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A Trichinella spiralis new born larvae-specific protein, Ts-NBL1, interacts with host’s cell vimentin

The parasitic nematode Trichinella has a special relationship with its host as it has a unique intracellular location within the feeder cell which is a structure derived from skeletal muscle fiber. It has been proposed that “parakines” secreted by Trichinella larvae serve as messengers to implement...

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Autores principales: Wang, A., Liu, X., Heckmann, A., Caignard, G., Vitour, D., Hirchaud, E., Liu, M., Boireau, P., Karadjian, G., Vallée, I.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Berlin Heidelberg 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8993751/
https://www.ncbi.nlm.nih.gov/pubmed/35320836
http://dx.doi.org/10.1007/s00436-022-07479-7
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author Wang, A.
Liu, X.
Heckmann, A.
Caignard, G.
Vitour, D.
Hirchaud, E.
Liu, M.
Boireau, P.
Karadjian, G.
Vallée, I.
author_facet Wang, A.
Liu, X.
Heckmann, A.
Caignard, G.
Vitour, D.
Hirchaud, E.
Liu, M.
Boireau, P.
Karadjian, G.
Vallée, I.
author_sort Wang, A.
collection PubMed
description The parasitic nematode Trichinella has a special relationship with its host as it has a unique intracellular location within the feeder cell which is a structure derived from skeletal muscle fiber. It has been proposed that “parakines” secreted by Trichinella larvae serve as messengers to implement communication between the parasite and the muscle cells through a molecular cross-talk to ensure permanent coexistence within the host. The Ts-NBL1 protein is considered to be a potential key “parakine” involved in the early invasion of the muscle fiber and its transformation into a feeder cell during Trichinella spiralis infection. This study used for the first time yeast two-hybrid (Y2H) technology in Trichinella to identify Ts-NBL1 interacting proteins. GST co-affinity purification experiments confirmed vimentin as an important interactor. The discovery of the new host proteins interacting with Ts-NBL1 will help to suggest that Ts-NBL1 contributes to participate in the capsule formation of feeder cells and provide ideas for understanding the molecular and cellular mechanisms involved in the survival of Trichinella in the host. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s00436-022-07479-7.
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spelling pubmed-89937512022-04-22 A Trichinella spiralis new born larvae-specific protein, Ts-NBL1, interacts with host’s cell vimentin Wang, A. Liu, X. Heckmann, A. Caignard, G. Vitour, D. Hirchaud, E. Liu, M. Boireau, P. Karadjian, G. Vallée, I. Parasitol Res Immunology and Host-Parasite Interactions - Original Paper The parasitic nematode Trichinella has a special relationship with its host as it has a unique intracellular location within the feeder cell which is a structure derived from skeletal muscle fiber. It has been proposed that “parakines” secreted by Trichinella larvae serve as messengers to implement communication between the parasite and the muscle cells through a molecular cross-talk to ensure permanent coexistence within the host. The Ts-NBL1 protein is considered to be a potential key “parakine” involved in the early invasion of the muscle fiber and its transformation into a feeder cell during Trichinella spiralis infection. This study used for the first time yeast two-hybrid (Y2H) technology in Trichinella to identify Ts-NBL1 interacting proteins. GST co-affinity purification experiments confirmed vimentin as an important interactor. The discovery of the new host proteins interacting with Ts-NBL1 will help to suggest that Ts-NBL1 contributes to participate in the capsule formation of feeder cells and provide ideas for understanding the molecular and cellular mechanisms involved in the survival of Trichinella in the host. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s00436-022-07479-7. Springer Berlin Heidelberg 2022-03-23 2022 /pmc/articles/PMC8993751/ /pubmed/35320836 http://dx.doi.org/10.1007/s00436-022-07479-7 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Immunology and Host-Parasite Interactions - Original Paper
Wang, A.
Liu, X.
Heckmann, A.
Caignard, G.
Vitour, D.
Hirchaud, E.
Liu, M.
Boireau, P.
Karadjian, G.
Vallée, I.
A Trichinella spiralis new born larvae-specific protein, Ts-NBL1, interacts with host’s cell vimentin
title A Trichinella spiralis new born larvae-specific protein, Ts-NBL1, interacts with host’s cell vimentin
title_full A Trichinella spiralis new born larvae-specific protein, Ts-NBL1, interacts with host’s cell vimentin
title_fullStr A Trichinella spiralis new born larvae-specific protein, Ts-NBL1, interacts with host’s cell vimentin
title_full_unstemmed A Trichinella spiralis new born larvae-specific protein, Ts-NBL1, interacts with host’s cell vimentin
title_short A Trichinella spiralis new born larvae-specific protein, Ts-NBL1, interacts with host’s cell vimentin
title_sort trichinella spiralis new born larvae-specific protein, ts-nbl1, interacts with host’s cell vimentin
topic Immunology and Host-Parasite Interactions - Original Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8993751/
https://www.ncbi.nlm.nih.gov/pubmed/35320836
http://dx.doi.org/10.1007/s00436-022-07479-7
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