Ribonucleocapsid formation of severe acute respiratory syndrome coronavirus through molecular action of the N-terminal domain of N protein
Identifieur interne : 000377 ( PascalFrancis/Corpus ); précédent : 000376; suivant : 000378Ribonucleocapsid formation of severe acute respiratory syndrome coronavirus through molecular action of the N-terminal domain of N protein
Auteurs : KUMAR SINGH SAIKATENDU ; Jeremiah S. Joseph ; Vanitha Subramanian ; Benjamin W. Neuman ; Michael J. Buchmeier ; Raymond C. Stevens ; Peter KuhnSource :
- Journal of virology [ 0022-538X ] ; 2007.
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- Pascal (Inist)
English descriptors
Abstract
Conserved among all coronaviruses are four structural proteins: the matrix (M), small envelope (E), and spike (S) proteins that are embedded in the viral membrane and the nucleocapsid phosphoprotein (N), which exists in a ribonucleoprotein complex in the lumen. The N-terminal domain of coronaviral N proteins (N-NTD) provides a scaffold for RNA binding, while the C-terminal domain (N-CTD) mainly acts as oligomerization modules during assembly. The C terminus of the N protein anchors it to the viral membrane by associating with M protein. We characterized the structures of N-NTD from severe acute respiratory syndrome coronavirus (SARS-CoV) in two crystal forms, at 1.17 Å (monoclinic) and at 1.85 Å (cubic), respectively, resolved by molecular replacement using the homologous avian infectious bronchitis virus (IBV) structure. Flexible loops in the solution structure of SARS-CoV N-NTD are now shown to be well ordered around the β-sheet core. The functionally important positively charged β-hairpin protrudes out of the core, is oriented similarly to that in the IBV N-NTD, and is involved in crystal packing in the monoclinic form. In the cubic form, the monomers form trimeric units that stack in a helical array. Comparison of crystal packing of SARS-CoV and IBV N-NTDs suggests a common mode of RNA recognition, but they probably associate differently in vivo during the formation of the ribonucleoprotein complex. Electrostatic potential distribution on the surface of homology models of related coronaviral N-NTDs suggests that they use different modes of both RNA recognition and oligomeric assembly, perhaps explaining why their nucleocapsids have different morphologies.
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| NO : | PASCAL 07-0211072 INIST |
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| ET : | Ribonucleocapsid formation of severe acute respiratory syndrome coronavirus through molecular action of the N-terminal domain of N protein |
| AU : | KUMAR SINGH SAIKATENDU; JOSEPH (Jeremiah S.); SUBRAMANIAN (Vanitha); NEUMAN (Benjamin W.); BUCHMEIER (Michael J.); STEVENS (Raymond C.); KUHN (Peter) |
| AF : | Department of Cell Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road/La Jolla, California 92037/Etats-Unis (1 aut., 2 aut., 3 aut., 7 aut.); Department of Molecular Integrative Neurosciences, The Scripps Research Institute, 10550 N. Torrey Pines Road/La Jolla, California 92037/Etats-Unis (4 aut., 5 aut.); Department of Molecular Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road/La Jolla, California 92037/Etats-Unis (6 aut.) |
| DT : | Publication en série; Niveau analytique |
| SO : | Journal of virology; ISSN 0022-538X; Etats-Unis; Da. 2007; Vol. 81; No. 8; Pp. 3913-3921; Bibl. 62 ref. |
| LA : | Anglais |
| EA : | Conserved among all coronaviruses are four structural proteins: the matrix (M), small envelope (E), and spike (S) proteins that are embedded in the viral membrane and the nucleocapsid phosphoprotein (N), which exists in a ribonucleoprotein complex in the lumen. The N-terminal domain of coronaviral N proteins (N-NTD) provides a scaffold for RNA binding, while the C-terminal domain (N-CTD) mainly acts as oligomerization modules during assembly. The C terminus of the N protein anchors it to the viral membrane by associating with M protein. We characterized the structures of N-NTD from severe acute respiratory syndrome coronavirus (SARS-CoV) in two crystal forms, at 1.17 Å (monoclinic) and at 1.85 Å (cubic), respectively, resolved by molecular replacement using the homologous avian infectious bronchitis virus (IBV) structure. Flexible loops in the solution structure of SARS-CoV N-NTD are now shown to be well ordered around the β-sheet core. The functionally important positively charged β-hairpin protrudes out of the core, is oriented similarly to that in the IBV N-NTD, and is involved in crystal packing in the monoclinic form. In the cubic form, the monomers form trimeric units that stack in a helical array. Comparison of crystal packing of SARS-CoV and IBV N-NTDs suggests a common mode of RNA recognition, but they probably associate differently in vivo during the formation of the ribonucleoprotein complex. Electrostatic potential distribution on the surface of homology models of related coronaviral N-NTDs suggests that they use different modes of both RNA recognition and oligomeric assembly, perhaps explaining why their nucleocapsids have different morphologies. |
| CC : | 002A05C10 |
| FD : | Coronavirus; Protéine; Virologie; Syndrome respiratoire aigu sévère |
| FG : | Coronaviridae; Nidovirales; Virus; Appareil respiratoire pathologie; Virose; Infection; Poumon pathologie |
| ED : | Coronavirus; Protein; Virology; Severe acute respiratory syndrome |
| EG : | Coronaviridae; Nidovirales; Virus; Respiratory disease; Viral disease; Infection; Lung disease |
| SD : | Coronavirus; Proteína; Virología; Síndrome respiratorio agudo severo |
| LO : | INIST-13592.354000143390310240 |
| ID : | 07-0211072 |
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Torrey Pines Road</s1><s2>La Jolla, California 92037</s2><s3>USA</s3><sZ>6 aut.</sZ></inist:fA14></affiliation></author><author><name sortKey="Kuhn, Peter" sort="Kuhn, Peter" uniqKey="Kuhn P" first="Peter" last="Kuhn">Peter Kuhn</name><affiliation><inist:fA14 i1="01"><s1>Department of Cell Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road</s1><s2>La Jolla, California 92037</s2><s3>USA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>7 aut.</sZ></inist:fA14></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">INIST</idno><idno type="inist">07-0211072</idno><date when="2007">2007</date><idno type="stanalyst">PASCAL 07-0211072 INIST</idno><idno type="RBID">Pascal:07-0211072</idno><idno type="wicri:Area/PascalFrancis/Corpus">000377</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a">Ribonucleocapsid formation of severe acute respiratory syndrome coronavirus through molecular action of the N-terminal domain of N protein</title><author><name sortKey="Kumar Singh Saikatendu" sort="Kumar Singh Saikatendu" uniqKey="Kumar Singh Saikatendu" last="Kumar Singh Saikatendu">KUMAR SINGH SAIKATENDU</name><affiliation><inist:fA14 i1="01"><s1>Department of Cell Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road</s1><s2>La Jolla, California 92037</s2><s3>USA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>7 aut.</sZ></inist:fA14></affiliation></author><author><name sortKey="Joseph, Jeremiah S" sort="Joseph, Jeremiah S" uniqKey="Joseph J" first="Jeremiah S." last="Joseph">Jeremiah S. Joseph</name><affiliation><inist:fA14 i1="01"><s1>Department of Cell Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road</s1><s2>La Jolla, California 92037</s2><s3>USA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>7 aut.</sZ></inist:fA14></affiliation></author><author><name sortKey="Subramanian, Vanitha" sort="Subramanian, Vanitha" uniqKey="Subramanian V" first="Vanitha" last="Subramanian">Vanitha Subramanian</name><affiliation><inist:fA14 i1="01"><s1>Department of Cell Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road</s1><s2>La Jolla, California 92037</s2><s3>USA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>7 aut.</sZ></inist:fA14></affiliation></author><author><name sortKey="Neuman, Benjamin W" sort="Neuman, Benjamin W" uniqKey="Neuman B" first="Benjamin W." last="Neuman">Benjamin W. Neuman</name><affiliation><inist:fA14 i1="02"><s1>Department of Molecular Integrative Neurosciences, The Scripps Research Institute, 10550 N. Torrey Pines Road</s1><s2>La Jolla, California 92037</s2><s3>USA</s3><sZ>4 aut.</sZ><sZ>5 aut.</sZ></inist:fA14></affiliation></author><author><name sortKey="Buchmeier, Michael J" sort="Buchmeier, Michael J" uniqKey="Buchmeier M" first="Michael J." last="Buchmeier">Michael J. Buchmeier</name><affiliation><inist:fA14 i1="02"><s1>Department of Molecular Integrative Neurosciences, The Scripps Research Institute, 10550 N. Torrey Pines Road</s1><s2>La Jolla, California 92037</s2><s3>USA</s3><sZ>4 aut.</sZ><sZ>5 aut.</sZ></inist:fA14></affiliation></author><author><name sortKey="Stevens, Raymond C" sort="Stevens, Raymond C" uniqKey="Stevens R" first="Raymond C." last="Stevens">Raymond C. Stevens</name><affiliation><inist:fA14 i1="03"><s1>Department of Molecular Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road</s1><s2>La Jolla, California 92037</s2><s3>USA</s3><sZ>6 aut.</sZ></inist:fA14></affiliation></author><author><name sortKey="Kuhn, Peter" sort="Kuhn, Peter" uniqKey="Kuhn P" first="Peter" last="Kuhn">Peter Kuhn</name><affiliation><inist:fA14 i1="01"><s1>Department of Cell Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road</s1><s2>La Jolla, California 92037</s2><s3>USA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>7 aut.</sZ></inist:fA14></affiliation></author></analytic><series><title level="j" type="main">Journal of virology</title><title level="j" type="abbreviated">J. virol.</title><idno type="ISSN">0022-538X</idno><imprint><date when="2007">2007</date></imprint></series></biblStruct></sourceDesc><seriesStmt><title level="j" type="main">Journal of virology</title><title level="j" type="abbreviated">J. virol.</title><idno type="ISSN">0022-538X</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Coronavirus</term><term>Protein</term><term>Severe acute respiratory syndrome</term><term>Virology</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Coronavirus</term><term>Protéine</term><term>Virologie</term><term>Syndrome respiratoire aigu sévère</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Conserved among all coronaviruses are four structural proteins: the matrix (M), small envelope (E), and spike (S) proteins that are embedded in the viral membrane and the nucleocapsid phosphoprotein (N), which exists in a ribonucleoprotein complex in the lumen. The N-terminal domain of coronaviral N proteins (N-NTD) provides a scaffold for RNA binding, while the C-terminal domain (N-CTD) mainly acts as oligomerization modules during assembly. The C terminus of the N protein anchors it to the viral membrane by associating with M protein. We characterized the structures of N-NTD from severe acute respiratory syndrome coronavirus (SARS-CoV) in two crystal forms, at 1.17 Å (monoclinic) and at 1.85 Å (cubic), respectively, resolved by molecular replacement using the homologous avian infectious bronchitis virus (IBV) structure. Flexible loops in the solution structure of SARS-CoV N-NTD are now shown to be well ordered around the β-sheet core. The functionally important positively charged β-hairpin protrudes out of the core, is oriented similarly to that in the IBV N-NTD, and is involved in crystal packing in the monoclinic form. In the cubic form, the monomers form trimeric units that stack in a helical array. Comparison of crystal packing of SARS-CoV and IBV N-NTDs suggests a common mode of RNA recognition, but they probably associate differently in vivo during the formation of the ribonucleoprotein complex. Electrostatic potential distribution on the surface of homology models of related coronaviral N-NTDs suggests that they use different modes of both RNA recognition and oligomeric assembly, perhaps explaining why their nucleocapsids have different morphologies.</div></front></TEI><inist><standard h6="B"><pA><fA01 i1="01" i2="1"><s0>0022-538X</s0></fA01><fA03 i2="1"><s0>J. virol.</s0></fA03><fA05><s2>81</s2></fA05><fA06><s2>8</s2></fA06><fA08 i1="01" i2="1" l="ENG"><s1>Ribonucleocapsid formation of severe acute respiratory syndrome coronavirus through molecular action of the N-terminal domain of N protein</s1></fA08><fA11 i1="01" i2="1"><s1>KUMAR SINGH SAIKATENDU</s1></fA11><fA11 i1="02" i2="1"><s1>JOSEPH (Jeremiah S.)</s1></fA11><fA11 i1="03" i2="1"><s1>SUBRAMANIAN (Vanitha)</s1></fA11><fA11 i1="04" i2="1"><s1>NEUMAN (Benjamin W.)</s1></fA11><fA11 i1="05" i2="1"><s1>BUCHMEIER (Michael J.)</s1></fA11><fA11 i1="06" i2="1"><s1>STEVENS (Raymond C.)</s1></fA11><fA11 i1="07" i2="1"><s1>KUHN (Peter)</s1></fA11><fA14 i1="01"><s1>Department of Cell Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road</s1><s2>La Jolla, California 92037</s2><s3>USA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>7 aut.</sZ></fA14><fA14 i1="02"><s1>Department of Molecular Integrative Neurosciences, The Scripps Research Institute, 10550 N. Torrey Pines Road</s1><s2>La Jolla, California 92037</s2><s3>USA</s3><sZ>4 aut.</sZ><sZ>5 aut.</sZ></fA14><fA14 i1="03"><s1>Department of Molecular Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road</s1><s2>La Jolla, California 92037</s2><s3>USA</s3><sZ>6 aut.</sZ></fA14><fA20><s1>3913-3921</s1></fA20><fA21><s1>2007</s1></fA21><fA23 i1="01"><s0>ENG</s0></fA23><fA43 i1="01"><s1>INIST</s1><s2>13592</s2><s5>354000143390310240</s5></fA43><fA44><s0>0000</s0><s1>© 2007 INIST-CNRS. All rights reserved.</s1></fA44><fA45><s0>62 ref.</s0></fA45><fA47 i1="01" i2="1"><s0>07-0211072</s0></fA47><fA60><s1>P</s1></fA60><fA61><s0>A</s0></fA61><fA64 i1="01" i2="1"><s0>Journal of virology</s0></fA64><fA66 i1="01"><s0>USA</s0></fA66><fC01 i1="01" l="ENG"><s0>Conserved among all coronaviruses are four structural proteins: the matrix (M), small envelope (E), and spike (S) proteins that are embedded in the viral membrane and the nucleocapsid phosphoprotein (N), which exists in a ribonucleoprotein complex in the lumen. The N-terminal domain of coronaviral N proteins (N-NTD) provides a scaffold for RNA binding, while the C-terminal domain (N-CTD) mainly acts as oligomerization modules during assembly. The C terminus of the N protein anchors it to the viral membrane by associating with M protein. We characterized the structures of N-NTD from severe acute respiratory syndrome coronavirus (SARS-CoV) in two crystal forms, at 1.17 Å (monoclinic) and at 1.85 Å (cubic), respectively, resolved by molecular replacement using the homologous avian infectious bronchitis virus (IBV) structure. Flexible loops in the solution structure of SARS-CoV N-NTD are now shown to be well ordered around the β-sheet core. The functionally important positively charged β-hairpin protrudes out of the core, is oriented similarly to that in the IBV N-NTD, and is involved in crystal packing in the monoclinic form. In the cubic form, the monomers form trimeric units that stack in a helical array. Comparison of crystal packing of SARS-CoV and IBV N-NTDs suggests a common mode of RNA recognition, but they probably associate differently in vivo during the formation of the ribonucleoprotein complex. Electrostatic potential distribution on the surface of homology models of related coronaviral N-NTDs suggests that they use different modes of both RNA recognition and oligomeric assembly, perhaps explaining why their nucleocapsids have different morphologies.</s0></fC01><fC02 i1="01" i2="X"><s0>002A05C10</s0></fC02><fC03 i1="01" i2="X" l="FRE"><s0>Coronavirus</s0><s2>NW</s2><s5>01</s5></fC03><fC03 i1="01" i2="X" l="ENG"><s0>Coronavirus</s0><s2>NW</s2><s5>01</s5></fC03><fC03 i1="01" i2="X" l="SPA"><s0>Coronavirus</s0><s2>NW</s2><s5>01</s5></fC03><fC03 i1="02" i2="X" l="FRE"><s0>Protéine</s0><s5>05</s5></fC03><fC03 i1="02" i2="X" l="ENG"><s0>Protein</s0><s5>05</s5></fC03><fC03 i1="02" i2="X" l="SPA"><s0>Proteína</s0><s5>05</s5></fC03><fC03 i1="03" i2="X" l="FRE"><s0>Virologie</s0><s5>06</s5></fC03><fC03 i1="03" i2="X" l="ENG"><s0>Virology</s0><s5>06</s5></fC03><fC03 i1="03" i2="X" l="SPA"><s0>Virología</s0><s5>06</s5></fC03><fC03 i1="04" i2="X" l="FRE"><s0>Syndrome respiratoire aigu sévère</s0><s2>NM</s2><s5>14</s5></fC03><fC03 i1="04" i2="X" l="ENG"><s0>Severe acute respiratory syndrome</s0><s2>NM</s2><s5>14</s5></fC03><fC03 i1="04" i2="X" l="SPA"><s0>Síndrome respiratorio agudo severo</s0><s2>NM</s2><s5>14</s5></fC03><fC07 i1="01" i2="X" l="FRE"><s0>Coronaviridae</s0><s2>NW</s2></fC07><fC07 i1="01" i2="X" l="ENG"><s0>Coronaviridae</s0><s2>NW</s2></fC07><fC07 i1="01" i2="X" l="SPA"><s0>Coronaviridae</s0><s2>NW</s2></fC07><fC07 i1="02" i2="X" l="FRE"><s0>Nidovirales</s0><s2>NW</s2></fC07><fC07 i1="02" i2="X" l="ENG"><s0>Nidovirales</s0><s2>NW</s2></fC07><fC07 i1="02" i2="X" l="SPA"><s0>Nidovirales</s0><s2>NW</s2></fC07><fC07 i1="03" i2="X" l="FRE"><s0>Virus</s0><s2>NW</s2></fC07><fC07 i1="03" i2="X" l="ENG"><s0>Virus</s0><s2>NW</s2></fC07><fC07 i1="03" i2="X" l="SPA"><s0>Virus</s0><s2>NW</s2></fC07><fC07 i1="04" i2="X" l="FRE"><s0>Appareil respiratoire pathologie</s0><s5>13</s5></fC07><fC07 i1="04" i2="X" l="ENG"><s0>Respiratory disease</s0><s5>13</s5></fC07><fC07 i1="04" i2="X" l="SPA"><s0>Aparato respiratorio patología</s0><s5>13</s5></fC07><fC07 i1="05" i2="X" l="FRE"><s0>Virose</s0></fC07><fC07 i1="05" i2="X" l="ENG"><s0>Viral disease</s0></fC07><fC07 i1="05" i2="X" l="SPA"><s0>Virosis</s0></fC07><fC07 i1="06" i2="X" l="FRE"><s0>Infection</s0></fC07><fC07 i1="06" i2="X" l="ENG"><s0>Infection</s0></fC07><fC07 i1="06" i2="X" l="SPA"><s0>Infección</s0></fC07><fC07 i1="07" i2="X" l="FRE"><s0>Poumon pathologie</s0><s5>16</s5></fC07><fC07 i1="07" i2="X" l="ENG"><s0>Lung disease</s0><s5>16</s5></fC07><fC07 i1="07" i2="X" l="SPA"><s0>Pulmón patología</s0><s5>16</s5></fC07><fN21><s1>141</s1></fN21><fN44 i1="01"><s1>OTO</s1></fN44><fN82><s1>OTO</s1></fN82></pA></standard><server><NO>PASCAL 07-0211072 INIST</NO><ET>Ribonucleocapsid formation of severe acute respiratory syndrome coronavirus through molecular action of the N-terminal domain of N protein</ET><AU>KUMAR SINGH SAIKATENDU; JOSEPH (Jeremiah S.); SUBRAMANIAN (Vanitha); NEUMAN (Benjamin W.); BUCHMEIER (Michael J.); STEVENS (Raymond C.); KUHN (Peter)</AU><AF>Department of Cell Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road/La Jolla, California 92037/Etats-Unis (1 aut., 2 aut., 3 aut., 7 aut.); Department of Molecular Integrative Neurosciences, The Scripps Research Institute, 10550 N. Torrey Pines Road/La Jolla, California 92037/Etats-Unis (4 aut., 5 aut.); Department of Molecular Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road/La Jolla, California 92037/Etats-Unis (6 aut.)</AF><DT>Publication en série; Niveau analytique</DT><SO>Journal of virology; ISSN 0022-538X; Etats-Unis; Da. 2007; Vol. 81; No. 8; Pp. 3913-3921; Bibl. 62 ref.</SO><LA>Anglais</LA><EA>Conserved among all coronaviruses are four structural proteins: the matrix (M), small envelope (E), and spike (S) proteins that are embedded in the viral membrane and the nucleocapsid phosphoprotein (N), which exists in a ribonucleoprotein complex in the lumen. The N-terminal domain of coronaviral N proteins (N-NTD) provides a scaffold for RNA binding, while the C-terminal domain (N-CTD) mainly acts as oligomerization modules during assembly. The C terminus of the N protein anchors it to the viral membrane by associating with M protein. We characterized the structures of N-NTD from severe acute respiratory syndrome coronavirus (SARS-CoV) in two crystal forms, at 1.17 Å (monoclinic) and at 1.85 Å (cubic), respectively, resolved by molecular replacement using the homologous avian infectious bronchitis virus (IBV) structure. Flexible loops in the solution structure of SARS-CoV N-NTD are now shown to be well ordered around the β-sheet core. The functionally important positively charged β-hairpin protrudes out of the core, is oriented similarly to that in the IBV N-NTD, and is involved in crystal packing in the monoclinic form. In the cubic form, the monomers form trimeric units that stack in a helical array. Comparison of crystal packing of SARS-CoV and IBV N-NTDs suggests a common mode of RNA recognition, but they probably associate differently in vivo during the formation of the ribonucleoprotein complex. Electrostatic potential distribution on the surface of homology models of related coronaviral N-NTDs suggests that they use different modes of both RNA recognition and oligomeric assembly, perhaps explaining why their nucleocapsids have different morphologies.</EA><CC>002A05C10</CC><FD>Coronavirus; Protéine; Virologie; Syndrome respiratoire aigu sévère</FD><FG>Coronaviridae; Nidovirales; Virus; Appareil respiratoire pathologie; Virose; Infection; Poumon pathologie</FG><ED>Coronavirus; Protein; Virology; Severe acute respiratory syndrome</ED><EG>Coronaviridae; Nidovirales; Virus; Respiratory disease; Viral disease; Infection; Lung disease</EG><SD>Coronavirus; Proteína; Virología; Síndrome respiratorio agudo severo</SD><LO>INIST-13592.354000143390310240</LO><ID>07-0211072</ID></server></inist></record>Pour manipuler ce document sous Unix (Dilib)
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