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Characterisation of N-linked protein glycosylation in the bacterial pathogen Campylobacter hepaticus
Campylobacter hepaticus is an important pathogen which causes Spotty Liver Disease (SLD) in layer chickens. SLD results in an increase in mortality and a significant decrease in egg production and therefore is an important economic concern of the global poultry industry. The human pathogen Campyloba...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9816155/ https://www.ncbi.nlm.nih.gov/pubmed/36604449 http://dx.doi.org/10.1038/s41598-022-26532-0 |
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author | McDonald, Jamieson B. Scott, Nichollas E. Underwood, Greg J. Andrews, Daniel M. Van, Thi Thu Hao Moore, Robert J. |
author_facet | McDonald, Jamieson B. Scott, Nichollas E. Underwood, Greg J. Andrews, Daniel M. Van, Thi Thu Hao Moore, Robert J. |
author_sort | McDonald, Jamieson B. |
collection | PubMed |
description | Campylobacter hepaticus is an important pathogen which causes Spotty Liver Disease (SLD) in layer chickens. SLD results in an increase in mortality and a significant decrease in egg production and therefore is an important economic concern of the global poultry industry. The human pathogen Campylobacter jejuni encodes an N-linked glycosylation system that plays fundamental roles in host colonization and pathogenicity. While N-linked glycosylation has been extensively studied in C. jejuni and is now known to occur in a range of Campylobacter species, little is known about C. hepaticus glycosylation. In this study glycoproteomic analysis was used to confirm the functionality of the C. hepaticus N-glycosylation system. It was shown that C. hepaticus HV10(T) modifies > 35 proteins with an N-linked heptasaccharide glycan. C. hepaticus shares highly conserved glycoproteins with C. jejuni that are involved in host colonisation and also possesses unique glycoproteins which may contribute to its ability to survive in challenging host environments. C. hepaticus N-glycosylation may function as an important virulence factor, providing an opportunity to investigate and develop a better understanding the system’s role in poultry infection. |
format | Online Article Text |
id | pubmed-9816155 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-98161552023-01-07 Characterisation of N-linked protein glycosylation in the bacterial pathogen Campylobacter hepaticus McDonald, Jamieson B. Scott, Nichollas E. Underwood, Greg J. Andrews, Daniel M. Van, Thi Thu Hao Moore, Robert J. Sci Rep Article Campylobacter hepaticus is an important pathogen which causes Spotty Liver Disease (SLD) in layer chickens. SLD results in an increase in mortality and a significant decrease in egg production and therefore is an important economic concern of the global poultry industry. The human pathogen Campylobacter jejuni encodes an N-linked glycosylation system that plays fundamental roles in host colonization and pathogenicity. While N-linked glycosylation has been extensively studied in C. jejuni and is now known to occur in a range of Campylobacter species, little is known about C. hepaticus glycosylation. In this study glycoproteomic analysis was used to confirm the functionality of the C. hepaticus N-glycosylation system. It was shown that C. hepaticus HV10(T) modifies > 35 proteins with an N-linked heptasaccharide glycan. C. hepaticus shares highly conserved glycoproteins with C. jejuni that are involved in host colonisation and also possesses unique glycoproteins which may contribute to its ability to survive in challenging host environments. C. hepaticus N-glycosylation may function as an important virulence factor, providing an opportunity to investigate and develop a better understanding the system’s role in poultry infection. Nature Publishing Group UK 2023-01-05 /pmc/articles/PMC9816155/ /pubmed/36604449 http://dx.doi.org/10.1038/s41598-022-26532-0 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open Access This 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 | Article McDonald, Jamieson B. Scott, Nichollas E. Underwood, Greg J. Andrews, Daniel M. Van, Thi Thu Hao Moore, Robert J. Characterisation of N-linked protein glycosylation in the bacterial pathogen Campylobacter hepaticus |
title | Characterisation of N-linked protein glycosylation in the bacterial pathogen Campylobacter hepaticus |
title_full | Characterisation of N-linked protein glycosylation in the bacterial pathogen Campylobacter hepaticus |
title_fullStr | Characterisation of N-linked protein glycosylation in the bacterial pathogen Campylobacter hepaticus |
title_full_unstemmed | Characterisation of N-linked protein glycosylation in the bacterial pathogen Campylobacter hepaticus |
title_short | Characterisation of N-linked protein glycosylation in the bacterial pathogen Campylobacter hepaticus |
title_sort | characterisation of n-linked protein glycosylation in the bacterial pathogen campylobacter hepaticus |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9816155/ https://www.ncbi.nlm.nih.gov/pubmed/36604449 http://dx.doi.org/10.1038/s41598-022-26532-0 |
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