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Common and unique features of glycosylation and glycosyltransferases in African trypanosomes

Eukaryotic protein glycosylation is mediated by glycosyl- and oligosaccharyl-transferases. Here, we describe how African trypanosomes exhibit both evolutionary conservation and significant divergence compared with other eukaryotes in how they synthesise their glycoproteins. The kinetoplastid parasit...

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Autores principales: Duncan, Samuel M., Ferguson, Michael A.J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9472816/
https://www.ncbi.nlm.nih.gov/pubmed/36066312
http://dx.doi.org/10.1042/BCJ20210778
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author Duncan, Samuel M.
Ferguson, Michael A.J.
author_facet Duncan, Samuel M.
Ferguson, Michael A.J.
author_sort Duncan, Samuel M.
collection PubMed
description Eukaryotic protein glycosylation is mediated by glycosyl- and oligosaccharyl-transferases. Here, we describe how African trypanosomes exhibit both evolutionary conservation and significant divergence compared with other eukaryotes in how they synthesise their glycoproteins. The kinetoplastid parasites have conserved components of the dolichol-cycle and oligosaccharyltransferases (OSTs) of protein N-glycosylation, and of glycosylphosphatidylinositol (GPI) anchor biosynthesis and transfer to protein. However, some components are missing, and they process and decorate their N-glycans and GPI anchors in unique ways. To do so, they appear to have evolved a distinct and functionally flexible glycosyltransferases (GT) family, the GT67 family, from an ancestral eukaryotic β3GT gene. The expansion and/or loss of GT67 genes appears to be dependent on parasite biology. Some appear to correlate with the obligate passage of parasites through an insect vector, suggesting they were acquired through GT67 gene expansion to assist insect vector (tsetse fly) colonisation. Others appear to have been lost in species that subsequently adopted contaminative transmission. We also highlight the recent discovery of a novel and essential GT11 family of kinetoplastid parasite fucosyltransferases that are uniquely localised to the mitochondria of Trypanosoma brucei and Leishmania major. The origins of these kinetoplastid FUT1 genes, and additional putative mitochondrial GT genes, are discussed.
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spelling pubmed-94728162022-09-19 Common and unique features of glycosylation and glycosyltransferases in African trypanosomes Duncan, Samuel M. Ferguson, Michael A.J. Biochem J Biochemical Techniques & Resources Eukaryotic protein glycosylation is mediated by glycosyl- and oligosaccharyl-transferases. Here, we describe how African trypanosomes exhibit both evolutionary conservation and significant divergence compared with other eukaryotes in how they synthesise their glycoproteins. The kinetoplastid parasites have conserved components of the dolichol-cycle and oligosaccharyltransferases (OSTs) of protein N-glycosylation, and of glycosylphosphatidylinositol (GPI) anchor biosynthesis and transfer to protein. However, some components are missing, and they process and decorate their N-glycans and GPI anchors in unique ways. To do so, they appear to have evolved a distinct and functionally flexible glycosyltransferases (GT) family, the GT67 family, from an ancestral eukaryotic β3GT gene. The expansion and/or loss of GT67 genes appears to be dependent on parasite biology. Some appear to correlate with the obligate passage of parasites through an insect vector, suggesting they were acquired through GT67 gene expansion to assist insect vector (tsetse fly) colonisation. Others appear to have been lost in species that subsequently adopted contaminative transmission. We also highlight the recent discovery of a novel and essential GT11 family of kinetoplastid parasite fucosyltransferases that are uniquely localised to the mitochondria of Trypanosoma brucei and Leishmania major. The origins of these kinetoplastid FUT1 genes, and additional putative mitochondrial GT genes, are discussed. Portland Press Ltd. 2022-09-06 /pmc/articles/PMC9472816/ /pubmed/36066312 http://dx.doi.org/10.1042/BCJ20210778 Text en © 2022 The Author(s) https://creativecommons.org/licenses/by/4.0/This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY) (https://creativecommons.org/licenses/by/4.0/) . Open access for this article was enabled by the participation of the University of Dundee in an all-inclusive Read & Publish agreement with Portland Press and the Biochemical Society under a transformative agreement with JISC.
spellingShingle Biochemical Techniques & Resources
Duncan, Samuel M.
Ferguson, Michael A.J.
Common and unique features of glycosylation and glycosyltransferases in African trypanosomes
title Common and unique features of glycosylation and glycosyltransferases in African trypanosomes
title_full Common and unique features of glycosylation and glycosyltransferases in African trypanosomes
title_fullStr Common and unique features of glycosylation and glycosyltransferases in African trypanosomes
title_full_unstemmed Common and unique features of glycosylation and glycosyltransferases in African trypanosomes
title_short Common and unique features of glycosylation and glycosyltransferases in African trypanosomes
title_sort common and unique features of glycosylation and glycosyltransferases in african trypanosomes
topic Biochemical Techniques & Resources
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9472816/
https://www.ncbi.nlm.nih.gov/pubmed/36066312
http://dx.doi.org/10.1042/BCJ20210778
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