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Mutation of a chloroplast-targeting signal in Alternanthera mosaic virus TGB3 impairs cell-to-cell movement and eliminates long-distance virus movement.

Identifieur interne : 000600 ( Main/Exploration ); précédent : 000599; suivant : 000601

Mutation of a chloroplast-targeting signal in Alternanthera mosaic virus TGB3 impairs cell-to-cell movement and eliminates long-distance virus movement.

Auteurs : Hyoun-Sub Lim [États-Unis] ; Anna Maria Vaira [Italie, États-Unis] ; Hanhong Bae [Corée du Sud] ; Jennifer N. Bragg [États-Unis] ; Steven E. Ruzin [États-Unis] ; Gary R. Bauchan [États-Unis] ; Margaret M. Dienelt [États-Unis] ; Robert A. Owens [États-Unis] ; John Hammond [États-Unis]

Source :

RBID : pubmed:20392901

Descripteurs français

English descriptors

Abstract

Cell-to-cell movement of potexviruses requires coordinated action of the coat protein and triple gene block (TGB) proteins. The structural properties of Alternanthera mosaic virus (AltMV) TGB3 were examined by methods differentiating between signal peptides and transmembrane domains, and its subcellular localization was studied by Agrobacterium-mediated transient expression and confocal microscopy. Unlike potato virus X (PVX) TGB3, AltMV TGB3 was not associated with the endoplasmic reticulum, and accumulated preferentially in mesophyll cells. Deletion and site-specific mutagenesis revealed an internal signal VL(17,18) of TGB3 essential for chloroplast localization, and either deletion of the TGB3 start codon or alteration of the chloroplast-localization signal limited cell-to-cell movement to the epidermis, yielding a virus that was unable to move into the mesophyll layer. Overexpression of AltMV TGB3 from either AltMV or PVX infectious clones resulted in veinal necrosis and vesiculation at the chloroplast membrane, a cytopathology not observed in wild-type infections. The distinctive mesophyll and chloroplast localization of AltMV TGB3 highlights the critical role played by mesophyll targeting in virus long-distance movement within plants.

DOI: 10.1099/vir.0.019448-0
PubMed: 20392901


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Le document en format XML

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<term>Amino Acid Sequence (MeSH)</term>
<term>Chloroplasts (metabolism)</term>
<term>Genetic Vectors (MeSH)</term>
<term>Microscopy, Confocal (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Mutagenesis, Site-Directed (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Plant Diseases (virology)</term>
<term>Potexvirus (genetics)</term>
<term>Potexvirus (pathogenicity)</term>
<term>Protein Sorting Signals (MeSH)</term>
<term>Protein Transport (MeSH)</term>
<term>Rhizobium (genetics)</term>
<term>Sequence Alignment (MeSH)</term>
<term>Sequence Deletion (MeSH)</term>
<term>Tobacco (virology)</term>
<term>Viral Proteins (genetics)</term>
<term>Viral Proteins (metabolism)</term>
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<term>Alignement de séquences (MeSH)</term>
<term>Chloroplastes (métabolisme)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Délétion de séquence (MeSH)</term>
<term>Maladies des plantes (virologie)</term>
<term>Microscopie confocale (MeSH)</term>
<term>Mutagenèse dirigée (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Potexvirus (génétique)</term>
<term>Potexvirus (pathogénicité)</term>
<term>Protéines virales (génétique)</term>
<term>Protéines virales (métabolisme)</term>
<term>Rhizobium (génétique)</term>
<term>Signaux de triage des protéines (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
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<term>Potexvirus</term>
<term>Protéines virales</term>
<term>Rhizobium</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en">
<term>Chloroplasts</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr">
<term>Chloroplastes</term>
<term>Protéines virales</term>
</keywords>
<keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en">
<term>Potexvirus</term>
</keywords>
<keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr">
<term>Potexvirus</term>
</keywords>
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<term>Maladies des plantes</term>
<term>Tabac</term>
</keywords>
<keywords scheme="MESH" qualifier="virology" xml:lang="en">
<term>Plant Diseases</term>
<term>Tobacco</term>
</keywords>
<keywords scheme="MESH" xml:lang="en">
<term>Amino Acid Sequence</term>
<term>Genetic Vectors</term>
<term>Microscopy, Confocal</term>
<term>Molecular Sequence Data</term>
<term>Mutagenesis, Site-Directed</term>
<term>Mutation</term>
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<term>Sequence Alignment</term>
<term>Sequence Deletion</term>
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<term>Mutation</term>
<term>Signaux de triage des protéines</term>
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<div type="abstract" xml:lang="en">Cell-to-cell movement of potexviruses requires coordinated action of the coat protein and triple gene block (TGB) proteins. The structural properties of Alternanthera mosaic virus (AltMV) TGB3 were examined by methods differentiating between signal peptides and transmembrane domains, and its subcellular localization was studied by Agrobacterium-mediated transient expression and confocal microscopy. Unlike potato virus X (PVX) TGB3, AltMV TGB3 was not associated with the endoplasmic reticulum, and accumulated preferentially in mesophyll cells. Deletion and site-specific mutagenesis revealed an internal signal VL(17,18) of TGB3 essential for chloroplast localization, and either deletion of the TGB3 start codon or alteration of the chloroplast-localization signal limited cell-to-cell movement to the epidermis, yielding a virus that was unable to move into the mesophyll layer. Overexpression of AltMV TGB3 from either AltMV or PVX infectious clones resulted in veinal necrosis and vesiculation at the chloroplast membrane, a cytopathology not observed in wild-type infections. The distinctive mesophyll and chloroplast localization of AltMV TGB3 highlights the critical role played by mesophyll targeting in virus long-distance movement within plants.</div>
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<AbstractText>Cell-to-cell movement of potexviruses requires coordinated action of the coat protein and triple gene block (TGB) proteins. The structural properties of Alternanthera mosaic virus (AltMV) TGB3 were examined by methods differentiating between signal peptides and transmembrane domains, and its subcellular localization was studied by Agrobacterium-mediated transient expression and confocal microscopy. Unlike potato virus X (PVX) TGB3, AltMV TGB3 was not associated with the endoplasmic reticulum, and accumulated preferentially in mesophyll cells. Deletion and site-specific mutagenesis revealed an internal signal VL(17,18) of TGB3 essential for chloroplast localization, and either deletion of the TGB3 start codon or alteration of the chloroplast-localization signal limited cell-to-cell movement to the epidermis, yielding a virus that was unable to move into the mesophyll layer. Overexpression of AltMV TGB3 from either AltMV or PVX infectious clones resulted in veinal necrosis and vesiculation at the chloroplast membrane, a cytopathology not observed in wild-type infections. The distinctive mesophyll and chloroplast localization of AltMV TGB3 highlights the critical role played by mesophyll targeting in virus long-distance movement within plants.</AbstractText>
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<ForeName>Anna Maria</ForeName>
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