744948bb9ad246c58ff837 |
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issn | 0031-1820 1469-8161 |
language | English |
last_indexed | 2024-04-24T12:12:10Z |
publishDate | 2024-03-01 |
publisher | Cambridge University Press |
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series | Parasitology |
spelling | doaj.art-2329217313744948bb9ad246c58ff8372024-04-08T10:29:10ZengCambridge University PressParasitology0031-18201469-81612024-03-0115128229410.1017/S0031182024000015A dominance of Mu class glutathione transferases within the equine tapeworm Anoplocephala perfoliataHolly M. Northcote0https://orcid.org/0000-0001-6066-6419Boontarikaan Wititkornkul1David J. Cutress2Nathan D. Allen3Peter M. Brophy4Ruth E. Wonfor5Russell M. Morphew6https://orcid.org/0000-0003-0304-4730Department of Life Sciences, Aberystwyth University, Aberystwyth SY23 3DA, UK;Department of Life Sciences, Aberystwyth University, Aberystwyth SY23 3DA, UK; Faculty of Veterinary Science, Rajamangala University of Technology Srivijaya, Nakhon Si Thammarat 80240, ThailandDepartment of Life Sciences, Aberystwyth University, Aberystwyth SY23 3DA, UK;Department of Life Sciences, Aberystwyth University, Aberystwyth SY23 3DA, UK;Department of Life Sciences, Aberystwyth University, Aberystwyth SY23 3DA, UK;Department of Life Sciences, Aberystwyth University, Aberystwyth SY23 3DA, UK;Department of Life Sciences, Aberystwyth University, Aberystwyth SY23 3DA, UK;The most common equine tapeworm, Anoplocephala perfoliata, has often been neglected amongst molecular investigations and has been faced with limited treatment options. However, the recent release of a transcriptome dataset has now provided opportunities for in-depth analysis of A. perfoliata protein expression. Here, global, and sub-proteomic approaches were utilized to provide a comprehensive characterization of the A. perfoliata soluble glutathione transferases (GST) (ApGST). Utilizing both bioinformatics and gel-based proteomics, GeLC and 2D-SDS PAGE, the A. perfoliata ‘GST-ome’ was observed to be dominated with Mu class GST representatives. In addition, both Sigma and Omega class GSTs were identified, albeit to a lesser extent and absent from affinity chromatography approaches. Moreover, 51 ApGSTs were localized across somatic (47 GSTs), extracellular vesicles (EVs) (Whole: 1 GST, Surface: 2 GSTs) and EV depleted excretory secretory product (ESP) (9 GSTs) proteomes. In related helminths, GSTs have shown promise as novel anthelmintic or vaccine targets for improved helminth control. Thus, provides potential targets for understanding A. perfoliata novel infection mechanisms, host–parasite relationships and anthelmintic treatments.https://www.cambridge.org/core/product/identifier/S0031182024000015/type/journal_articleAnoplocephala perfoliataglutathione transferasemuomegasigmasomatic |
spellingShingle | Holly M. Northcote Boontarikaan Wititkornkul David J. Cutress Nathan D. Allen Peter M. Brophy Ruth E. Wonfor Russell M. Morphew A dominance of Mu class glutathione transferases within the equine tapeworm Anoplocephala perfoliata Parasitology Anoplocephala perfoliata glutathione transferase mu omega sigma somatic |
title | A dominance of Mu class glutathione transferases within the equine tapeworm Anoplocephala perfoliata |
title_full | A dominance of Mu class glutathione transferases within the equine tapeworm Anoplocephala perfoliata |
title_fullStr | A dominance of Mu class glutathione transferases within the equine tapeworm Anoplocephala perfoliata |
title_full_unstemmed | A dominance of Mu class glutathione transferases within the equine tapeworm Anoplocephala perfoliata |
title_short | A dominance of Mu class glutathione transferases within the equine tapeworm Anoplocephala perfoliata |
title_sort | dominance of mu class glutathione transferases within the equine tapeworm anoplocephala perfoliata |
topic | Anoplocephala perfoliata glutathione transferase mu omega sigma somatic |
url | https://www.cambridge.org/core/product/identifier/S0031182024000015/type/journal_article |
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