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Exploring and Expanding the Fatty Acid Binding Protein superfamily in Fasciola species.

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Morphew, Russell Mark, Wilkinson, Toby J, Mackintosh, Neil, Jahndel, Veronika, Paterson, Steve, McVeigh, Paul, Abbas Abidi, Syed M, Saifullah, Khalid, Raman, Muthusamy, Ravikumar, Gopalakrishnan, LaCourse, James ORCID: https://orcid.org/0000-0001-9261-7136, Maule, Aaron G and Brophy, Peter M (2016) 'Exploring and Expanding the Fatty Acid Binding Protein superfamily in Fasciola species.'. Journal of proteome research, Vol 15, Issue 9, pp. 3308-3321.

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Abstract

The liver flukes Fasciola hepatica and F. gigantica infect livestock worldwide and threaten food security with climate change and problematic control measures spreading disease. Fascioliasis is also a food borne disease with up to 17 million humans infected. In the absence of vaccines, treatment depends on Triclabendazole (TCBZ) and over-use has led to widespread resistance, compromising future TCBZ control. Reductionist biology from many laboratories has predicted new therapeutic targets. To this end, the fatty acid binding protein (FABP) superfamily have proposed multi-functional roles, including functions intersecting vaccine and drug therapy, such as immune modulation and anthelmintic sequestration. Research is hindered by a lack of understanding of the full FABP superfamily complement. Although discovery studies predicted FABPs as promising vaccine candidates, it is unclear if uncharacterised FABPs are more relevant for vaccine formulations. We have coupled genome, transcriptome and EST data mining with proteomics and phylogenetics, to reveal a liver fluke FABP superfamily of 7 clades: previously identified clades I-III and newly identified clades IV-VII. All new clade FABPs were analysed using bioinformatics and cloned from both liver flukes. The extended FABP dataset will provide new study tools to research the role of FABPs in parasite biology and as therapy targets.

Item Type: Article
Uncontrolled Keywords: Fasciola hepatica; F. gigantica; Proteomics; Diagnosis; Gene Characterisation
Subjects: QU Biochemistry > Genetics > QU 460 Genomics. Proteomics
QW Microbiology and Immunology > Immunotherapy and Hypersensitivity > QW 805 Vaccines. Antitoxins. Toxoids
QX Parasitology > Helminths. Annelida > QX 365 Fasciola
Faculty: Department: Biological Sciences > Department of Tropical Disease Biology
Digital Object Identifer (DOI): https://doi.org/10.1021/acs.jproteome.6b00331
Depositing User: Mary Creegan
Date Deposited: 16 Aug 2016 15:43
Last Modified: 06 Feb 2018 13:13
URI: http://archive.lstmed.ac.uk/id/eprint/6058

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