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Systematic analysis of Plasmodium myosins reveals differential expression, localisation, and function in invasive and proliferative parasite stages

The myosin superfamily comprises of actin‐dependent eukaryotic molecular motors important in a variety of cellular functions. Although well studied in many systems, knowledge of their functions in Plasmodium, the causative agent of malaria, is restricted. Previously, six myosins were identified in t...

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Autores principales: Wall, Richard J., Zeeshan, Mohammad, Katris, Nicholas J., Limenitakis, Rebecca, Rea, Edward, Stock, Jessica, Brady, Declan, Waller, Ross F., Holder, Anthony A., Tewari, Rita
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6851706/
https://www.ncbi.nlm.nih.gov/pubmed/31283102
http://dx.doi.org/10.1111/cmi.13082
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author Wall, Richard J.
Zeeshan, Mohammad
Katris, Nicholas J.
Limenitakis, Rebecca
Rea, Edward
Stock, Jessica
Brady, Declan
Waller, Ross F.
Holder, Anthony A.
Tewari, Rita
author_facet Wall, Richard J.
Zeeshan, Mohammad
Katris, Nicholas J.
Limenitakis, Rebecca
Rea, Edward
Stock, Jessica
Brady, Declan
Waller, Ross F.
Holder, Anthony A.
Tewari, Rita
author_sort Wall, Richard J.
collection PubMed
description The myosin superfamily comprises of actin‐dependent eukaryotic molecular motors important in a variety of cellular functions. Although well studied in many systems, knowledge of their functions in Plasmodium, the causative agent of malaria, is restricted. Previously, six myosins were identified in this genus, including three Class XIV myosins found only in Apicomplexa and some Ciliates. The well characterized MyoA is a Class XIV myosin essential for gliding motility and invasion. Here, we characterize all other Plasmodium myosins throughout the parasite life cycle and show that they have very diverse patterns of expression and cellular location. MyoB and MyoE, the other two Class XIV myosins, are expressed in all invasive stages, with apical and basal locations, respectively. Gene deletion revealed that MyoE is involved in sporozoite traversal, MyoF and MyoK are likely essential in the asexual blood stages, and MyoJ and MyoB are not essential. Both MyoB and its essential light chain (MCL‐B) are localised at the apical end of ookinetes but expressed at completely different time points. This work provides a better understanding of the role of actomyosin motors in Apicomplexan parasites, particularly in the motile and invasive stages of Plasmodium during sexual and asexual development within the mosquito.
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spelling pubmed-68517062019-11-18 Systematic analysis of Plasmodium myosins reveals differential expression, localisation, and function in invasive and proliferative parasite stages Wall, Richard J. Zeeshan, Mohammad Katris, Nicholas J. Limenitakis, Rebecca Rea, Edward Stock, Jessica Brady, Declan Waller, Ross F. Holder, Anthony A. Tewari, Rita Cell Microbiol Editor's Choice The myosin superfamily comprises of actin‐dependent eukaryotic molecular motors important in a variety of cellular functions. Although well studied in many systems, knowledge of their functions in Plasmodium, the causative agent of malaria, is restricted. Previously, six myosins were identified in this genus, including three Class XIV myosins found only in Apicomplexa and some Ciliates. The well characterized MyoA is a Class XIV myosin essential for gliding motility and invasion. Here, we characterize all other Plasmodium myosins throughout the parasite life cycle and show that they have very diverse patterns of expression and cellular location. MyoB and MyoE, the other two Class XIV myosins, are expressed in all invasive stages, with apical and basal locations, respectively. Gene deletion revealed that MyoE is involved in sporozoite traversal, MyoF and MyoK are likely essential in the asexual blood stages, and MyoJ and MyoB are not essential. Both MyoB and its essential light chain (MCL‐B) are localised at the apical end of ookinetes but expressed at completely different time points. This work provides a better understanding of the role of actomyosin motors in Apicomplexan parasites, particularly in the motile and invasive stages of Plasmodium during sexual and asexual development within the mosquito. John Wiley and Sons Inc. 2019-07-23 2019-10 /pmc/articles/PMC6851706/ /pubmed/31283102 http://dx.doi.org/10.1111/cmi.13082 Text en © 2019 The Authors Cellular Microbiology Published by John Wiley & Sons Ltd This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Editor's Choice
Wall, Richard J.
Zeeshan, Mohammad
Katris, Nicholas J.
Limenitakis, Rebecca
Rea, Edward
Stock, Jessica
Brady, Declan
Waller, Ross F.
Holder, Anthony A.
Tewari, Rita
Systematic analysis of Plasmodium myosins reveals differential expression, localisation, and function in invasive and proliferative parasite stages
title Systematic analysis of Plasmodium myosins reveals differential expression, localisation, and function in invasive and proliferative parasite stages
title_full Systematic analysis of Plasmodium myosins reveals differential expression, localisation, and function in invasive and proliferative parasite stages
title_fullStr Systematic analysis of Plasmodium myosins reveals differential expression, localisation, and function in invasive and proliferative parasite stages
title_full_unstemmed Systematic analysis of Plasmodium myosins reveals differential expression, localisation, and function in invasive and proliferative parasite stages
title_short Systematic analysis of Plasmodium myosins reveals differential expression, localisation, and function in invasive and proliferative parasite stages
title_sort systematic analysis of plasmodium myosins reveals differential expression, localisation, and function in invasive and proliferative parasite stages
topic Editor's Choice
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6851706/
https://www.ncbi.nlm.nih.gov/pubmed/31283102
http://dx.doi.org/10.1111/cmi.13082
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