Analyses of Compact Trichinella Kinomes Reveal a MOS-like Protein Kinase with a Unique N-terminal Domain
Abstract
Parasitic worms of the genus Trichinella (phylum Nematoda; class Enoplea) represent a complex of at least twelve taxa that infect a range of different host animals, including humans, around the world. They are foodborne, intracellular nematodes, and their life cycles differ substantially from those of other nematodes. The recent characterization of the genomes and transcriptomes of all twelve recognized taxa of Trichinella now allows, for the first time, detailed studies of their molecular biology. In the present study, we defined, curated, and compared the protein kinase complements (kinomes) of Trichinella spiralis and T. pseudospiralis using an integrated bioinformatic workflow employing transcriptomic and genomic data sets. We examined how variation in the kinome might link to unique aspects of Trichinella morphology, biology, and evolution. Furthermore, we utilized in silico structural modeling to discover and characterize a novel, MOS-like kinase with an unusual, previously undescribed N-terminal domain. Taken together, the present findings provide a basis for comparative investigations of nematode kinomes, and might facilitate the identification of Enoplea-specific intervention and diagnostic targets. Importantly, the in silico modeling approach assessed here provides an exciting prospect of being able to identify and classify currently unknown (orphan) kinases, as a foundation for their subsequent structural and functional investigation.
Additional Information
© 2016 Stroehlein et al. Published by the Genetics Society of America. This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Manuscript received May 19, 2016; accepted for publication July 7, 2016; published Early Online July 13, 2016. Research funding from the National Health and Medical Research Council (NHMRC), Australian Research Council, Wellcome Trust, and The University of Melbourne Business Improvement Program is gratefully acknowledged (R.B.G.). Support from the Australian Academy of Science, the Australian-American Fulbright Commission, Alexander von Humboldt Foundation, and Melbourne Water Corporation, as well as the Victorian Life Sciences Computation Initiative and WormBase (www.wormbase.org), is gratefully acknowledged. P.W.S. acknowledges support from the Howard Hughes Medical Institute and the National Institutes of Health. A.J.S. is a recipient of a Melbourne International Research Scholarship and a Melbourne International Fee Remission Scholarship from the University of Melbourne. N.D.Y. holds an NHMRC Career Development Fellowship.Attached Files
Published - 2847.full.pdf
Submitted - TableS4.xlsx
Supplemental Material - FigureS1.pdf
Supplemental Material - FigureS2.pdf
Supplemental Material - TableS1.xlsx
Supplemental Material - TableS10.xlsx
Supplemental Material - TableS2.xlsx
Supplemental Material - TableS3.xlsx
Supplemental Material - TableS5.xlsx
Supplemental Material - TableS6.xlsx
Supplemental Material - TableS7.xlsx
Supplemental Material - TableS8.xlsx
Supplemental Material - TableS9.xlsx
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Additional details
- PMCID
- PMC5015942
- Eprint ID
- 69202
- DOI
- 10.1534/g3.116.032961
- Resolver ID
- CaltechAUTHORS:20160725-131922343
- National Health and Medical Research Council (NHMRC)
- Australian Research Council
- Wellcome Trust
- University of Melbourne
- Australian Academy of Science
- Australian-American Fulbright Commission
- Alexander von Humboldt Foundation
- Melbourne Water Corporation
- Victorian Life Sciences Computation Initiative (VLSCI)
- WormBase
- Howard Hughes Medical Institute (HHMI)
- NIH
- Created
-
2016-07-25Created from EPrint's datestamp field
- Updated
-
2022-04-26Created from EPrint's last_modified field