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Analyses of Compact Trichinella Kinomes Reveal a MOS-Like Protein Kinase with a Unique N-Terminal Domain
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...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Genetics Society of America
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5015942/ https://www.ncbi.nlm.nih.gov/pubmed/27412987 http://dx.doi.org/10.1534/g3.116.032961 |
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author | Stroehlein, Andreas J. Young, Neil D. Korhonen, Pasi K. Chang, Bill C. H. Sternberg, Paul W. La Rosa, Giuseppe Pozio, Edoardo Gasser, Robin B. |
author_facet | Stroehlein, Andreas J. Young, Neil D. Korhonen, Pasi K. Chang, Bill C. H. Sternberg, Paul W. La Rosa, Giuseppe Pozio, Edoardo Gasser, Robin B. |
author_sort | Stroehlein, Andreas J. |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-5015942 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Genetics Society of America |
record_format | MEDLINE/PubMed |
spelling | pubmed-50159422016-09-09 Analyses of Compact Trichinella Kinomes Reveal a MOS-Like Protein Kinase with a Unique N-Terminal Domain Stroehlein, Andreas J. Young, Neil D. Korhonen, Pasi K. Chang, Bill C. H. Sternberg, Paul W. La Rosa, Giuseppe Pozio, Edoardo Gasser, Robin B. G3 (Bethesda) Investigations 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. Genetics Society of America 2016-07-13 /pmc/articles/PMC5015942/ /pubmed/27412987 http://dx.doi.org/10.1534/g3.116.032961 Text en Copyright © 2016 Stroehlein et al. http://creativecommons.org/licenses/by/4.0/ 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. |
spellingShingle | Investigations Stroehlein, Andreas J. Young, Neil D. Korhonen, Pasi K. Chang, Bill C. H. Sternberg, Paul W. La Rosa, Giuseppe Pozio, Edoardo Gasser, Robin B. Analyses of Compact Trichinella Kinomes Reveal a MOS-Like Protein Kinase with a Unique N-Terminal Domain |
title | Analyses of Compact Trichinella Kinomes Reveal a MOS-Like Protein Kinase with a Unique N-Terminal Domain |
title_full | Analyses of Compact Trichinella Kinomes Reveal a MOS-Like Protein Kinase with a Unique N-Terminal Domain |
title_fullStr | Analyses of Compact Trichinella Kinomes Reveal a MOS-Like Protein Kinase with a Unique N-Terminal Domain |
title_full_unstemmed | Analyses of Compact Trichinella Kinomes Reveal a MOS-Like Protein Kinase with a Unique N-Terminal Domain |
title_short | Analyses of Compact Trichinella Kinomes Reveal a MOS-Like Protein Kinase with a Unique N-Terminal Domain |
title_sort | analyses of compact trichinella kinomes reveal a mos-like protein kinase with a unique n-terminal domain |
topic | Investigations |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5015942/ https://www.ncbi.nlm.nih.gov/pubmed/27412987 http://dx.doi.org/10.1534/g3.116.032961 |
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