MersV1, Main, Exploration, bibRecord, 004894

pH-dependent solubility shift of rubella virus capsid protein

Identifieur interne : 004894 ( Main/Exploration ); précédent : 004893; suivant : 004895

pH-dependent solubility shift of rubella virus capsid protein

Auteurs : Christoph A. Mauracher [Canada] ; Shirley Gillam [Canada] ; Robert Shukin [Canada] ; Aubrey J. Tingle [Canada]

Source :

Virology [ 0042-6822 ] ; 1991.

RBID : ISTEX:0575254A4DC543A91D561D36FC6DE4AD4909B3C0

English descriptors

Teeft :
- Academic press, Acidic conditions, Amino acid residues, Capsid, Capsid gene, Capsid protein, Capsid uncoating, Capsomere, Capsomere structure, Cell lysate, Cleavage product, Detergent pellets, Detergent phase, Endolysosomal vesicle, Intact capsomere, Intrinsic property, Large arrow, Membrane fusion, Nucleic acids, Other togaviridae, Pellet, Primary antibody, Rubella, Rubella virus, Short communications, Signal peptide, Solubility, Solubility shift, Structural change, Sucrose, Tissue culture, Treatment groups, Triton, Uncoating, Viral, Viral envelope, Viral membrane, Western blot analysis.

Abstract

Abstract: The mechanism of capsid uncoating in rubella virus and other togaviridae is not well understood. This study presents data which suggest that rubella virus capsid undergoes a structural change from having hydrophilic to hydrophobic properties, between pH 5 and 5.5. Such a conformational change would allow capsid uncoating to occur within the lysosome, allowing RNA penetration to occur upon fusion of the viral envelope with the limiting membrane of the lysosome.

Url:

https://api.istex.fr/ark:/67375/6H6-T8W5ST06-C/fulltext.pdf

DOI: 10.1016/0042-6822(91)90916-Y

Affiliations:

Canada

Links toward previous steps (curation, corpus...)

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to stream Main, to step Curation: 004894

Le document en format XML

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<author><name sortKey="Tingle, Aubrey J" sort="Tingle, Aubrey J" uniqKey="Tingle A" first="Aubrey J." last="Tingle">Aubrey J. Tingle</name>
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<term>Capsid gene</term>
<term>Capsid protein</term>
<term>Capsid uncoating</term>
<term>Capsomere</term>
<term>Capsomere structure</term>
<term>Cell lysate</term>
<term>Cleavage product</term>
<term>Detergent pellets</term>
<term>Detergent phase</term>
<term>Endolysosomal vesicle</term>
<term>Intact capsomere</term>
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<term>Membrane fusion</term>
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<term>Rubella</term>
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<term>Short communications</term>
<term>Signal peptide</term>
<term>Solubility</term>
<term>Solubility shift</term>
<term>Structural change</term>
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<term>Tissue culture</term>
<term>Treatment groups</term>
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<term>Uncoating</term>
<term>Viral</term>
<term>Viral envelope</term>
<term>Viral membrane</term>
<term>Western blot analysis</term>
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<front><div type="abstract" xml:lang="en">Abstract: The mechanism of capsid uncoating in rubella virus and other togaviridae is not well understood. This study presents data which suggest that rubella virus capsid undergoes a structural change from having hydrophilic to hydrophobic properties, between pH 5 and 5.5. Such a conformational change would allow capsid uncoating to occur within the lysosome, allowing RNA penetration to occur upon fusion of the viral envelope with the limiting membrane of the lysosome.</div>
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<tree><country name="Canada"><noRegion><name sortKey="Mauracher, Christoph A" sort="Mauracher, Christoph A" uniqKey="Mauracher C" first="Christoph A." last="Mauracher">Christoph A. Mauracher</name>
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<name sortKey="Gillam, Shirley" sort="Gillam, Shirley" uniqKey="Gillam S" first="Shirley" last="Gillam">Shirley Gillam</name>
<name sortKey="Shukin, Robert" sort="Shukin, Robert" uniqKey="Shukin R" first="Robert" last="Shukin">Robert Shukin</name>
<name sortKey="Tingle, Aubrey J" sort="Tingle, Aubrey J" uniqKey="Tingle A" first="Aubrey J." last="Tingle">Aubrey J. Tingle</name>
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pH-dependent solubility shift of rubella virus capsid protein

pH-dependent solubility shift of rubella virus capsid protein

Source :

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri