Measurement of enzymatic activity and specificity of human and avian influenza neuraminidases from whole virus by glycoarray and MALDI-TOF mass spectrometry.
Identifieur interne : 000172 ( France/Analysis ); précédent : 000171; suivant : 000173Measurement of enzymatic activity and specificity of human and avian influenza neuraminidases from whole virus by glycoarray and MALDI-TOF mass spectrometry.
Auteurs : Gwladys Pourceau [France] ; Yann Chevolot [France] ; Alice Goudot [France] ; Fabienne Giroux [France] ; Albert Meyer [France] ; Vincent Moulés [France] ; Bruno Lina [France] ; Samy Cecioni [France] ; Sébastien Vidal [France] ; Hai Yu [États-Unis] ; Xi Chen [États-Unis] ; Olivier Ferraris [France] ; Jean-Pierre Praly [France] ; Eliane Souteyrand [France] ; Jean-Jacques Vasseur [France] ; François Morvan [France]Source :
- ChemBioChem [ 1439-4227 ] ; 2011-09-05.
Abstract
Influenza neuraminidases hydrolyze the ketosidic linkage between N-acetylneuraminic acid and its adjacent galactose residue in sialosides. This enzyme is a tetrameric protein that plays a critical role in the release of progeny virions. Several methods have been described for the determination of neuraminidase activity, usually based on colorimetric, fluorescent, or chemiluminescent detection. However, only a few of these tests allow discrimination of the sialyl-linkage specificity (i.e., α2-3- versus α2-6-linked sialyllactosides) of the neuraminidase. Herein we report a glycoarray-based assay and a MALDI-TOF study for assessing the activity and specificity of two influenza neuraminidases on whole viruses. The human A(H3N2) and avian A(H5N2) neuraminidase activities were investigated. The results from both approaches demonstrated that α2-3 sialyllactoside was a better substrate than α2-6 sialyllactoside for both viruses and that H5N2 virus had a lower hydrolytic activity than H3N2.
Url:
DOI: 10.1002/cbic.201100128
Affiliations:
- France, États-Unis
- Auvergne-Rhône-Alpes, Rhône-Alpes
- Lyon
- Université Claude Bernard Lyon 1, Université de Lyon
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Hal:hal-00691511Le document en format XML
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</org></tutelle><tutelle active="#struct-126765" type="indirect"><org type="institution" xml:id="struct-126765" status="VALID"> <orgName>École Centrale de Lyon</orgName> <orgName type="acronym">ECL</orgName> <desc> <address> <addrLine>36 avenue Guy de Collongue - 69134 Ecully cedex</addrLine> <country key="FR"></country> </address> <ref type="url">http://www.ec-lyon.fr</ref> </desc> <listRelation> <relation active="#struct-301088" type="direct"></relation> </listRelation> </org></tutelle><tutelle active="#struct-301088" type="indirect"><org type="regroupinstitution" xml:id="struct-301088" status="VALID"> <orgName>Université de Lyon</orgName> <desc> <address> <addrLine>92 rue Pasteur - CS 30122, 69361 Lyon Cedex 07</addrLine> <country key="FR"></country> </address> <ref type="url">https://www.universite-lyon.fr/</ref> </desc> </org></tutelle><tutelle name="UMR5270" active="#struct-441569" type="indirect"><org type="institution" xml:id="struct-441569" status="VALID"> <idno type="IdRef">02636817X</idno> <idno type="ISNI">0000000122597504</idno> <orgName>Centre National de la Recherche Scientifique</orgName> <orgName type="acronym">CNRS</orgName> <date type="start">1939-10-19</date> <desc> <address> <country key="FR"></country> </address> <ref type="url">http://www.cnrs.fr/</ref> </desc> </org></tutelle><tutelle active="#struct-219748" type="indirect"><org type="institution" xml:id="struct-219748" status="VALID"> <idno type="IdRef">052444724</idno> <idno type="ISNI">0000 0001 2292 0228</idno> <orgName>Institut National des Sciences Appliquées de Lyon</orgName> <orgName type="acronym">INSA Lyon</orgName> <date type="start">1957-03-18</date> <desc> <address> <addrLine>20 Avenue Albert Einstein, 69621 Villeurbanne cedex</addrLine> <country key="FR"></country> </address> <ref type="url">http://www.insa-lyon.fr/</ref> </desc> <listRelation> <relation active="#struct-301088" type="direct"></relation> <relation active="#struct-301232" type="direct"></relation> </listRelation> </org></tutelle><tutelle active="#struct-301232" type="indirect"><org type="regroupinstitution" xml:id="struct-301232" status="VALID"> <idno type="IdRef">162105150</idno> <orgName>Institut National des Sciences Appliquées</orgName> <orgName type="acronym">INSA</orgName> <desc> <address> <country key="FR"></country> </address> </desc> </org></tutelle><tutelle active="#struct-210962" type="indirect"><org type="institution" xml:id="struct-210962" status="VALID"> <orgName>École supérieure de Chimie Physique Electronique de Lyon</orgName> <orgName type="acronym">CPE</orgName> <desc> <address> <addrLine>Domaine Scientifique de la DouaBâtiment Hubert Curien 43 Boulevard du 11 Novembre 191869616 Villeurbanne</addrLine> <country key="FR"></country> </address> <ref type="url">http://www.cpe.fr/</ref> </desc> </org></tutelle><tutelle active="#struct-194495" type="indirect"><org type="institution" xml:id="struct-194495" status="VALID"> <idno type="IdRef">026402823</idno> <idno type="ISNI">0000000121686185</idno> <orgName>Université Claude Bernard Lyon 1</orgName> <orgName type="acronym">UCBL</orgName> <desc> <address> <addrLine>43, boulevard du 11 novembre 1918, 69622 Villeurbanne cedex</addrLine> <country key="FR"></country> </address> <ref type="url">http://www.univ-lyon1.fr/</ref> </desc> <listRelation> <relation active="#struct-301088" type="direct"></relation> </listRelation> </org></tutelle></tutelles></hal:affiliation><country>France</country><placeName><settlement type="city">Lyon</settlement><region type="region" nuts="2">Auvergne-Rhône-Alpes</region><region type="old region" nuts="2">Rhône-Alpes</region></placeName><orgName type="university">Université Claude Bernard Lyon 1</orgName><orgName type="institution" wicri:auto="newGroup">Université de Lyon</orgName></affiliation></author><author><name sortKey="Vasseur, Jean Jacques" sort="Vasseur, Jean Jacques" uniqKey="Vasseur J" first="Jean-Jacques" last="Vasseur">Jean-Jacques Vasseur</name><affiliation wicri:level="1"><hal:affiliation type="laboratory" xml:id="struct-24488" status="VALID"> <idno type="RNSR">200711912X</idno> <orgName>Institut des Biomolécules Max Mousseron [Pôle Chimie Balard]</orgName> <orgName type="acronym">IBMM</orgName> <desc> <address> <addrLine>Faculté de Pharmacie - 15 Av. Charles Flahault - BP 14 491 - 34093 Montpellier Cedex 5</addrLine> <country key="FR"></country> </address> <ref type="url">http://www.ibmm.univ-montp1.fr</ref> </desc> <listRelation> <relation active="#struct-300370" type="direct"></relation> <relation active="#struct-410122" type="direct"></relation> <relation name="UMR5247" active="#struct-441569" type="direct"></relation> </listRelation> <tutelles><tutelle active="#struct-300370" type="direct"><org type="institution" xml:id="struct-300370" status="VALID"> <orgName>Ecole Nationale Supérieure de Chimie de Montpellier</orgName> <orgName type="acronym">ENSCM</orgName> <desc> <address> <addrLine>8 Rue de l'Ecole Normale 34296 Montpellier Cedex 5</addrLine> <country key="FR"></country> </address> <ref type="url">http://www.enscm.fr</ref> </desc> </org></tutelle><tutelle active="#struct-410122" type="direct"><org type="institution" xml:id="struct-410122" status="VALID"> <idno type="ISNI">0000000120970141</idno> <orgName>Université de Montpellier</orgName> <orgName type="acronym">UM</orgName> <desc> <address> <addrLine>163 rue Auguste Broussonnet - 34090 Montpellier</addrLine> <country key="FR"></country> </address> <ref type="url">http://www.umontpellier.fr/</ref> </desc> </org></tutelle><tutelle name="UMR5247" active="#struct-441569" type="direct"><org type="institution" xml:id="struct-441569" status="VALID"> <idno type="IdRef">02636817X</idno> <idno type="ISNI">0000000122597504</idno> <orgName>Centre National de la Recherche Scientifique</orgName> <orgName type="acronym">CNRS</orgName> <date type="start">1939-10-19</date> <desc> <address> <country key="FR"></country> </address> <ref type="url">http://www.cnrs.fr/</ref> </desc> </org></tutelle></tutelles></hal:affiliation><country>France</country></affiliation></author><author><name sortKey="Morvan, Francois" sort="Morvan, Francois" uniqKey="Morvan F" first="François" last="Morvan">François Morvan</name><affiliation wicri:level="1"><hal:affiliation type="laboratory" xml:id="struct-24488" status="VALID"> <idno type="RNSR">200711912X</idno> <orgName>Institut des Biomolécules Max Mousseron [Pôle Chimie Balard]</orgName> <orgName type="acronym">IBMM</orgName> <desc> <address> <addrLine>Faculté de Pharmacie - 15 Av. Charles Flahault - BP 14 491 - 34093 Montpellier Cedex 5</addrLine> <country key="FR"></country> </address> <ref type="url">http://www.ibmm.univ-montp1.fr</ref> </desc> <listRelation> <relation active="#struct-300370" type="direct"></relation> <relation active="#struct-410122" type="direct"></relation> <relation name="UMR5247" active="#struct-441569" type="direct"></relation> </listRelation> <tutelles><tutelle active="#struct-300370" type="direct"><org type="institution" xml:id="struct-300370" status="VALID"> <orgName>Ecole Nationale Supérieure de Chimie de Montpellier</orgName> <orgName type="acronym">ENSCM</orgName> <desc> <address> <addrLine>8 Rue de l'Ecole Normale 34296 Montpellier Cedex 5</addrLine> <country key="FR"></country> </address> <ref type="url">http://www.enscm.fr</ref> </desc> </org></tutelle><tutelle active="#struct-410122" type="direct"><org type="institution" xml:id="struct-410122" status="VALID"> <idno type="ISNI">0000000120970141</idno> <orgName>Université de Montpellier</orgName> <orgName type="acronym">UM</orgName> <desc> <address> <addrLine>163 rue Auguste Broussonnet - 34090 Montpellier</addrLine> <country key="FR"></country> </address> <ref type="url">http://www.umontpellier.fr/</ref> </desc> </org></tutelle><tutelle name="UMR5247" active="#struct-441569" type="direct"><org type="institution" xml:id="struct-441569" status="VALID"> <idno type="IdRef">02636817X</idno> <idno type="ISNI">0000000122597504</idno> <orgName>Centre National de la Recherche Scientifique</orgName> <orgName type="acronym">CNRS</orgName> <date type="start">1939-10-19</date> <desc> <address> <country key="FR"></country> </address> <ref type="url">http://www.cnrs.fr/</ref> </desc> </org></tutelle></tutelles></hal:affiliation><country>France</country></affiliation></author></analytic><idno type="DOI">10.1002/cbic.201100128</idno><series><title level="j">ChemBioChem</title><idno type="ISSN">1439-4227</idno><imprint><date type="datePub">2011-09-05</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"> <p>Influenza neuraminidases hydrolyze the ketosidic linkage between N-acetylneuraminic acid and its adjacent galactose residue in sialosides. This enzyme is a tetrameric protein that plays a critical role in the release of progeny virions. Several methods have been described for the determination of neuraminidase activity, usually based on colorimetric, fluorescent, or chemiluminescent detection. However, only a few of these tests allow discrimination of the sialyl-linkage specificity (i.e., α2-3- versus α2-6-linked sialyllactosides) of the neuraminidase. Herein we report a glycoarray-based assay and a MALDI-TOF study for assessing the activity and specificity of two influenza neuraminidases on whole viruses. The human A(H3N2) and avian A(H5N2) neuraminidase activities were investigated. The results from both approaches demonstrated that α2-3 sialyllactoside was a better substrate than α2-6 sialyllactoside for both viruses and that H5N2 virus had a lower hydrolytic activity than H3N2.</p> </div></front></TEI><affiliations><list><country><li>France</li><li>États-Unis</li></country><region><li>Auvergne-Rhône-Alpes</li><li>Rhône-Alpes</li></region><settlement><li>Lyon</li></settlement><orgName><li>Université Claude Bernard Lyon 1</li><li>Université de Lyon</li></orgName></list><tree><country name="France"><noRegion><name sortKey="Pourceau, Gwladys" sort="Pourceau, Gwladys" uniqKey="Pourceau G" first="Gwladys" last="Pourceau">Gwladys Pourceau</name></noRegion><name sortKey="Cecioni, Samy" sort="Cecioni, Samy" uniqKey="Cecioni S" first="Samy" last="Cecioni">Samy Cecioni</name><name sortKey="Chevolot, Yann" sort="Chevolot, Yann" uniqKey="Chevolot Y" first="Yann" last="Chevolot">Yann Chevolot</name><name sortKey="Ferraris, Olivier" sort="Ferraris, Olivier" uniqKey="Ferraris O" first="Olivier" last="Ferraris">Olivier Ferraris</name><name sortKey="Giroux, Fabienne" sort="Giroux, Fabienne" uniqKey="Giroux F" first="Fabienne" last="Giroux">Fabienne Giroux</name><name sortKey="Goudot, Alice" sort="Goudot, Alice" uniqKey="Goudot A" first="Alice" last="Goudot">Alice Goudot</name><name sortKey="Lina, Bruno" sort="Lina, Bruno" uniqKey="Lina B" first="Bruno" last="Lina">Bruno Lina</name><name sortKey="Meyer, Albert" sort="Meyer, Albert" uniqKey="Meyer A" first="Albert" last="Meyer">Albert Meyer</name><name sortKey="Morvan, Francois" sort="Morvan, Francois" uniqKey="Morvan F" first="François" last="Morvan">François Morvan</name><name sortKey="Moules, Vincent" sort="Moules, Vincent" uniqKey="Moules V" first="Vincent" last="Moulés">Vincent Moulés</name><name sortKey="Praly, Jean Pierre" sort="Praly, Jean Pierre" uniqKey="Praly J" first="Jean-Pierre" last="Praly">Jean-Pierre Praly</name><name sortKey="Souteyrand, Eliane" sort="Souteyrand, Eliane" uniqKey="Souteyrand E" first="Eliane" last="Souteyrand">Eliane Souteyrand</name><name sortKey="Vasseur, Jean Jacques" sort="Vasseur, Jean Jacques" uniqKey="Vasseur J" first="Jean-Jacques" last="Vasseur">Jean-Jacques Vasseur</name><name sortKey="Vidal, Sebastien" sort="Vidal, Sebastien" uniqKey="Vidal S" first="Sébastien" last="Vidal">Sébastien Vidal</name></country><country name="États-Unis"><noRegion><name sortKey="Yu, Hai" sort="Yu, Hai" uniqKey="Yu H" first="Hai" last="Yu">Hai Yu</name></noRegion><name sortKey="Chen, Xi" sort="Chen, Xi" uniqKey="Chen X" first="Xi" last="Chen">Xi Chen</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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