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Comparative Analysis of Protein Glycosylation Pathways in Humans and the Fungal Pathogen Candida albicans

Protein glycosylation pathways are present in all kingdoms of life and are metabolic pathways found in all the life kingdoms. Despite sharing commonalities in their synthesis, glycans attached to glycoproteins have species-specific structures generated by the presence of different sets of enzymes an...

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Autores principales: Martínez-Duncker, Iván, Díaz-Jímenez, Diana F., Mora-Montes, Héctor M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4106090/
https://www.ncbi.nlm.nih.gov/pubmed/25104959
http://dx.doi.org/10.1155/2014/267497
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author Martínez-Duncker, Iván
Díaz-Jímenez, Diana F.
Mora-Montes, Héctor M.
author_facet Martínez-Duncker, Iván
Díaz-Jímenez, Diana F.
Mora-Montes, Héctor M.
author_sort Martínez-Duncker, Iván
collection PubMed
description Protein glycosylation pathways are present in all kingdoms of life and are metabolic pathways found in all the life kingdoms. Despite sharing commonalities in their synthesis, glycans attached to glycoproteins have species-specific structures generated by the presence of different sets of enzymes and acceptor substrates in each organism. In this review, we present a comparative analysis of the main glycosylation pathways shared by humans and the fungal pathogen Candida albicans: N-linked glycosylation, O-linked mannosylation and glycosylphosphatidylinositol-anchorage. The knowledge of similarities and divergences between these metabolic pathways could help find new pharmacological targets for C. albicans infection.
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spelling pubmed-41060902014-08-07 Comparative Analysis of Protein Glycosylation Pathways in Humans and the Fungal Pathogen Candida albicans Martínez-Duncker, Iván Díaz-Jímenez, Diana F. Mora-Montes, Héctor M. Int J Microbiol Review Article Protein glycosylation pathways are present in all kingdoms of life and are metabolic pathways found in all the life kingdoms. Despite sharing commonalities in their synthesis, glycans attached to glycoproteins have species-specific structures generated by the presence of different sets of enzymes and acceptor substrates in each organism. In this review, we present a comparative analysis of the main glycosylation pathways shared by humans and the fungal pathogen Candida albicans: N-linked glycosylation, O-linked mannosylation and glycosylphosphatidylinositol-anchorage. The knowledge of similarities and divergences between these metabolic pathways could help find new pharmacological targets for C. albicans infection. Hindawi Publishing Corporation 2014 2014-07-03 /pmc/articles/PMC4106090/ /pubmed/25104959 http://dx.doi.org/10.1155/2014/267497 Text en Copyright © 2014 Iván Martínez-Duncker et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Martínez-Duncker, Iván
Díaz-Jímenez, Diana F.
Mora-Montes, Héctor M.
Comparative Analysis of Protein Glycosylation Pathways in Humans and the Fungal Pathogen Candida albicans
title Comparative Analysis of Protein Glycosylation Pathways in Humans and the Fungal Pathogen Candida albicans
title_full Comparative Analysis of Protein Glycosylation Pathways in Humans and the Fungal Pathogen Candida albicans
title_fullStr Comparative Analysis of Protein Glycosylation Pathways in Humans and the Fungal Pathogen Candida albicans
title_full_unstemmed Comparative Analysis of Protein Glycosylation Pathways in Humans and the Fungal Pathogen Candida albicans
title_short Comparative Analysis of Protein Glycosylation Pathways in Humans and the Fungal Pathogen Candida albicans
title_sort comparative analysis of protein glycosylation pathways in humans and the fungal pathogen candida albicans
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4106090/
https://www.ncbi.nlm.nih.gov/pubmed/25104959
http://dx.doi.org/10.1155/2014/267497
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