Biochemical diversity in the Trypanosoma congolense trans-sialidase family.
Trans-sialidases are key enzymes in the life cycle of African trypanosomes in both, mammalian host and insect vector and have been associated with the disease trypanosomiasis, namely sleeping sickness and nagana. Besides the previously reported TconTS1, we have identified three additional active tra...
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ftdoajarticles:oai:doaj.org/article:d82a03f96b5d4150b42c0eeff23a4e8a 2023-05-15T15:09:35+02:00 Biochemical diversity in the Trypanosoma congolense trans-sialidase family. Thaddeus T Gbem Mario Waespy Bettina Hesse Frank Dietz Joel Smith Gloria D Chechet Jonathan A Nok Sørge Kelm 2013-01-01T00:00:00Z https://doi.org/10.1371/journal.pntd.0002549 https://doaj.org/article/d82a03f96b5d4150b42c0eeff23a4e8a EN eng Public Library of Science (PLoS) http://europepmc.org/articles/PMC3855035?pdf=render https://doaj.org/toc/1935-2727 https://doaj.org/toc/1935-2735 1935-2727 1935-2735 doi:10.1371/journal.pntd.0002549 https://doaj.org/article/d82a03f96b5d4150b42c0eeff23a4e8a PLoS Neglected Tropical Diseases, Vol 7, Iss 12, p e2549 (2013) Arctic medicine. Tropical medicine RC955-962 Public aspects of medicine RA1-1270 article 2013 ftdoajarticles https://doi.org/10.1371/journal.pntd.0002549 2023-01-08T01:28:20Z Trans-sialidases are key enzymes in the life cycle of African trypanosomes in both, mammalian host and insect vector and have been associated with the disease trypanosomiasis, namely sleeping sickness and nagana. Besides the previously reported TconTS1, we have identified three additional active trans-sialidases, TconTS2, TconTS3 and TconTS4, and three trans-sialidase like genes in Trypanosoma congolense. At least TconTS1, TconTS2 and TconTS4 are found in the bloodstream of infected animals. We have characterised the enzymatic properties of recombinant proteins expressed in eukaryotic fibroblasts using fetuin as model blood glycoprotein donor substrate. One of the recombinant trans-sialidases, TconTS2, had the highest specific activity reported thus far with very low sialidase activity. The active trans-sialidases share all the amino acids critical for the catalytic reaction with few variations in the predicted binding site for the leaving or acceptor glycan. However, these differences cannot explain the orders of magnitudes between their transfer activities, which must be due to other unidentified structural features of the proteins or substrates selectivity. Interestingly, the phylogenetic relationships between the lectin domains correlate with their specific trans-sialylation activities. This raises the question whether and how the lectin domains regulate the trans-sialidase reaction. The identification and enzymatic characterisation of the trans-sialidase family in T. congolense will contribute significantly towards the understanding of the roles of these enzymes in the pathogenesis of Animal African Trypanosomiasis. Article in Journal/Newspaper Arctic Directory of Open Access Journals: DOAJ Articles Arctic PLoS Neglected Tropical Diseases 7 12 e2549 |
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Open Polar |
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Directory of Open Access Journals: DOAJ Articles |
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English |
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Arctic medicine. Tropical medicine RC955-962 Public aspects of medicine RA1-1270 |
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Arctic medicine. Tropical medicine RC955-962 Public aspects of medicine RA1-1270 Thaddeus T Gbem Mario Waespy Bettina Hesse Frank Dietz Joel Smith Gloria D Chechet Jonathan A Nok Sørge Kelm Biochemical diversity in the Trypanosoma congolense trans-sialidase family. |
topic_facet |
Arctic medicine. Tropical medicine RC955-962 Public aspects of medicine RA1-1270 |
description |
Trans-sialidases are key enzymes in the life cycle of African trypanosomes in both, mammalian host and insect vector and have been associated with the disease trypanosomiasis, namely sleeping sickness and nagana. Besides the previously reported TconTS1, we have identified three additional active trans-sialidases, TconTS2, TconTS3 and TconTS4, and three trans-sialidase like genes in Trypanosoma congolense. At least TconTS1, TconTS2 and TconTS4 are found in the bloodstream of infected animals. We have characterised the enzymatic properties of recombinant proteins expressed in eukaryotic fibroblasts using fetuin as model blood glycoprotein donor substrate. One of the recombinant trans-sialidases, TconTS2, had the highest specific activity reported thus far with very low sialidase activity. The active trans-sialidases share all the amino acids critical for the catalytic reaction with few variations in the predicted binding site for the leaving or acceptor glycan. However, these differences cannot explain the orders of magnitudes between their transfer activities, which must be due to other unidentified structural features of the proteins or substrates selectivity. Interestingly, the phylogenetic relationships between the lectin domains correlate with their specific trans-sialylation activities. This raises the question whether and how the lectin domains regulate the trans-sialidase reaction. The identification and enzymatic characterisation of the trans-sialidase family in T. congolense will contribute significantly towards the understanding of the roles of these enzymes in the pathogenesis of Animal African Trypanosomiasis. |
format |
Article in Journal/Newspaper |
author |
Thaddeus T Gbem Mario Waespy Bettina Hesse Frank Dietz Joel Smith Gloria D Chechet Jonathan A Nok Sørge Kelm |
author_facet |
Thaddeus T Gbem Mario Waespy Bettina Hesse Frank Dietz Joel Smith Gloria D Chechet Jonathan A Nok Sørge Kelm |
author_sort |
Thaddeus T Gbem |
title |
Biochemical diversity in the Trypanosoma congolense trans-sialidase family. |
title_short |
Biochemical diversity in the Trypanosoma congolense trans-sialidase family. |
title_full |
Biochemical diversity in the Trypanosoma congolense trans-sialidase family. |
title_fullStr |
Biochemical diversity in the Trypanosoma congolense trans-sialidase family. |
title_full_unstemmed |
Biochemical diversity in the Trypanosoma congolense trans-sialidase family. |
title_sort |
biochemical diversity in the trypanosoma congolense trans-sialidase family. |
publisher |
Public Library of Science (PLoS) |
publishDate |
2013 |
url |
https://doi.org/10.1371/journal.pntd.0002549 https://doaj.org/article/d82a03f96b5d4150b42c0eeff23a4e8a |
geographic |
Arctic |
geographic_facet |
Arctic |
genre |
Arctic |
genre_facet |
Arctic |
op_source |
PLoS Neglected Tropical Diseases, Vol 7, Iss 12, p e2549 (2013) |
op_relation |
http://europepmc.org/articles/PMC3855035?pdf=render https://doaj.org/toc/1935-2727 https://doaj.org/toc/1935-2735 1935-2727 1935-2735 doi:10.1371/journal.pntd.0002549 https://doaj.org/article/d82a03f96b5d4150b42c0eeff23a4e8a |
op_doi |
https://doi.org/10.1371/journal.pntd.0002549 |
container_title |
PLoS Neglected Tropical Diseases |
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12 |
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e2549 |
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