Characterization of the complete mitochondrial genome of Diplostomum baeri

Article

Landeryou, T., Ropiquet, A., Kett, S., Wildeboer, D. and Lawton, S. 2020. Characterization of the complete mitochondrial genome of Diplostomum baeri. Parasitology International. 79. https://doi.org/10.1016/j.parint.2020.102166
TypeArticle
TitleCharacterization of the complete mitochondrial genome of Diplostomum baeri
AuthorsLanderyou, T., Ropiquet, A., Kett, S., Wildeboer, D. and Lawton, S.
Abstract

Despite Diplostomum baeri (Dubois, 1937) being one of the most widely distributed parasites of freshwater fish, there is no complete mitochondrial (mt) genome currently available. The complicated systematics presented by D. baeri has hampered investigations into the species distributions and infective dynamics of the species. Within this study we obtained complete mt genome sequences of D. baeri and assessed its phylogenetic relationship with other species of Digenea. The complete mitochondrial genome of D. baeri is 14,480 bp in length, containing 36 genes in total. The phylogenetic tree resulting from Bayesian inference of concatenated 12 protein coding gene sequences placed D. baeri alongside published mt genomes of Diplostomidae, with the overall taxonomic placement of the genus being a sister lineage of the order Plagiochiida The characterization of further mitochondrial genomes within the family Diplostomidae will help progress phylogenetic and epidemiological investigations as well as providing a framework for the analysis of diagnostic markers to be used in further monitoring of the parasite worldwide. [Abstract copyright: Copyright © 2019. Published by Elsevier B.V.]

KeywordsDiplostomum baeri, Freshwater parasite, Metacercariae, Mitochondrial genome, Trematode
PublisherElsevier
JournalParasitology International
ISSN1383-5769
Electronic1873-0329
Publication dates
Online27 Jun 2020
Print01 Dec 2020
Publication process dates
Deposited14 Jul 2020
Submitted18 Jul 2019
Accepted23 Jun 2020
Output statusPublished
Digital Object Identifier (DOI)https://doi.org/10.1016/j.parint.2020.102166
LanguageEnglish
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Naus, S., Reipschläger, S., Wildeboer, D., Lichtenthaler, S., Mitterreiter, S., Guan, Z., Moss, M. and Bartsch, J. 2006. Identification of candidate substrates for ectodomain shedding by the metalloprotease-disintegrin ADAM8. Biological Chemistry. 387 (3), pp. 337-346. https://doi.org/10.1515/BC.2006.045
Metalloproteinase disintegrins ADAM8 and ADAM19 are highly regulated in human primary brain tumors and their expression levels and activities are associated with invasiveness.
Wildeboer, D., Naus, S., Sang, Q., Bartsch, J. and Pagenstecher, A. 2006. Metalloproteinase disintegrins ADAM8 and ADAM19 are highly regulated in human primary brain tumors and their expression levels and activities are associated with invasiveness. Journal of Neuropathology and Experimental Neurology. 65 (5), pp. 516-527.
Screening of herbal constituents for aromatase inhibitory activity
Paoletta, S., Steventon, G., Wildeboer, D., Ehrman, T., Hylands, P. and Barlow, D. 2008. Screening of herbal constituents for aromatase inhibitory activity. Bioorganic & Medicinal Chemistry. 16 (18), pp. 8466-8470. https://doi.org/10.1016/j.bmc.2008.08.034
Use of antibody–hapten complexes attached to optical sensor surfaces as a substrate for proteases: real-time biosensing of protease activity
Wildeboer, D., Jiang, P., Price, R., Yu, S., Jeganathan, F. and Abuknesha, R. 2010. Use of antibody–hapten complexes attached to optical sensor surfaces as a substrate for proteases: real-time biosensing of protease activity. Talanta. 81 (1-2), pp. 68-75. https://doi.org/10.1016/j.talanta.2009.11.036
Characterization of bacterial proteases with a panel of fluorescent peptide substrates
Wildeboer, D., Jeganathan, F., Price, R. and Abuknesha, R. 2009. Characterization of bacterial proteases with a panel of fluorescent peptide substrates. Analytical Biochemistry. 384 (2), pp. 321-328. https://doi.org/10.1016/j.ab.2008.10.004
The ADAM10 prodomain is a specific inhibitor of ADAM10 proteolytic activity and inhibits cellular shedding events
Moss, M., Bomar, M., Liu, Q., Sage, H., Dempsey, P., Lenhart, P., Gillispie, P., Stoeck, A., Wildeboer, D., Bartsch, J., Palmisano, R. and Zhou, P. 2007. The ADAM10 prodomain is a specific inhibitor of ADAM10 proteolytic activity and inhibits cellular shedding events. Journal of Biological Chemistry. 282 (49), pp. 35712-35721. https://doi.org/10.1074/jbc.M703231200