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...
Main Authors: | , , , , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
Oxford University Press
2016-09-01
|
Series: | G3: Genes, Genomes, Genetics |
Subjects: | |
Online Access: | http://g3journal.org/lookup/doi/10.1534/g3.116.032961 |
id |
doaj-8effd942c89b41519e9b0d7293e5d662 |
---|---|
record_format |
Article |
spelling |
doaj-8effd942c89b41519e9b0d7293e5d6622021-07-02T03:12:44ZengOxford University PressG3: Genes, Genomes, Genetics2160-18362016-09-01692847285610.1534/g3.116.03296117Analyses of Compact Trichinella Kinomes Reveal a MOS-Like Protein Kinase with a Unique N-Terminal DomainAndreas J. StroehleinNeil D. YoungPasi K. KorhonenBill C. H. ChangPaul W. SternbergGiuseppe La RosaEdoardo PozioRobin B. GasserParasitic 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.http://g3journal.org/lookup/doi/10.1534/g3.116.032961parasitic wormsTrichinellakinomeprotein kinasesprotein annotation |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Andreas J. Stroehlein Neil D. Young Pasi K. Korhonen Bill C. H. Chang Paul W. Sternberg Giuseppe La Rosa Edoardo Pozio Robin B. Gasser |
spellingShingle |
Andreas J. Stroehlein Neil D. Young Pasi K. Korhonen Bill C. H. Chang Paul W. Sternberg Giuseppe La Rosa Edoardo Pozio Robin B. Gasser Analyses of Compact Trichinella Kinomes Reveal a MOS-Like Protein Kinase with a Unique N-Terminal Domain G3: Genes, Genomes, Genetics parasitic worms Trichinella kinome protein kinases protein annotation |
author_facet |
Andreas J. Stroehlein Neil D. Young Pasi K. Korhonen Bill C. H. Chang Paul W. Sternberg Giuseppe La Rosa Edoardo Pozio Robin B. Gasser |
author_sort |
Andreas J. Stroehlein |
title |
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_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_sort |
analyses of compact trichinella kinomes reveal a mos-like protein kinase with a unique n-terminal domain |
publisher |
Oxford University Press |
series |
G3: Genes, Genomes, Genetics |
issn |
2160-1836 |
publishDate |
2016-09-01 |
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. |
topic |
parasitic worms Trichinella kinome protein kinases protein annotation |
url |
http://g3journal.org/lookup/doi/10.1534/g3.116.032961 |
work_keys_str_mv |
AT andreasjstroehlein analysesofcompacttrichinellakinomesrevealamoslikeproteinkinasewithauniquenterminaldomain AT neildyoung analysesofcompacttrichinellakinomesrevealamoslikeproteinkinasewithauniquenterminaldomain AT pasikkorhonen analysesofcompacttrichinellakinomesrevealamoslikeproteinkinasewithauniquenterminaldomain AT billchchang analysesofcompacttrichinellakinomesrevealamoslikeproteinkinasewithauniquenterminaldomain AT paulwsternberg analysesofcompacttrichinellakinomesrevealamoslikeproteinkinasewithauniquenterminaldomain AT giuseppelarosa analysesofcompacttrichinellakinomesrevealamoslikeproteinkinasewithauniquenterminaldomain AT edoardopozio analysesofcompacttrichinellakinomesrevealamoslikeproteinkinasewithauniquenterminaldomain AT robinbgasser analysesofcompacttrichinellakinomesrevealamoslikeproteinkinasewithauniquenterminaldomain |
_version_ |
1721341972544749568 |