Exocytosis and protein secretion in Trypanosoma
Human African trypanosomiasis is a lethal disease caused by the extracellular parasite Trypanosoma brucei. The proteins secreted by T. brucei inhibit the maturation of dendritic cells and their ability to induce lymphocytic allogenic responses. To better understand the pathogenic process, we combined different approaches to characterize these secreted proteins. Overall, 444 proteins were identified using mass spectrometry, the largest parasite secretome described to date. Functional analysis of these proteins revealed a strong bias toward folding and degradation processes and to a lesser extent toward nucleotide metabolism. These features were shared by different strains of T. brucei, but distinguished the secretome from published T. brucei whole proteome or glycosome. In addition, several proteins had not been previously described in Trypanosoma and some constitute novel potential therapeutic targets or diagnostic markers. Interestingly, a high proportion of these secreted proteins are known to have alternative roles once secreted. Furthermore, bioinformatic analysis showed that a significant proportion of proteins in the secretome lack transit peptide and are probably not secreted through the classical sorting pathway. Membrane vesicles from secretion buffer and infested rat serum were purified on sucrose gradient and electron microscopy pictures have shown 50- to 100-nm vesicles budding from the coated plasma membrane. Mass spectrometry confirmed the presence of Trypanosoma proteins in these microvesicles, showing that an active exocytosis might occur beyond the flagellar pocket. This study brings out several unexpected features of the secreted proteins and opens novel perspectives concerning the survival strategy of Trypanosoma as well as possible ways to control the disease. In addition, concordant lines of evidence support the original hypothesis of the involvement of microvesicle-like bodies in the survival strategy allowing Trypanosoma to exchange proteins at least between parasites and/or to manipulate the host immune system.
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Subjects: | L73 - Maladies des animaux, protéine microbienne, Trypanosoma brucei, http://aims.fao.org/aos/agrovoc/c_12537, http://aims.fao.org/aos/agrovoc/c_27400, |
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dig-cirad-fr-5566772024-01-28T18:37:53Z http://agritrop.cirad.fr/556677/ http://agritrop.cirad.fr/556677/ Exocytosis and protein secretion in Trypanosoma. Geiger Anne, Hirtz Christophe, Bécue Thierry, Bellard Eric, Centeno Delphine, Gargani Daniel, Rossignol Michel, Cuny Gérard, Peltier Jean-Benoît. 2010. BMC Microbiology, 10 (20), 17 p.https://doi.org/10.1186/1471-2180-10-20 <https://doi.org/10.1186/1471-2180-10-20> Exocytosis and protein secretion in Trypanosoma Geiger, Anne Hirtz, Christophe Bécue, Thierry Bellard, Eric Centeno, Delphine Gargani, Daniel Rossignol, Michel Cuny, Gérard Peltier, Jean-Benoît eng 2010 BMC Microbiology L73 - Maladies des animaux protéine microbienne Trypanosoma brucei http://aims.fao.org/aos/agrovoc/c_12537 http://aims.fao.org/aos/agrovoc/c_27400 Human African trypanosomiasis is a lethal disease caused by the extracellular parasite Trypanosoma brucei. The proteins secreted by T. brucei inhibit the maturation of dendritic cells and their ability to induce lymphocytic allogenic responses. To better understand the pathogenic process, we combined different approaches to characterize these secreted proteins. Overall, 444 proteins were identified using mass spectrometry, the largest parasite secretome described to date. Functional analysis of these proteins revealed a strong bias toward folding and degradation processes and to a lesser extent toward nucleotide metabolism. These features were shared by different strains of T. brucei, but distinguished the secretome from published T. brucei whole proteome or glycosome. In addition, several proteins had not been previously described in Trypanosoma and some constitute novel potential therapeutic targets or diagnostic markers. Interestingly, a high proportion of these secreted proteins are known to have alternative roles once secreted. Furthermore, bioinformatic analysis showed that a significant proportion of proteins in the secretome lack transit peptide and are probably not secreted through the classical sorting pathway. Membrane vesicles from secretion buffer and infested rat serum were purified on sucrose gradient and electron microscopy pictures have shown 50- to 100-nm vesicles budding from the coated plasma membrane. Mass spectrometry confirmed the presence of Trypanosoma proteins in these microvesicles, showing that an active exocytosis might occur beyond the flagellar pocket. This study brings out several unexpected features of the secreted proteins and opens novel perspectives concerning the survival strategy of Trypanosoma as well as possible ways to control the disease. In addition, concordant lines of evidence support the original hypothesis of the involvement of microvesicle-like bodies in the survival strategy allowing Trypanosoma to exchange proteins at least between parasites and/or to manipulate the host immune system. article info:eu-repo/semantics/article Journal Article info:eu-repo/semantics/publishedVersion http://agritrop.cirad.fr/556677/1/document_556677.pdf application/pdf Cirad license info:eu-repo/semantics/openAccess https://agritrop.cirad.fr/mention_legale.html https://doi.org/10.1186/1471-2180-10-20 10.1186/1471-2180-10-20 info:eu-repo/semantics/altIdentifier/doi/10.1186/1471-2180-10-20 info:eu-repo/semantics/altIdentifier/purl/https://doi.org/10.1186/1471-2180-10-20 |
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L73 - Maladies des animaux protéine microbienne Trypanosoma brucei http://aims.fao.org/aos/agrovoc/c_12537 http://aims.fao.org/aos/agrovoc/c_27400 L73 - Maladies des animaux protéine microbienne Trypanosoma brucei http://aims.fao.org/aos/agrovoc/c_12537 http://aims.fao.org/aos/agrovoc/c_27400 |
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L73 - Maladies des animaux protéine microbienne Trypanosoma brucei http://aims.fao.org/aos/agrovoc/c_12537 http://aims.fao.org/aos/agrovoc/c_27400 L73 - Maladies des animaux protéine microbienne Trypanosoma brucei http://aims.fao.org/aos/agrovoc/c_12537 http://aims.fao.org/aos/agrovoc/c_27400 Geiger, Anne Hirtz, Christophe Bécue, Thierry Bellard, Eric Centeno, Delphine Gargani, Daniel Rossignol, Michel Cuny, Gérard Peltier, Jean-Benoît Exocytosis and protein secretion in Trypanosoma |
description |
Human African trypanosomiasis is a lethal disease caused by the extracellular parasite Trypanosoma brucei. The proteins secreted by T. brucei inhibit the maturation of dendritic cells and their ability to induce lymphocytic allogenic responses. To better understand the pathogenic process, we combined different approaches to characterize these secreted proteins. Overall, 444 proteins were identified using mass spectrometry, the largest parasite secretome described to date. Functional analysis of these proteins revealed a strong bias toward folding and degradation processes and to a lesser extent toward nucleotide metabolism. These features were shared by different strains of T. brucei, but distinguished the secretome from published T. brucei whole proteome or glycosome. In addition, several proteins had not been previously described in Trypanosoma and some constitute novel potential therapeutic targets or diagnostic markers. Interestingly, a high proportion of these secreted proteins are known to have alternative roles once secreted. Furthermore, bioinformatic analysis showed that a significant proportion of proteins in the secretome lack transit peptide and are probably not secreted through the classical sorting pathway. Membrane vesicles from secretion buffer and infested rat serum were purified on sucrose gradient and electron microscopy pictures have shown 50- to 100-nm vesicles budding from the coated plasma membrane. Mass spectrometry confirmed the presence of Trypanosoma proteins in these microvesicles, showing that an active exocytosis might occur beyond the flagellar pocket. This study brings out several unexpected features of the secreted proteins and opens novel perspectives concerning the survival strategy of Trypanosoma as well as possible ways to control the disease. In addition, concordant lines of evidence support the original hypothesis of the involvement of microvesicle-like bodies in the survival strategy allowing Trypanosoma to exchange proteins at least between parasites and/or to manipulate the host immune system. |
format |
article |
topic_facet |
L73 - Maladies des animaux protéine microbienne Trypanosoma brucei http://aims.fao.org/aos/agrovoc/c_12537 http://aims.fao.org/aos/agrovoc/c_27400 |
author |
Geiger, Anne Hirtz, Christophe Bécue, Thierry Bellard, Eric Centeno, Delphine Gargani, Daniel Rossignol, Michel Cuny, Gérard Peltier, Jean-Benoît |
author_facet |
Geiger, Anne Hirtz, Christophe Bécue, Thierry Bellard, Eric Centeno, Delphine Gargani, Daniel Rossignol, Michel Cuny, Gérard Peltier, Jean-Benoît |
author_sort |
Geiger, Anne |
title |
Exocytosis and protein secretion in Trypanosoma |
title_short |
Exocytosis and protein secretion in Trypanosoma |
title_full |
Exocytosis and protein secretion in Trypanosoma |
title_fullStr |
Exocytosis and protein secretion in Trypanosoma |
title_full_unstemmed |
Exocytosis and protein secretion in Trypanosoma |
title_sort |
exocytosis and protein secretion in trypanosoma |
url |
http://agritrop.cirad.fr/556677/ http://agritrop.cirad.fr/556677/1/document_556677.pdf |
work_keys_str_mv |
AT geigeranne exocytosisandproteinsecretionintrypanosoma AT hirtzchristophe exocytosisandproteinsecretionintrypanosoma AT becuethierry exocytosisandproteinsecretionintrypanosoma AT bellarderic exocytosisandproteinsecretionintrypanosoma AT centenodelphine exocytosisandproteinsecretionintrypanosoma AT garganidaniel exocytosisandproteinsecretionintrypanosoma AT rossignolmichel exocytosisandproteinsecretionintrypanosoma AT cunygerard exocytosisandproteinsecretionintrypanosoma AT peltierjeanbenoit exocytosisandproteinsecretionintrypanosoma |
_version_ |
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