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Parasitic nematode fatty acid- and retinol-binding proteins compromise host immunity by interfering with host lipid signaling pathways
Parasitic nematodes cause significant morbidity and mortality globally. Excretory/secretory products (ESPs) such as fatty acid- and retinol- binding proteins (FARs) are hypothesized to suppress host immunity during nematode infection, yet little is known about their interactions with host tissues. L...
Autores principales: | , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8580252/ https://www.ncbi.nlm.nih.gov/pubmed/34714893 http://dx.doi.org/10.1371/journal.ppat.1010027 |
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author | Parks, Sophia C. Nguyen, Susan Nasrolahi, Shyon Bhat, Chaitra Juncaj, Damian Lu, Dihong Ramaswamy, Raghavendran Dhillon, Harpal Fujiwara, Hideji Buchman, Anna Akbari, Omar S. Yamanaka, Naoki Boulanger, Martin J. Dillman, Adler R. |
author_facet | Parks, Sophia C. Nguyen, Susan Nasrolahi, Shyon Bhat, Chaitra Juncaj, Damian Lu, Dihong Ramaswamy, Raghavendran Dhillon, Harpal Fujiwara, Hideji Buchman, Anna Akbari, Omar S. Yamanaka, Naoki Boulanger, Martin J. Dillman, Adler R. |
author_sort | Parks, Sophia C. |
collection | PubMed |
description | Parasitic nematodes cause significant morbidity and mortality globally. Excretory/secretory products (ESPs) such as fatty acid- and retinol- binding proteins (FARs) are hypothesized to suppress host immunity during nematode infection, yet little is known about their interactions with host tissues. Leveraging the insect parasitic nematode, Steinernema carpocapsae, we describe here the first in vivo study demonstrating that FARs modulate animal immunity, causing an increase in susceptibility to bacterial co-infection. Moreover, we show that FARs dampen key components of the fly immune response including the phenoloxidase cascade and antimicrobial peptide (AMP) production. Our data also reveal that FARs deplete lipid signaling precursors in vivo as well as bind to these fatty acids in vitro, suggesting that FARs elicit their immunomodulatory effects by altering the availability of lipid signaling molecules necessary for an efficient immune response. Collectively, these data support a complex role for FARs in immunosuppression in animals and provide detailed mechanistic insight into parasitism in phylum Nematoda. |
format | Online Article Text |
id | pubmed-8580252 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-85802522021-11-11 Parasitic nematode fatty acid- and retinol-binding proteins compromise host immunity by interfering with host lipid signaling pathways Parks, Sophia C. Nguyen, Susan Nasrolahi, Shyon Bhat, Chaitra Juncaj, Damian Lu, Dihong Ramaswamy, Raghavendran Dhillon, Harpal Fujiwara, Hideji Buchman, Anna Akbari, Omar S. Yamanaka, Naoki Boulanger, Martin J. Dillman, Adler R. PLoS Pathog Research Article Parasitic nematodes cause significant morbidity and mortality globally. Excretory/secretory products (ESPs) such as fatty acid- and retinol- binding proteins (FARs) are hypothesized to suppress host immunity during nematode infection, yet little is known about their interactions with host tissues. Leveraging the insect parasitic nematode, Steinernema carpocapsae, we describe here the first in vivo study demonstrating that FARs modulate animal immunity, causing an increase in susceptibility to bacterial co-infection. Moreover, we show that FARs dampen key components of the fly immune response including the phenoloxidase cascade and antimicrobial peptide (AMP) production. Our data also reveal that FARs deplete lipid signaling precursors in vivo as well as bind to these fatty acids in vitro, suggesting that FARs elicit their immunomodulatory effects by altering the availability of lipid signaling molecules necessary for an efficient immune response. Collectively, these data support a complex role for FARs in immunosuppression in animals and provide detailed mechanistic insight into parasitism in phylum Nematoda. Public Library of Science 2021-10-29 /pmc/articles/PMC8580252/ /pubmed/34714893 http://dx.doi.org/10.1371/journal.ppat.1010027 Text en © 2021 Parks et al https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Parks, Sophia C. Nguyen, Susan Nasrolahi, Shyon Bhat, Chaitra Juncaj, Damian Lu, Dihong Ramaswamy, Raghavendran Dhillon, Harpal Fujiwara, Hideji Buchman, Anna Akbari, Omar S. Yamanaka, Naoki Boulanger, Martin J. Dillman, Adler R. Parasitic nematode fatty acid- and retinol-binding proteins compromise host immunity by interfering with host lipid signaling pathways |
title | Parasitic nematode fatty acid- and retinol-binding proteins compromise host immunity by interfering with host lipid signaling pathways |
title_full | Parasitic nematode fatty acid- and retinol-binding proteins compromise host immunity by interfering with host lipid signaling pathways |
title_fullStr | Parasitic nematode fatty acid- and retinol-binding proteins compromise host immunity by interfering with host lipid signaling pathways |
title_full_unstemmed | Parasitic nematode fatty acid- and retinol-binding proteins compromise host immunity by interfering with host lipid signaling pathways |
title_short | Parasitic nematode fatty acid- and retinol-binding proteins compromise host immunity by interfering with host lipid signaling pathways |
title_sort | parasitic nematode fatty acid- and retinol-binding proteins compromise host immunity by interfering with host lipid signaling pathways |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8580252/ https://www.ncbi.nlm.nih.gov/pubmed/34714893 http://dx.doi.org/10.1371/journal.ppat.1010027 |
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