Electron-lucent inclusion bodies are structures specialized for aphid transmission of cauliflower mosaic virus

Cauliflower mosaic virus (CaMV) is transmitted by aphids. For acquisition by the vector, a transmissible complex must form, composed of the virus particle, the viral coat-associated protein P3 and the helper protein P2. However, the components of the transmissible complex are largely separated in infected plant cells: most P3 virions are confined in electron-dense inclusion bodies, whereas P2 is sequestered in electron-lucent inclusion bodies (elIBs). This spatial separation controls virus acquisition by favouring the binding of virus-free P2 to the vector first, rendering the vector competent for later uptake of P3 virions. Consequently, sequential acquisition of virus from different cells or tissues is possible, with important implications for the biology of CaMV transmission. CaMV strains Campbell and CM1841 contain a single amino acid mutation (G94R) in the helper protein P2, rendering them non-transmissible from plant to plant. However, the mutant P2-94 protein supports aphid transmission when expressed heterologously and supplied to P3-CaMV complexes in vitro. The non-transmissibility of P2-94 was re-examined in vivo and it is shown here that the non-transmissibility of this P2 mutant is not due to low accumulation levels in infected plants, as suggested previously, but more specifically to the failure to form elIBs within infected plant cells. This demonstrates that elIBs are complex viral structures specialized for aphid transmission and suggests that viral inclusion bodies other than viral factories, most often considered as 'garbage cans', can in fact exhibit specific functions.

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Main Authors: Khelifa, Mounia, Journou, Sandra, krishnan, Kalpana, Gargani, Daniel, Espérandiau, Pascal, Blanc, Stéphane, Drucker, Martin
Format: article biblioteca
Language:eng
Subjects:H20 - Maladies des plantes, caulimovirus mosaïque du chou fleur, transmission des maladies, Aphididae, vecteur de maladie, http://aims.fao.org/aos/agrovoc/c_35617, http://aims.fao.org/aos/agrovoc/c_2329, http://aims.fao.org/aos/agrovoc/c_525, http://aims.fao.org/aos/agrovoc/c_8164,
Online Access:http://agritrop.cirad.fr/542550/
http://agritrop.cirad.fr/542550/1/document_542550.pdf
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spelling dig-cirad-fr-5425502024-01-28T15:30:44Z http://agritrop.cirad.fr/542550/ http://agritrop.cirad.fr/542550/ Electron-lucent inclusion bodies are structures specialized for aphid transmission of cauliflower mosaic virus. Khelifa Mounia, Journou Sandra, krishnan Kalpana, Gargani Daniel, Espérandiau Pascal, Blanc Stéphane, Drucker Martin. 2007. Journal of General Virology, 88 (10) : 2872-2880.https://doi.org/10.1099/vir.0.83009-0 <https://doi.org/10.1099/vir.0.83009-0> Electron-lucent inclusion bodies are structures specialized for aphid transmission of cauliflower mosaic virus Khelifa, Mounia Journou, Sandra krishnan, Kalpana Gargani, Daniel Espérandiau, Pascal Blanc, Stéphane Drucker, Martin eng 2007 Journal of General Virology H20 - Maladies des plantes caulimovirus mosaïque du chou fleur transmission des maladies Aphididae vecteur de maladie http://aims.fao.org/aos/agrovoc/c_35617 http://aims.fao.org/aos/agrovoc/c_2329 http://aims.fao.org/aos/agrovoc/c_525 http://aims.fao.org/aos/agrovoc/c_8164 Cauliflower mosaic virus (CaMV) is transmitted by aphids. For acquisition by the vector, a transmissible complex must form, composed of the virus particle, the viral coat-associated protein P3 and the helper protein P2. However, the components of the transmissible complex are largely separated in infected plant cells: most P3 virions are confined in electron-dense inclusion bodies, whereas P2 is sequestered in electron-lucent inclusion bodies (elIBs). This spatial separation controls virus acquisition by favouring the binding of virus-free P2 to the vector first, rendering the vector competent for later uptake of P3 virions. Consequently, sequential acquisition of virus from different cells or tissues is possible, with important implications for the biology of CaMV transmission. CaMV strains Campbell and CM1841 contain a single amino acid mutation (G94R) in the helper protein P2, rendering them non-transmissible from plant to plant. However, the mutant P2-94 protein supports aphid transmission when expressed heterologously and supplied to P3-CaMV complexes in vitro. The non-transmissibility of P2-94 was re-examined in vivo and it is shown here that the non-transmissibility of this P2 mutant is not due to low accumulation levels in infected plants, as suggested previously, but more specifically to the failure to form elIBs within infected plant cells. This demonstrates that elIBs are complex viral structures specialized for aphid transmission and suggests that viral inclusion bodies other than viral factories, most often considered as 'garbage cans', can in fact exhibit specific functions. article info:eu-repo/semantics/article Journal Article info:eu-repo/semantics/publishedVersion http://agritrop.cirad.fr/542550/1/document_542550.pdf application/pdf Cirad license info:eu-repo/semantics/restrictedAccess https://agritrop.cirad.fr/mention_legale.html https://doi.org/10.1099/vir.0.83009-0 10.1099/vir.0.83009-0 info:eu-repo/semantics/altIdentifier/doi/10.1099/vir.0.83009-0 info:eu-repo/semantics/altIdentifier/purl/https://doi.org/10.1099/vir.0.83009-0
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 H20 - Maladies des plantes
caulimovirus mosaïque du chou fleur
transmission des maladies
Aphididae
vecteur de maladie
http://aims.fao.org/aos/agrovoc/c_35617
http://aims.fao.org/aos/agrovoc/c_2329
http://aims.fao.org/aos/agrovoc/c_525
http://aims.fao.org/aos/agrovoc/c_8164
H20 - Maladies des plantes
caulimovirus mosaïque du chou fleur
transmission des maladies
Aphididae
vecteur de maladie
http://aims.fao.org/aos/agrovoc/c_35617
http://aims.fao.org/aos/agrovoc/c_2329
http://aims.fao.org/aos/agrovoc/c_525
http://aims.fao.org/aos/agrovoc/c_8164
spellingShingle H20 - Maladies des plantes
caulimovirus mosaïque du chou fleur
transmission des maladies
Aphididae
vecteur de maladie
http://aims.fao.org/aos/agrovoc/c_35617
http://aims.fao.org/aos/agrovoc/c_2329
http://aims.fao.org/aos/agrovoc/c_525
http://aims.fao.org/aos/agrovoc/c_8164
H20 - Maladies des plantes
caulimovirus mosaïque du chou fleur
transmission des maladies
Aphididae
vecteur de maladie
http://aims.fao.org/aos/agrovoc/c_35617
http://aims.fao.org/aos/agrovoc/c_2329
http://aims.fao.org/aos/agrovoc/c_525
http://aims.fao.org/aos/agrovoc/c_8164
Khelifa, Mounia
Journou, Sandra
krishnan, Kalpana
Gargani, Daniel
Espérandiau, Pascal
Blanc, Stéphane
Drucker, Martin
Electron-lucent inclusion bodies are structures specialized for aphid transmission of cauliflower mosaic virus
description Cauliflower mosaic virus (CaMV) is transmitted by aphids. For acquisition by the vector, a transmissible complex must form, composed of the virus particle, the viral coat-associated protein P3 and the helper protein P2. However, the components of the transmissible complex are largely separated in infected plant cells: most P3 virions are confined in electron-dense inclusion bodies, whereas P2 is sequestered in electron-lucent inclusion bodies (elIBs). This spatial separation controls virus acquisition by favouring the binding of virus-free P2 to the vector first, rendering the vector competent for later uptake of P3 virions. Consequently, sequential acquisition of virus from different cells or tissues is possible, with important implications for the biology of CaMV transmission. CaMV strains Campbell and CM1841 contain a single amino acid mutation (G94R) in the helper protein P2, rendering them non-transmissible from plant to plant. However, the mutant P2-94 protein supports aphid transmission when expressed heterologously and supplied to P3-CaMV complexes in vitro. The non-transmissibility of P2-94 was re-examined in vivo and it is shown here that the non-transmissibility of this P2 mutant is not due to low accumulation levels in infected plants, as suggested previously, but more specifically to the failure to form elIBs within infected plant cells. This demonstrates that elIBs are complex viral structures specialized for aphid transmission and suggests that viral inclusion bodies other than viral factories, most often considered as 'garbage cans', can in fact exhibit specific functions.
format article
topic_facet H20 - Maladies des plantes
caulimovirus mosaïque du chou fleur
transmission des maladies
Aphididae
vecteur de maladie
http://aims.fao.org/aos/agrovoc/c_35617
http://aims.fao.org/aos/agrovoc/c_2329
http://aims.fao.org/aos/agrovoc/c_525
http://aims.fao.org/aos/agrovoc/c_8164
author Khelifa, Mounia
Journou, Sandra
krishnan, Kalpana
Gargani, Daniel
Espérandiau, Pascal
Blanc, Stéphane
Drucker, Martin
author_facet Khelifa, Mounia
Journou, Sandra
krishnan, Kalpana
Gargani, Daniel
Espérandiau, Pascal
Blanc, Stéphane
Drucker, Martin
author_sort Khelifa, Mounia
title Electron-lucent inclusion bodies are structures specialized for aphid transmission of cauliflower mosaic virus
title_short Electron-lucent inclusion bodies are structures specialized for aphid transmission of cauliflower mosaic virus
title_full Electron-lucent inclusion bodies are structures specialized for aphid transmission of cauliflower mosaic virus
title_fullStr Electron-lucent inclusion bodies are structures specialized for aphid transmission of cauliflower mosaic virus
title_full_unstemmed Electron-lucent inclusion bodies are structures specialized for aphid transmission of cauliflower mosaic virus
title_sort electron-lucent inclusion bodies are structures specialized for aphid transmission of cauliflower mosaic virus
url http://agritrop.cirad.fr/542550/
http://agritrop.cirad.fr/542550/1/document_542550.pdf
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AT krishnankalpana electronlucentinclusionbodiesarestructuresspecializedforaphidtransmissionofcauliflowermosaicvirus
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