Cargando…
The sweet side of the pathogenic Neisseria: the role of glycan interactions in colonisation and disease
Glycomics is a rapidly growing field that focuses on the structure and function of carbohydrates (glycans) in biological systems. Glycan interactions play a major role in infectious disease, at all stages of colonisation and disease progression. Neisseria meningitidis, the cause of meningococcal sep...
Autores principales: | , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5808653/ https://www.ncbi.nlm.nih.gov/pubmed/28633281 http://dx.doi.org/10.1093/femspd/ftx063 |
_version_ | 1783299485401612288 |
---|---|
author | Mubaiwa, Tsitsi D. Semchenko, Evgeny A. Hartley-Tassell, Lauren E. Day, Christopher J. Jennings, Michael P. Seib, Kate L. |
author_facet | Mubaiwa, Tsitsi D. Semchenko, Evgeny A. Hartley-Tassell, Lauren E. Day, Christopher J. Jennings, Michael P. Seib, Kate L. |
author_sort | Mubaiwa, Tsitsi D. |
collection | PubMed |
description | Glycomics is a rapidly growing field that focuses on the structure and function of carbohydrates (glycans) in biological systems. Glycan interactions play a major role in infectious disease, at all stages of colonisation and disease progression. Neisseria meningitidis, the cause of meningococcal sepsis and meningitis, and Neisseria gonorrhoeae, which causes the sexually transmitted infection gonorrhoea, are responsible for significant morbidity and mortality worldwide. Neisseria meningitidis displays a range of surface glycosylations including capsule polysaccharide, lipooligosaccharide and O-linked glycoproteins. While N. gonorrhoeae does not have a capsule, it does express both lipooligosaccharide and O-linked glycoproteins. Neisseria gonorrhoeae also has the ability to scavenge host sialic acids, while several N. meningitidis serogroups can synthesise sialic acid. Surface expressed sialic acid is key in serum resistance and survival in the host. On the host side, the pathogenic Neisseria protein adhesins such as Opc and NHBA bind to host glycans for adherence and colonisation of host cells. Essentially, from both the bacterial and host perspective, glycan interactions are fundamental in colonisation and disease of pathogenic Neisseria. The key aspects of glycobiology of the pathogenic Neisseria are reviewed herein. |
format | Online Article Text |
id | pubmed-5808653 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-58086532018-02-15 The sweet side of the pathogenic Neisseria: the role of glycan interactions in colonisation and disease Mubaiwa, Tsitsi D. Semchenko, Evgeny A. Hartley-Tassell, Lauren E. Day, Christopher J. Jennings, Michael P. Seib, Kate L. Pathog Dis Minireview Glycomics is a rapidly growing field that focuses on the structure and function of carbohydrates (glycans) in biological systems. Glycan interactions play a major role in infectious disease, at all stages of colonisation and disease progression. Neisseria meningitidis, the cause of meningococcal sepsis and meningitis, and Neisseria gonorrhoeae, which causes the sexually transmitted infection gonorrhoea, are responsible for significant morbidity and mortality worldwide. Neisseria meningitidis displays a range of surface glycosylations including capsule polysaccharide, lipooligosaccharide and O-linked glycoproteins. While N. gonorrhoeae does not have a capsule, it does express both lipooligosaccharide and O-linked glycoproteins. Neisseria gonorrhoeae also has the ability to scavenge host sialic acids, while several N. meningitidis serogroups can synthesise sialic acid. Surface expressed sialic acid is key in serum resistance and survival in the host. On the host side, the pathogenic Neisseria protein adhesins such as Opc and NHBA bind to host glycans for adherence and colonisation of host cells. Essentially, from both the bacterial and host perspective, glycan interactions are fundamental in colonisation and disease of pathogenic Neisseria. The key aspects of glycobiology of the pathogenic Neisseria are reviewed herein. Oxford University Press 2017-06-13 /pmc/articles/PMC5808653/ /pubmed/28633281 http://dx.doi.org/10.1093/femspd/ftx063 Text en © FEMS 2017. http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs licence (http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial reproduction and distribution of the work, in any medium, provided the original work is not altered or transformed in any way, and that the work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Minireview Mubaiwa, Tsitsi D. Semchenko, Evgeny A. Hartley-Tassell, Lauren E. Day, Christopher J. Jennings, Michael P. Seib, Kate L. The sweet side of the pathogenic Neisseria: the role of glycan interactions in colonisation and disease |
title | The sweet side of the pathogenic Neisseria: the role of glycan interactions in colonisation and disease |
title_full | The sweet side of the pathogenic Neisseria: the role of glycan interactions in colonisation and disease |
title_fullStr | The sweet side of the pathogenic Neisseria: the role of glycan interactions in colonisation and disease |
title_full_unstemmed | The sweet side of the pathogenic Neisseria: the role of glycan interactions in colonisation and disease |
title_short | The sweet side of the pathogenic Neisseria: the role of glycan interactions in colonisation and disease |
title_sort | sweet side of the pathogenic neisseria: the role of glycan interactions in colonisation and disease |
topic | Minireview |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5808653/ https://www.ncbi.nlm.nih.gov/pubmed/28633281 http://dx.doi.org/10.1093/femspd/ftx063 |
work_keys_str_mv | AT mubaiwatsitsid thesweetsideofthepathogenicneisseriatheroleofglycaninteractionsincolonisationanddisease AT semchenkoevgenya thesweetsideofthepathogenicneisseriatheroleofglycaninteractionsincolonisationanddisease AT hartleytasselllaurene thesweetsideofthepathogenicneisseriatheroleofglycaninteractionsincolonisationanddisease AT daychristopherj thesweetsideofthepathogenicneisseriatheroleofglycaninteractionsincolonisationanddisease AT jenningsmichaelp thesweetsideofthepathogenicneisseriatheroleofglycaninteractionsincolonisationanddisease AT seibkatel thesweetsideofthepathogenicneisseriatheroleofglycaninteractionsincolonisationanddisease AT mubaiwatsitsid sweetsideofthepathogenicneisseriatheroleofglycaninteractionsincolonisationanddisease AT semchenkoevgenya sweetsideofthepathogenicneisseriatheroleofglycaninteractionsincolonisationanddisease AT hartleytasselllaurene sweetsideofthepathogenicneisseriatheroleofglycaninteractionsincolonisationanddisease AT daychristopherj sweetsideofthepathogenicneisseriatheroleofglycaninteractionsincolonisationanddisease AT jenningsmichaelp sweetsideofthepathogenicneisseriatheroleofglycaninteractionsincolonisationanddisease AT seibkatel sweetsideofthepathogenicneisseriatheroleofglycaninteractionsincolonisationanddisease |