Ultrastructural and biochemical evidence of the trimeric nature of frog virus 3 (FV3) six-coordinated capsomers
Identifieur interne : 000417 ( France/Analysis ); précédent : 000416; suivant : 000418Ultrastructural and biochemical evidence of the trimeric nature of frog virus 3 (FV3) six-coordinated capsomers
Auteurs : F. Darcy-Tripier [France] ; M. V. Nermut [Royaume-Uni] ; E. Brown [Royaume-Uni] ; H. Nonnenmacher [France] ; J. Braunwald [France]Source :
- Virology [ 0042-6822 ] ; 1986.
English descriptors
- Teeft :
- Aberrant form, Aberrant forms, Adenovirus, Adenovirus hexon, Bovine serum albumin, Braunwald, Capsid, Capsid subunits, Capsomer, Capsomeric structure, Capsomers, Capsomers form, Central channel, Chemical nature, Density contour maps, Disulfide bonds, Disulfide bridges, Dose conditions, Electron microscope study, Electron microscopy, Faint band, Frog, Frog virus, Hexagonal, Hexagonal profiles, Icosahedral, Icosahedral form, Icosahedral forms, Image analysis, Image processing, Influenza virus, Interpolypeptide bonds, Iridoviridae family, Lactate dehydrogenase, Major band, Marker proteins, Medical research, Micrographs, Migration distance, Molecular biology, Molecular weight, Morphological subunits, Morphological units, Native capsomers, Negative staining, Nermut, Nonreducing conditions, Oligomeric proteins, Optical diffraction, Optical diffraction pattern, Order spots, Paper squares, Polyacrylamide, Polyacrylamide concentration, Polypeptide, Polypeptide chains, Polypeptide composition, Present study, Quaternary structure, Replica, Several attempts, Single band, Sodium silicotungstate, Spherical subviral particles, Structural polypeptides, Structure units, Subunit, Threefold symmetry orientation, Triangular mask, Triangular profiles, Triangulation number, Trimer, Trimeric, Trimeric nature, Triton, Underfocused micrographs, Virology, Virus particle, Virus particles, Water bath.
Abstract
Abstract: Image analysis of freeze-etch replicas of cylindrical aberrant forms of FV3 provided evidence for three morphological subunits protruding from the six-coordinated capsomers. Negatively stained capsomers displayed both triangular and hexagonal profiles which suggests that their innermost portion is pseudohexagonal. Images from underfocused micrographs of capsomers are indicative of a central channel. The trimeric nature of the capsomer has been established by electrophoresis in the presence of Triton X-100, which showed that the molecular weight of the nondiesociated capsomer is about 140,000 whereas that of the polypeptide itself is 48,000. This trimeric association does not occur via disulfide bonds, and inside the capsomers there are no free amino groups accessible to the usual bifunctional reagents. Thus, the chemical nature of the interpolypeptide bonds inside the trimers is still unknown. We have previously estimated the triangulation number (T) of FV3 to be 147 or 133 (Darcy-Tripier et al., 1984). The present study, using optical diffraction of the facets of FV3, allowed a better determination of the angle of skewness and is in favor of T = 133 (h = 9, k = 4, 18°).
Url:
DOI: 10.1016/0042-6822(86)90085-1
Affiliations:
- France, Royaume-Uni
- Alsace (région administrative), Angleterre, Grand Est, Grand Londres, Hauts-de-France, Nord-Pas-de-Calais
- Cédex, Londres
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ISTEX:B651FCB4F56623A841D07EA1BF35573D37370A74Le document en format XML
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Braunwald</name><affiliation></affiliation><affiliation wicri:level="3"><country xml:lang="fr">France</country><wicri:regionArea>Groupe de Recherches de l'INSERM (U74) et Laboratoire de Virologie de la Faculté de Médecine, Universit́e Louis Pasteur, 3 rue Koeberlé, Strasbourg 67000</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Alsace (région administrative)</region></placeName></affiliation></author></analytic><monogr></monogr><series><title level="j">Virology</title><title level="j" type="abbrev">YVIRO</title><idno type="ISSN">0042-6822</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1986">1986</date><biblScope unit="volume">149</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="44">44</biblScope><biblScope unit="page" to="54">54</biblScope></imprint><idno type="ISSN">0042-6822</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0042-6822</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Aberrant form</term><term>Aberrant forms</term><term>Adenovirus</term><term>Adenovirus hexon</term><term>Bovine serum albumin</term><term>Braunwald</term><term>Capsid</term><term>Capsid subunits</term><term>Capsomer</term><term>Capsomeric structure</term><term>Capsomers</term><term>Capsomers form</term><term>Central channel</term><term>Chemical nature</term><term>Density contour maps</term><term>Disulfide bonds</term><term>Disulfide bridges</term><term>Dose conditions</term><term>Electron microscope study</term><term>Electron microscopy</term><term>Faint band</term><term>Frog</term><term>Frog virus</term><term>Hexagonal</term><term>Hexagonal profiles</term><term>Icosahedral</term><term>Icosahedral form</term><term>Icosahedral forms</term><term>Image analysis</term><term>Image processing</term><term>Influenza virus</term><term>Interpolypeptide bonds</term><term>Iridoviridae family</term><term>Lactate dehydrogenase</term><term>Major band</term><term>Marker proteins</term><term>Medical research</term><term>Micrographs</term><term>Migration distance</term><term>Molecular biology</term><term>Molecular weight</term><term>Morphological subunits</term><term>Morphological units</term><term>Native capsomers</term><term>Negative staining</term><term>Nermut</term><term>Nonreducing conditions</term><term>Oligomeric proteins</term><term>Optical diffraction</term><term>Optical diffraction pattern</term><term>Order spots</term><term>Paper squares</term><term>Polyacrylamide</term><term>Polyacrylamide concentration</term><term>Polypeptide</term><term>Polypeptide chains</term><term>Polypeptide composition</term><term>Present study</term><term>Quaternary structure</term><term>Replica</term><term>Several attempts</term><term>Single band</term><term>Sodium silicotungstate</term><term>Spherical subviral particles</term><term>Structural polypeptides</term><term>Structure units</term><term>Subunit</term><term>Threefold symmetry orientation</term><term>Triangular mask</term><term>Triangular profiles</term><term>Triangulation number</term><term>Trimer</term><term>Trimeric</term><term>Trimeric nature</term><term>Triton</term><term>Underfocused micrographs</term><term>Virology</term><term>Virus particle</term><term>Virus particles</term><term>Water bath</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Image analysis of freeze-etch replicas of cylindrical aberrant forms of FV3 provided evidence for three morphological subunits protruding from the six-coordinated capsomers. Negatively stained capsomers displayed both triangular and hexagonal profiles which suggests that their innermost portion is pseudohexagonal. Images from underfocused micrographs of capsomers are indicative of a central channel. The trimeric nature of the capsomer has been established by electrophoresis in the presence of Triton X-100, which showed that the molecular weight of the nondiesociated capsomer is about 140,000 whereas that of the polypeptide itself is 48,000. This trimeric association does not occur via disulfide bonds, and inside the capsomers there are no free amino groups accessible to the usual bifunctional reagents. Thus, the chemical nature of the interpolypeptide bonds inside the trimers is still unknown. We have previously estimated the triangulation number (T) of FV3 to be 147 or 133 (Darcy-Tripier et al., 1984). The present study, using optical diffraction of the facets of FV3, allowed a better determination of the angle of skewness and is in favor of T = 133 (h = 9, k = 4, 18°).</div></front></TEI><affiliations><list><country><li>France</li><li>Royaume-Uni</li></country><region><li>Alsace (région administrative)</li><li>Angleterre</li><li>Grand Est</li><li>Grand Londres</li><li>Hauts-de-France</li><li>Nord-Pas-de-Calais</li></region><settlement><li>Cédex</li><li>Londres</li></settlement></list><tree><country name="France"><region name="Grand Est"><name sortKey="Darcy Tripier, F" sort="Darcy Tripier, F" uniqKey="Darcy Tripier F" first="F." last="Darcy-Tripier">F. Darcy-Tripier</name></region><name sortKey="Braunwald, J" sort="Braunwald, J" uniqKey="Braunwald J" first="J." last="Braunwald">J. Braunwald</name><name sortKey="Darcy Tripier, F" sort="Darcy Tripier, F" uniqKey="Darcy Tripier F" first="F." last="Darcy-Tripier">F. Darcy-Tripier</name><name sortKey="Nonnenmacher, H" sort="Nonnenmacher, H" uniqKey="Nonnenmacher H" first="H." last="Nonnenmacher">H. Nonnenmacher</name></country><country name="Royaume-Uni"><region name="Angleterre"><name sortKey="Nermut, M V" sort="Nermut, M V" uniqKey="Nermut M" first="M. V." last="Nermut">M. V. Nermut</name></region><name sortKey="Brown, E" sort="Brown, E" uniqKey="Brown E" first="E." last="Brown">E. Brown</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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