Ultrastructural and biochemical evidence of the trimeric nature of frog virus 3 (FV3) six-coordinated capsomers
Identifieur interne : 001592 ( Istex/Corpus ); précédent : 001591; suivant : 001593Ultrastructural and biochemical evidence of the trimeric nature of frog virus 3 (FV3) six-coordinated capsomers
Auteurs : F. Darcy-Tripier ; M. V. Nermut ; E. Brown ; H. Nonnenmacher ; J. BraunwaldSource :
- 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
Links to Exploration step
ISTEX:B651FCB4F56623A841D07EA1BF35573D37370A74Le document en format XML
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Nermut</name><affiliation><mods:affiliation>National Institute for Medical Research, Mill Hill, London NW7, United Kingdom</mods:affiliation></affiliation></author><author><name sortKey="Brown, E" sort="Brown, E" uniqKey="Brown E" first="E." last="Brown">E. Brown</name><affiliation><mods:affiliation>National Institute for Medical Research, Mill Hill, London NW7, United Kingdom</mods:affiliation></affiliation></author><author><name sortKey="Nonnenmacher, H" sort="Nonnenmacher, H" uniqKey="Nonnenmacher H" first="H." last="Nonnenmacher">H. Nonnenmacher</name><affiliation><mods:affiliation>Groupe de Recherches de l'INSERM (U74) et Laboratoire de Virologie de la Faculté de Médecine, Universit́e Louis Pasteur, 3 rue Koeberlé, Strasbourg 67000, France</mods:affiliation></affiliation></author><author><name sortKey="Braunwald, J" sort="Braunwald, J" uniqKey="Braunwald J" first="J." last="Braunwald">J. Braunwald</name><affiliation><mods:affiliation>To whom reprint requests should be sent.</mods:affiliation></affiliation><affiliation><mods:affiliation>Groupe de Recherches de l'INSERM (U74) et Laboratoire de Virologie de la Faculté de Médecine, Universit́e Louis Pasteur, 3 rue Koeberlé, Strasbourg 67000, France</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:B651FCB4F56623A841D07EA1BF35573D37370A74</idno><date when="1986" year="1986">1986</date><idno type="doi">10.1016/0042-6822(86)90085-1</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-KKWZN4M2-D/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">001592</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">001592</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">Ultrastructural and biochemical evidence of the trimeric nature of frog virus 3 (FV3) six-coordinated capsomers</title><author><name sortKey="Darcy Tripier, F" sort="Darcy Tripier, F" uniqKey="Darcy Tripier F" first="F." last="Darcy-Tripier">F. Darcy-Tripier</name><affiliation><mods:affiliation>Groupe de Recherches de l'INSERM (U74) et Laboratoire de Virologie de la Faculté de Médecine, Universit́e Louis Pasteur, 3 rue Koeberlé, Strasbourg 67000, France</mods:affiliation></affiliation><affiliation><mods:affiliation>1 Present address: Centre d'Immunologie et de Biologic Parasitaire, Institut Pasteur, 15 rue Camille Guérin, Lille 59019, Cédex, France</mods:affiliation></affiliation></author><author><name sortKey="Nermut, M V" sort="Nermut, M V" uniqKey="Nermut M" first="M. V." last="Nermut">M. V. Nermut</name><affiliation><mods:affiliation>National Institute for Medical Research, Mill Hill, London NW7, United Kingdom</mods:affiliation></affiliation></author><author><name sortKey="Brown, E" sort="Brown, E" uniqKey="Brown E" first="E." last="Brown">E. Brown</name><affiliation><mods:affiliation>National Institute for Medical Research, Mill Hill, London NW7, United Kingdom</mods:affiliation></affiliation></author><author><name sortKey="Nonnenmacher, H" sort="Nonnenmacher, H" uniqKey="Nonnenmacher H" first="H." last="Nonnenmacher">H. Nonnenmacher</name><affiliation><mods:affiliation>Groupe de Recherches de l'INSERM (U74) et Laboratoire de Virologie de la Faculté de Médecine, Universit́e Louis Pasteur, 3 rue Koeberlé, Strasbourg 67000, France</mods:affiliation></affiliation></author><author><name sortKey="Braunwald, J" sort="Braunwald, J" uniqKey="Braunwald J" first="J." last="Braunwald">J. Braunwald</name><affiliation><mods:affiliation>To whom reprint requests should be sent.</mods:affiliation></affiliation><affiliation><mods:affiliation>Groupe de Recherches de l'INSERM (U74) et Laboratoire de Virologie de la Faculté de Médecine, Universit́e Louis Pasteur, 3 rue Koeberlé, Strasbourg 67000, France</mods:affiliation></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><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>capsomers</json:string><json:string>polypeptide</json:string><json:string>capsid</json:string><json:string>capsomer</json:string><json:string>polyacrylamide</json:string><json:string>subunit</json:string><json:string>virology</json:string><json:string>adenovirus</json:string><json:string>trimeric</json:string><json:string>triton</json:string><json:string>molecular weight</json:string><json:string>micrographs</json:string><json:string>trimer</json:string><json:string>nermut</json:string><json:string>braunwald</json:string><json:string>icosahedral</json:string><json:string>frog virus</json:string><json:string>image processing</json:string><json:string>trimeric nature</json:string><json:string>optical diffraction</json:string><json:string>aberrant forms</json:string><json:string>replica</json:string><json:string>frog</json:string><json:string>electron microscopy</json:string><json:string>triangulation number</json:string><json:string>threefold symmetry orientation</json:string><json:string>negative staining</json:string><json:string>aberrant form</json:string><json:string>virus particle</json:string><json:string>quaternary structure</json:string><json:string>disulfide bonds</json:string><json:string>lactate dehydrogenase</json:string><json:string>nonreducing conditions</json:string><json:string>native capsomers</json:string><json:string>morphological units</json:string><json:string>central channel</json:string><json:string>adenovirus hexon</json:string><json:string>optical diffraction pattern</json:string><json:string>dose conditions</json:string><json:string>spherical subviral particles</json:string><json:string>chemical nature</json:string><json:string>interpolypeptide bonds</json:string><json:string>underfocused micrographs</json:string><json:string>molecular biology</json:string><json:string>density contour maps</json:string><json:string>electron microscope study</json:string><json:string>marker proteins</json:string><json:string>present study</json:string><json:string>bovine serum albumin</json:string><json:string>triangular mask</json:string><json:string>medical research</json:string><json:string>polypeptide composition</json:string><json:string>iridoviridae family</json:string><json:string>order spots</json:string><json:string>capsomers form</json:string><json:string>icosahedral form</json:string><json:string>polypeptide chains</json:string><json:string>triangular profiles</json:string><json:string>morphological subunits</json:string><json:string>faint band</json:string><json:string>structural polypeptides</json:string><json:string>several attempts</json:string><json:string>capsid subunits</json:string><json:string>water bath</json:string><json:string>single band</json:string><json:string>migration distance</json:string><json:string>polyacrylamide concentration</json:string><json:string>paper squares</json:string><json:string>structure units</json:string><json:string>hexagonal profiles</json:string><json:string>image analysis</json:string><json:string>icosahedral forms</json:string><json:string>major band</json:string><json:string>sodium silicotungstate</json:string><json:string>influenza virus</json:string><json:string>capsomeric structure</json:string><json:string>oligomeric proteins</json:string><json:string>disulfide bridges</json:string><json:string>virus particles</json:string><json:string>hexagonal</json:string></teeft></keywords><author><json:item><name>F. Darcy-Tripier</name><affiliations><json:string>Groupe de Recherches de l'INSERM (U74) et Laboratoire de Virologie de la Faculté de Médecine, Universit́e Louis Pasteur, 3 rue Koeberlé, Strasbourg 67000, France</json:string><json:string>1 Present address: Centre d'Immunologie et de Biologic Parasitaire, Institut Pasteur, 15 rue Camille Guérin, Lille 59019, Cédex, France</json:string></affiliations></json:item><json:item><name>M.V. Nermut</name><affiliations><json:string>National Institute for Medical Research, Mill Hill, London NW7, United Kingdom</json:string></affiliations></json:item><json:item><name>E. Brown</name><affiliations><json:string>National Institute for Medical Research, Mill Hill, London NW7, United Kingdom</json:string></affiliations></json:item><json:item><name>H. Nonnenmacher</name><affiliations><json:string>Groupe de Recherches de l'INSERM (U74) et Laboratoire de Virologie de la Faculté de Médecine, Universit́e Louis Pasteur, 3 rue Koeberlé, Strasbourg 67000, France</json:string></affiliations></json:item><json:item><name>J. Braunwald</name><affiliations><json:string>To whom reprint requests should be sent.</json:string><json:string>Groupe de Recherches de l'INSERM (U74) et Laboratoire de Virologie de la Faculté de Médecine, Universit́e Louis Pasteur, 3 rue Koeberlé, Strasbourg 67000, France</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-KKWZN4M2-D</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><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°).</abstract><qualityIndicators><score>8.583</score><pdfWordCount>4387</pdfWordCount><pdfCharCount>28478</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>11</pdfPageCount><pdfPageSize>504 x 720 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>183</abstractWordCount><abstractCharCount>1199</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>Ultrastructural and biochemical evidence of the trimeric nature of frog virus 3 (FV3) six-coordinated capsomers</title><pmid><json:string>2418581</json:string></pmid><pii><json:string>0042-6822(86)90085-1</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>Biological Macromolecules and Assemblies</title><language><json:string>unknown</json:string></language><volume>Vol. 1</volume><pages><first>337</first><last>385</last></pages><editor><json:item><name>F.A. Jurnak</name></json:item><json:item><name>A. McPherson</name></json:item></editor></serie><host><title>Virology</title><language><json:string>unknown</json:string></language><publicationDate>1986</publicationDate><issn><json:string>0042-6822</json:string></issn><pii><json:string>S0042-6822(00)X0314-5</json:string></pii><volume>149</volume><issue>1</issue><pages><first>44</first><last>54</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1986</json:string><json:string>5/5/0.7</json:string><json:string>3/2/35</json:string></date><geogName><json:string>Semliki</json:string></geogName><orgName><json:string>Laboratory of Molecular Biology</json:string><json:string>Matsushita Co., Japan</json:string><json:string>Academic Press, Inc</json:string><json:string>National Panasonic WV</json:string><json:string>National Institute for Medical Research</json:string><json:string>Biozentrum</json:string><json:string>Computing Department, NIMR, London, UK</json:string><json:string>Aeademie Press, Inc.</json:string><json:string>MRC Laboratory of Molecular Biology, Cambridge, UK</json:string><json:string>Pierce Chemical Co.</json:string><json:string>United Kingdom Received</json:string><json:string>British Council</json:string><json:string>EMBO</json:string></orgName><orgName_funder><json:string>British Council</json:string><json:string>EMBO</json:string></orgName_funder><orgName_provider></orgName_provider><persName><json:string>G. 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Williams</json:string></persName><placeName><json:string>Uppsala</json:string><json:string>Switzerland</json:string><json:string>Germany</json:string><json:string>UK</json:string><json:string>Canada</json:string><json:string>Darmstadt</json:string><json:string>London</json:string><json:string>Palo Alto</json:string><json:string>Liechtenstein</json:string><json:string>Basel</json:string><json:string>France</json:string><json:string>Quebec</json:string><json:string>Calif.</json:string><json:string>Cambridge</json:string><json:string>Sweden</json:string><json:string>Lille</json:string><json:string>Goldberg</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Darcy-Tripier et al, 1984</json:string><json:string>Braunwald et al., 1979</json:string><json:string>Burnett, 1984</json:string><json:string>Garoff, 1974</json:string><json:string>Thorun and Maurer (1971)</json:string><json:string>Aubertin et al., 1973</json:string><json:string>Mans and Novelli, 1961</json:string><json:string>Aubertin et al. (1980)</json:string><json:string>TripierDarcy et ah, 1982</json:string><json:string>Lomant and Fairbanks (1976)</json:string><json:string>Fenner and Gibbs, 1983</json:string><json:string>Boulanger and Puvion (1974)</json:string><json:string>Rayment et ab, 1982</json:string><json:string>Ichihashi, 1981</json:string><json:string>Tripier et aL, 1977</json:string><json:string>1969, 1970</json:string><json:string>DarcyTripier et al., 1984</json:string><json:string>Wrigley et al, 1983</json:string><json:string>Carrascosa et al, 1984</json:string><json:string>Reginster and Nermut, 1976</json:string><json:string>Boulanger and Puvion, 1974</json:string><json:string>Escaig, 1982</json:string><json:string>Tripier et al.</json:string><json:string>Kelly and Atkinson, 1975</json:string><json:string>Davies and Stark, 1970</json:string><json:string>Cerutti and Devauchelle, 1985</json:string><json:string>Caspar and Klug (1962)</json:string><json:string>Rakonczay et al., 1981</json:string><json:string>Laemmli, 1970</json:string><json:string>Darcy-Tripier et al., 1984</json:string><json:string>Bonner and Laskey, 1974</json:string><json:string>Nermut and Williams, 1977</json:string><json:string>Nermut and Perkins, 1979</json:string><json:string>Darcy-Tripier et aL, 1934</json:string><json:string>Takamatsu and Iso, 1982</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-KKWZN4M2-D</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - virology</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - biomedical research</json:string><json:string>3 - virology</json:string></scienceMetrix><scopus><json:string>1 - Life Sciences</json:string><json:string>2 - Immunology and Microbiology</json:string><json:string>3 - Virology</json:string></scopus><inist><json:string>1 - sciences appliquees, technologies et medecines</json:string><json:string>2 - sciences biologiques et medicales</json:string><json:string>3 - sciences biologiques fondamentales et appliquees. psychologie</json:string><json:string>4 - biophysique moleculaire</json:string></inist></categories><publicationDate>1986</publicationDate><copyrightDate>1986</copyrightDate><doi><json:string>10.1016/0042-6822(86)90085-1</json:string></doi><id>B651FCB4F56623A841D07EA1BF35573D37370A74</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-KKWZN4M2-D/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-KKWZN4M2-D/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-KKWZN4M2-D/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a">Ultrastructural and biochemical evidence of the trimeric nature of frog virus 3 (FV3) six-coordinated capsomers</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://scientific-publisher.data.istex.fr">ELSEVIER</publisher><availability><licence><p>elsevier</p></licence></availability><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M"></p><date>1986</date></publicationStmt><notesStmt><note type="research-article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</note><note type="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Ultrastructural and biochemical evidence of the trimeric nature of frog virus 3 (FV3) six-coordinated capsomers</title><author xml:id="author-0000"><persName><forename type="first">F.</forename><surname>Darcy-Tripier</surname></persName><affiliation>Groupe de Recherches de l'INSERM (U74) et Laboratoire de Virologie de la Faculté de Médecine, Universit́e Louis Pasteur, 3 rue Koeberlé, Strasbourg 67000, France</affiliation><affiliation>1 Present address: Centre d'Immunologie et de Biologic Parasitaire, Institut Pasteur, 15 rue Camille Guérin, Lille 59019, Cédex, France</affiliation></author><author xml:id="author-0001"><persName><forename type="first">M.V.</forename><surname>Nermut</surname></persName><affiliation>National Institute for Medical Research, Mill Hill, London NW7, United Kingdom</affiliation></author><author xml:id="author-0002"><persName><forename type="first">E.</forename><surname>Brown</surname></persName><affiliation>National Institute for Medical Research, Mill Hill, London NW7, United Kingdom</affiliation></author><author xml:id="author-0003"><persName><forename type="first">H.</forename><surname>Nonnenmacher</surname></persName><affiliation>Groupe de Recherches de l'INSERM (U74) et Laboratoire de Virologie de la Faculté de Médecine, Universit́e Louis Pasteur, 3 rue Koeberlé, Strasbourg 67000, France</affiliation></author><author xml:id="author-0004"><persName><forename type="first">J.</forename><surname>Braunwald</surname></persName><affiliation>To whom reprint requests should be sent.</affiliation><affiliation>Groupe de Recherches de l'INSERM (U74) et Laboratoire de Virologie de la Faculté de Médecine, Universit́e Louis Pasteur, 3 rue Koeberlé, Strasbourg 67000, France</affiliation></author><idno type="istex">B651FCB4F56623A841D07EA1BF35573D37370A74</idno><idno type="ark">ark:/67375/6H6-KKWZN4M2-D</idno><idno type="DOI">10.1016/0042-6822(86)90085-1</idno><idno type="PII">0042-6822(86)90085-1</idno></analytic><monogr><title level="j">Virology</title><title level="j" type="abbrev">YVIRO</title><idno type="pISSN">0042-6822</idno><idno type="PII">S0042-6822(00)X0314-5</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="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></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1986</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>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°).</p></abstract></profileDesc><revisionDesc><change when="1986">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-KKWZN4M2-D/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>YVIRO</jid><aid>86900851</aid><ce:pii>0042-6822(86)90085-1</ce:pii><ce:doi>10.1016/0042-6822(86)90085-1</ce:doi><ce:copyright type="unknown" year="1986"></ce:copyright></item-info><head><ce:title>Ultrastructural and biochemical evidence of the trimeric nature of frog virus 3 (FV3) six-coordinated capsomers</ce:title><ce:author-group><ce:author><ce:given-name>F.</ce:given-name><ce:surname>Darcy-Tripier</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref><ce:cross-ref refid="FN1"><ce:sup>1</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>M.V.</ce:given-name><ce:surname>Nermut</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>†</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>E.</ce:given-name><ce:surname>Brown</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>†</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>H.</ce:given-name><ce:surname>Nonnenmacher</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>J.</ce:given-name><ce:surname>Braunwald</ce:surname><ce:cross-ref refid="COR1"><ce:sup>2</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>Groupe de Recherches de l'INSERM (U74) et Laboratoire de Virologie de la Faculté de Médecine, Universit́e Louis Pasteur, 3 rue Koeberlé, Strasbourg 67000, France</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>National Institute for Medical Research, Mill Hill, London NW7, United Kingdom</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>2</ce:label><ce:text>To whom reprint requests should be sent.</ce:text></ce:correspondence><ce:footnote id="FN1"><ce:label>1</ce:label><ce:note-para>Present address: Centre d'Immunologie et de Biologic Parasitaire, Institut Pasteur, 15 rue Camille Guérin, Lille 59019, Cédex, France</ce:note-para></ce:footnote></ce:author-group><ce:date-received day="12" month="6" year="1985"></ce:date-received><ce:date-accepted day="23" month="10" year="1985"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>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 (<ce:cross-ref refid="BIB11">Darcy-Tripier <ce:italic>et al.</ce:italic>, 1984</ce:cross-ref>). 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 <ce:italic>T</ce:italic> = 133 (<ce:italic>h</ce:italic> = 9, <ce:italic>k</ce:italic> = 4, 18°).</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Ultrastructural and biochemical evidence of the trimeric nature of frog virus 3 (FV3) six-coordinated capsomers</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Ultrastructural and biochemical evidence of the trimeric nature of frog virus 3 (FV3) six-coordinated capsomers</title></titleInfo><name type="personal"><namePart type="given">F.</namePart><namePart type="family">Darcy-Tripier</namePart><affiliation>Groupe de Recherches de l'INSERM (U74) et Laboratoire de Virologie de la Faculté de Médecine, Universit́e Louis Pasteur, 3 rue Koeberlé, Strasbourg 67000, France</affiliation><affiliation>1 Present address: Centre d'Immunologie et de Biologic Parasitaire, Institut Pasteur, 15 rue Camille Guérin, Lille 59019, Cédex, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">M.V.</namePart><namePart type="family">Nermut</namePart><affiliation>National Institute for Medical Research, Mill Hill, London NW7, United Kingdom</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">E.</namePart><namePart type="family">Brown</namePart><affiliation>National Institute for Medical Research, Mill Hill, London NW7, United Kingdom</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">H.</namePart><namePart type="family">Nonnenmacher</namePart><affiliation>Groupe de Recherches de l'INSERM (U74) et Laboratoire de Virologie de la Faculté de Médecine, Universit́e Louis Pasteur, 3 rue Koeberlé, Strasbourg 67000, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">J.</namePart><namePart type="family">Braunwald</namePart><affiliation>To whom reprint requests should be sent.</affiliation><affiliation>Groupe de Recherches de l'INSERM (U74) et Laboratoire de Virologie de la Faculté de Médecine, Universit́e Louis Pasteur, 3 rue Koeberlé, Strasbourg 67000, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1986</dateIssued><copyrightDate encoding="w3cdtf">1986</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract 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°).</abstract><relatedItem type="host"><titleInfo><title>Virology</title></titleInfo><titleInfo type="abbreviated"><title>YVIRO</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1986</dateIssued></originInfo><identifier type="ISSN">0042-6822</identifier><identifier type="PII">S0042-6822(00)X0314-5</identifier><part><date>1986</date><detail type="volume"><number>149</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="issue-pages"><start>1</start><end>137</end></extent><extent unit="pages"><start>44</start><end>54</end></extent></part></relatedItem><identifier type="istex">B651FCB4F56623A841D07EA1BF35573D37370A74</identifier><identifier type="ark">ark:/67375/6H6-KKWZN4M2-D</identifier><identifier type="DOI">10.1016/0042-6822(86)90085-1</identifier><identifier type="PII">0042-6822(86)90085-1</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-KKWZN4M2-D/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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