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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Main Authors: 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
Format: article biblioteca
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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spelling 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
institution CIRAD FR
collection DSpace
country Francia
countrycode FR
component Bibliográfico
access En linea
databasecode dig-cirad-fr
tag biblioteca
region Europa del Oeste
libraryname Biblioteca del CIRAD Francia
language eng
topic 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
spellingShingle 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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