Serveur d'exploration sur les interactions arbre microorganisme

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Single amino acid changes in the 6K1-CI region can promote the alternative adaptation of Prunus- and Nicotiana-propagated Plum pox virus C isolates to either host.

Identifieur interne : 000195 ( Main/Exploration ); précédent : 000194; suivant : 000196

Single amino acid changes in the 6K1-CI region can promote the alternative adaptation of Prunus- and Nicotiana-propagated Plum pox virus C isolates to either host.

Auteurs : María Calvo ; Tadeusz Malinowski ; Juan Antonio García

Source :

RBID : pubmed:24200075

Descripteurs français

English descriptors

Abstract

Plum pox virus (PPV) C is one of the less common PPV strains and specifically infects cherry trees in nature. Making use of two PPV-C isolates that display different pathogenicity features, i.e., SwCMp, which had been adapted to Nicotiana species, and BY101, which had been isolated from cherry rootstock L2 (Prunus lannesiana) and propagated only in cherry species, we have generated two infective full-length cDNA clones in order to determine which viral factors are involved in the adaptation to each host. According to our results, the C-P3(PIPO)/6K1/N-CI (cylindrical inclusion) region contains overlapping but not coincident viral determinants involved in symptoms development, local viral amplification, and systemic movement capacity. Amino acid changes in this region promoting the adaptation to N. benthamiana or P. avium have trade-off effects in the alternative host. In both cases, adaptation can be achieved through single amino acid changes in the NIapro protease recognition motif between 6K1 and CI or in nearby sequences. Thus, we hypothesize that the potyvirus polyprotein processing could depend on specific host factors and the adaptation of PPV-C isolates to particular hosts relies on a fine regulation of the proteolytic cleavage of the 6K1-CI junction.

DOI: 10.1094/MPMI-08-13-0242-R
PubMed: 24200075


Affiliations:


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Le document en format XML

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<name sortKey="Calvo, Maria" sort="Calvo, Maria" uniqKey="Calvo M" first="María" last="Calvo">María Calvo</name>
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<name sortKey="Malinowski, Tadeusz" sort="Malinowski, Tadeusz" uniqKey="Malinowski T" first="Tadeusz" last="Malinowski">Tadeusz Malinowski</name>
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<term>Host Specificity (MeSH)</term>
<term>Host-Pathogen Interactions (MeSH)</term>
<term>Plant Diseases (virology)</term>
<term>Plant Leaves (virology)</term>
<term>Plum Pox Virus (genetics)</term>
<term>Plum Pox Virus (pathogenicity)</term>
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<term>Maladies des plantes (virologie)</term>
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<term>Protéines virales (métabolisme)</term>
<term>Prunus (virologie)</term>
<term>Spécificité d'hôte (MeSH)</term>
<term>Substitution d'acide aminé (MeSH)</term>
<term>Tabac (virologie)</term>
<term>Virus de la variole du prunier (génétique)</term>
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<term>ADN complémentaire</term>
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<div type="abstract" xml:lang="en">Plum pox virus (PPV) C is one of the less common PPV strains and specifically infects cherry trees in nature. Making use of two PPV-C isolates that display different pathogenicity features, i.e., SwCMp, which had been adapted to Nicotiana species, and BY101, which had been isolated from cherry rootstock L2 (Prunus lannesiana) and propagated only in cherry species, we have generated two infective full-length cDNA clones in order to determine which viral factors are involved in the adaptation to each host. According to our results, the C-P3(PIPO)/6K1/N-CI (cylindrical inclusion) region contains overlapping but not coincident viral determinants involved in symptoms development, local viral amplification, and systemic movement capacity. Amino acid changes in this region promoting the adaptation to N. benthamiana or P. avium have trade-off effects in the alternative host. In both cases, adaptation can be achieved through single amino acid changes in the NIapro protease recognition motif between 6K1 and CI or in nearby sequences. Thus, we hypothesize that the potyvirus polyprotein processing could depend on specific host factors and the adaptation of PPV-C isolates to particular hosts relies on a fine regulation of the proteolytic cleavage of the 6K1-CI junction. </div>
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