Proteo-Trancriptomic analyses reveal a large expansion of metalloprotease-like proteins in atypical venom vesicles of the wasp Meteorus pulchricornis (Braconidae)
Meteorus pulchricornis (Ichneumonoidea, Braconidae) is an endoparasitoid wasp of lepidopteran caterpillars. Its parasitic success relies on vesicles (named M. pulchricornis Virus-Like Particles or MpVLPs) that are synthesized in the venom gland and injected into the parasitoid host along with the venom during oviposition. In order to define the content and understand the biogenesis of these atypical vesicles, we performed a transcriptome analysis of the venom gland and a proteomic analysis of the venom and purified MpVLPs. About half of the MpVLPs and soluble venom proteins identified were unknown and no similarity with any known viral sequence was found. However, MpVLPs contained a large number of proteins labelled as metalloproteinases while the most abundant protein family in the soluble venom was that of proteins containing the Domain of Unknown Function DUF-4803. The high number of these proteins identified suggests that a large expansion of these two protein families occurred in M. pulchricornis. Therefore, although the exact mechanism of MpVLPs formation remains to be elucidated, these vesicles appear to be “metalloproteinase bombs” that may have several physiological roles in the host including modifying the functions of its immune cells. The role of DUF4803 proteins, also present in the venom of other braconids, remains to be clarified.
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Language: | eng |
Subjects: | Meteorus, Braconidae, venin, parasitoïde, Vespidae, Helicoverpa armigera, fonction physiologique, http://aims.fao.org/aos/agrovoc/c_29843, http://aims.fao.org/aos/agrovoc/c_29830, http://aims.fao.org/aos/agrovoc/c_8187, http://aims.fao.org/aos/agrovoc/c_34070, http://aims.fao.org/aos/agrovoc/c_8303, http://aims.fao.org/aos/agrovoc/c_30255, http://aims.fao.org/aos/agrovoc/c_5837, http://aims.fao.org/aos/agrovoc/c_3081, |
Online Access: | http://agritrop.cirad.fr/608248/ http://agritrop.cirad.fr/608248/1/Proteo-Trancriptomic%20Analyses%20Reveal%20a%20Large%20Expansion%20of%20Metalloprotease-Like%20Proteins%20in%20Atypical%20Venom%20Vesicles%20of%20the%20Wasp%20Meteorus%20pulchricornis%20%28Braconidae%29_20210719.pdf |
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dig-cirad-fr-6082482024-02-12T05:32:12Z http://agritrop.cirad.fr/608248/ http://agritrop.cirad.fr/608248/ Proteo-Trancriptomic analyses reveal a large expansion of metalloprotease-like proteins in atypical venom vesicles of the wasp Meteorus pulchricornis (Braconidae). Gatti Jean-Luc, Belghazi Maya, Legeai Fabrice, Ravallec Marc, Frayssinet Marie, Robin Stéphanie, Aboubakar Souna Djibril, Srinivasan Ramasamy, Tamo Manuele, Poirié Marylène, Volkoff Anne-Nathalie. 2021. Toxins, 13 (7), n.spéc. Evolution, Genomics and Proteomics of Venom:502, 36 p.https://doi.org/10.3390/toxins13070502 <https://doi.org/10.3390/toxins13070502> Proteo-Trancriptomic analyses reveal a large expansion of metalloprotease-like proteins in atypical venom vesicles of the wasp Meteorus pulchricornis (Braconidae) Gatti, Jean-Luc Belghazi, Maya Legeai, Fabrice Ravallec, Marc Frayssinet, Marie Robin, Stéphanie Aboubakar Souna, Djibril Srinivasan, Ramasamy Tamo, Manuele Poirié, Marylène Volkoff, Anne-Nathalie eng 2021 Toxins Meteorus Braconidae venin parasitoïde Vespidae Helicoverpa armigera fonction physiologique http://aims.fao.org/aos/agrovoc/c_29843 http://aims.fao.org/aos/agrovoc/c_29830 http://aims.fao.org/aos/agrovoc/c_8187 http://aims.fao.org/aos/agrovoc/c_34070 http://aims.fao.org/aos/agrovoc/c_8303 http://aims.fao.org/aos/agrovoc/c_30255 http://aims.fao.org/aos/agrovoc/c_5837 France http://aims.fao.org/aos/agrovoc/c_3081 Meteorus pulchricornis (Ichneumonoidea, Braconidae) is an endoparasitoid wasp of lepidopteran caterpillars. Its parasitic success relies on vesicles (named M. pulchricornis Virus-Like Particles or MpVLPs) that are synthesized in the venom gland and injected into the parasitoid host along with the venom during oviposition. In order to define the content and understand the biogenesis of these atypical vesicles, we performed a transcriptome analysis of the venom gland and a proteomic analysis of the venom and purified MpVLPs. About half of the MpVLPs and soluble venom proteins identified were unknown and no similarity with any known viral sequence was found. However, MpVLPs contained a large number of proteins labelled as metalloproteinases while the most abundant protein family in the soluble venom was that of proteins containing the Domain of Unknown Function DUF-4803. The high number of these proteins identified suggests that a large expansion of these two protein families occurred in M. pulchricornis. Therefore, although the exact mechanism of MpVLPs formation remains to be elucidated, these vesicles appear to be “metalloproteinase bombs” that may have several physiological roles in the host including modifying the functions of its immune cells. The role of DUF4803 proteins, also present in the venom of other braconids, remains to be clarified. article info:eu-repo/semantics/article Journal Article info:eu-repo/semantics/publishedVersion http://agritrop.cirad.fr/608248/1/Proteo-Trancriptomic%20Analyses%20Reveal%20a%20Large%20Expansion%20of%20Metalloprotease-Like%20Proteins%20in%20Atypical%20Venom%20Vesicles%20of%20the%20Wasp%20Meteorus%20pulchricornis%20%28Braconidae%29_20210719.pdf text cc_by info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by/4.0/ https://doi.org/10.3390/toxins13070502 10.3390/toxins13070502 info:eu-repo/semantics/altIdentifier/doi/10.3390/toxins13070502 info:eu-repo/semantics/altIdentifier/purl/https://doi.org/10.3390/toxins13070502 info:eu-repo/semantics/dataset/purl/https://www.ncbi.nlm.nih.gov/bioproject/PRJNA733444/ info:eu-repo/semantics/dataset/purl/https://www.ncbi.nlm.nih.gov/bioproject/PRJNA734452 info:eu-repo/semantics/reference/purl/https://proteomecentral.proteomexchange.org/ info:eu-repo/grantAgreement///ANR-12-ADAP-0001//(FRA) Adaptation en lutte biologique - Génomique des populations de parasitoïdes/ABC - PaPoGen info:eu-repo/grantAgreement///ANR-11-LABX-0028//(FRA) Réseau d'Innovation sur les Voies de Signalisation en Sciences de la Vie/SIGNALIFE info:eu-repo/grantAgreement///ANR-15-IDEX-0001//(FRA) Idex UCA JEDI/UCA JEDI |
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Meteorus Braconidae venin parasitoïde Vespidae Helicoverpa armigera fonction physiologique http://aims.fao.org/aos/agrovoc/c_29843 http://aims.fao.org/aos/agrovoc/c_29830 http://aims.fao.org/aos/agrovoc/c_8187 http://aims.fao.org/aos/agrovoc/c_34070 http://aims.fao.org/aos/agrovoc/c_8303 http://aims.fao.org/aos/agrovoc/c_30255 http://aims.fao.org/aos/agrovoc/c_5837 http://aims.fao.org/aos/agrovoc/c_3081 Meteorus Braconidae venin parasitoïde Vespidae Helicoverpa armigera fonction physiologique http://aims.fao.org/aos/agrovoc/c_29843 http://aims.fao.org/aos/agrovoc/c_29830 http://aims.fao.org/aos/agrovoc/c_8187 http://aims.fao.org/aos/agrovoc/c_34070 http://aims.fao.org/aos/agrovoc/c_8303 http://aims.fao.org/aos/agrovoc/c_30255 http://aims.fao.org/aos/agrovoc/c_5837 http://aims.fao.org/aos/agrovoc/c_3081 |
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Meteorus Braconidae venin parasitoïde Vespidae Helicoverpa armigera fonction physiologique http://aims.fao.org/aos/agrovoc/c_29843 http://aims.fao.org/aos/agrovoc/c_29830 http://aims.fao.org/aos/agrovoc/c_8187 http://aims.fao.org/aos/agrovoc/c_34070 http://aims.fao.org/aos/agrovoc/c_8303 http://aims.fao.org/aos/agrovoc/c_30255 http://aims.fao.org/aos/agrovoc/c_5837 http://aims.fao.org/aos/agrovoc/c_3081 Meteorus Braconidae venin parasitoïde Vespidae Helicoverpa armigera fonction physiologique http://aims.fao.org/aos/agrovoc/c_29843 http://aims.fao.org/aos/agrovoc/c_29830 http://aims.fao.org/aos/agrovoc/c_8187 http://aims.fao.org/aos/agrovoc/c_34070 http://aims.fao.org/aos/agrovoc/c_8303 http://aims.fao.org/aos/agrovoc/c_30255 http://aims.fao.org/aos/agrovoc/c_5837 http://aims.fao.org/aos/agrovoc/c_3081 Gatti, Jean-Luc Belghazi, Maya Legeai, Fabrice Ravallec, Marc Frayssinet, Marie Robin, Stéphanie Aboubakar Souna, Djibril Srinivasan, Ramasamy Tamo, Manuele Poirié, Marylène Volkoff, Anne-Nathalie Proteo-Trancriptomic analyses reveal a large expansion of metalloprotease-like proteins in atypical venom vesicles of the wasp Meteorus pulchricornis (Braconidae) |
description |
Meteorus pulchricornis (Ichneumonoidea, Braconidae) is an endoparasitoid wasp of lepidopteran caterpillars. Its parasitic success relies on vesicles (named M. pulchricornis Virus-Like Particles or MpVLPs) that are synthesized in the venom gland and injected into the parasitoid host along with the venom during oviposition. In order to define the content and understand the biogenesis of these atypical vesicles, we performed a transcriptome analysis of the venom gland and a proteomic analysis of the venom and purified MpVLPs. About half of the MpVLPs and soluble venom proteins identified were unknown and no similarity with any known viral sequence was found. However, MpVLPs contained a large number of proteins labelled as metalloproteinases while the most abundant protein family in the soluble venom was that of proteins containing the Domain of Unknown Function DUF-4803. The high number of these proteins identified suggests that a large expansion of these two protein families occurred in M. pulchricornis. Therefore, although the exact mechanism of MpVLPs formation remains to be elucidated, these vesicles appear to be “metalloproteinase bombs” that may have several physiological roles in the host including modifying the functions of its immune cells. The role of DUF4803 proteins, also present in the venom of other braconids, remains to be clarified. |
format |
article |
topic_facet |
Meteorus Braconidae venin parasitoïde Vespidae Helicoverpa armigera fonction physiologique http://aims.fao.org/aos/agrovoc/c_29843 http://aims.fao.org/aos/agrovoc/c_29830 http://aims.fao.org/aos/agrovoc/c_8187 http://aims.fao.org/aos/agrovoc/c_34070 http://aims.fao.org/aos/agrovoc/c_8303 http://aims.fao.org/aos/agrovoc/c_30255 http://aims.fao.org/aos/agrovoc/c_5837 http://aims.fao.org/aos/agrovoc/c_3081 |
author |
Gatti, Jean-Luc Belghazi, Maya Legeai, Fabrice Ravallec, Marc Frayssinet, Marie Robin, Stéphanie Aboubakar Souna, Djibril Srinivasan, Ramasamy Tamo, Manuele Poirié, Marylène Volkoff, Anne-Nathalie |
author_facet |
Gatti, Jean-Luc Belghazi, Maya Legeai, Fabrice Ravallec, Marc Frayssinet, Marie Robin, Stéphanie Aboubakar Souna, Djibril Srinivasan, Ramasamy Tamo, Manuele Poirié, Marylène Volkoff, Anne-Nathalie |
author_sort |
Gatti, Jean-Luc |
title |
Proteo-Trancriptomic analyses reveal a large expansion of metalloprotease-like proteins in atypical venom vesicles of the wasp Meteorus pulchricornis (Braconidae) |
title_short |
Proteo-Trancriptomic analyses reveal a large expansion of metalloprotease-like proteins in atypical venom vesicles of the wasp Meteorus pulchricornis (Braconidae) |
title_full |
Proteo-Trancriptomic analyses reveal a large expansion of metalloprotease-like proteins in atypical venom vesicles of the wasp Meteorus pulchricornis (Braconidae) |
title_fullStr |
Proteo-Trancriptomic analyses reveal a large expansion of metalloprotease-like proteins in atypical venom vesicles of the wasp Meteorus pulchricornis (Braconidae) |
title_full_unstemmed |
Proteo-Trancriptomic analyses reveal a large expansion of metalloprotease-like proteins in atypical venom vesicles of the wasp Meteorus pulchricornis (Braconidae) |
title_sort |
proteo-trancriptomic analyses reveal a large expansion of metalloprotease-like proteins in atypical venom vesicles of the wasp meteorus pulchricornis (braconidae) |
url |
http://agritrop.cirad.fr/608248/ http://agritrop.cirad.fr/608248/1/Proteo-Trancriptomic%20Analyses%20Reveal%20a%20Large%20Expansion%20of%20Metalloprotease-Like%20Proteins%20in%20Atypical%20Venom%20Vesicles%20of%20the%20Wasp%20Meteorus%20pulchricornis%20%28Braconidae%29_20210719.pdf |
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