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Measurement of enzymatic activity and specificity of human and avian influenza neuraminidases from whole virus by glycoarray and MALDI-TOF mass spectrometry.

Identifieur interne : 000200 ( Hal/Corpus ); précédent : 000199; suivant : 000201

Measurement of enzymatic activity and specificity of human and avian influenza neuraminidases from whole virus by glycoarray and MALDI-TOF mass spectrometry.

Auteurs : Gwladys Pourceau ; Yann Chevolot ; Alice Goudot ; Fabienne Giroux ; Albert Meyer ; Vincent Moulés ; Bruno Lina ; Samy Cecioni ; Sébastien Vidal ; Hai Yu ; Xi Chen ; Olivier Ferraris ; Jean-Pierre Praly ; Eliane Souteyrand ; Jean-Jacques Vasseur ; François Morvan

Source :

RBID : Hal:hal-00691511

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

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Hal:hal-00691511

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<idno type="DOI">10.1002/cbic.201100128</idno>
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<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>
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<title xml:lang="en">Measurement of enzymatic activity and specificity of human and avian influenza neuraminidases from whole virus by glycoarray and MALDI-TOF mass spectrometry.</title>
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<forename type="first">Gwladys</forename>
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<forename type="first">François</forename>
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</persName>
<idno type="halauthorid">400981</idno>
<affiliation ref="#struct-508819"></affiliation>
</author>
<author role="aut">
<persName>
<forename type="first">Samy</forename>
<surname>Cecioni</surname>
</persName>
<idno type="halauthorid">716807</idno>
<affiliation ref="#struct-24487"></affiliation>
</author>
<author role="aut">
<persName>
<forename type="first">Sébastien</forename>
<surname>Vidal</surname>
</persName>
<idno type="halauthorid">107313</idno>
<affiliation ref="#struct-24487"></affiliation>
</author>
<author role="aut">
<persName>
<forename type="first">Hai</forename>
<surname>Yu</surname>
</persName>
<idno type="halauthorid">636376</idno>
<affiliation ref="#struct-17255"></affiliation>
</author>
<author role="aut">
<persName>
<forename type="first">Xi</forename>
<surname>Chen</surname>
</persName>
<idno type="halauthorid">219147</idno>
<affiliation ref="#struct-17255"></affiliation>
</author>
<author role="aut">
<persName>
<forename type="first">Olivier</forename>
<surname>Ferraris</surname>
</persName>
<idno type="halauthorid">616550</idno>
<affiliation ref="#struct-508819"></affiliation>
</author>
<author role="aut">
<persName>
<forename type="first">Jean-Pierre</forename>
<surname>Praly</surname>
</persName>
<idno type="halauthorid">107317</idno>
<affiliation ref="#struct-24487"></affiliation>
</author>
<author role="aut">
<persName>
<forename type="first">Eliane</forename>
<surname>Souteyrand</surname>
</persName>
<idno type="halauthorid">209762</idno>
<affiliation ref="#struct-527410"></affiliation>
</author>
<author role="aut">
<persName>
<forename type="first">Jean-Jacques</forename>
<surname>Vasseur</surname>
</persName>
<email type="md5">a09fe1c7c0bc71361d6718947b1ccb17</email>
<email type="domain">umontpellier.fr</email>
<idno type="idhal" notation="string">jean-jacques-vasseur</idno>
<idno type="idhal" notation="numeric">176784</idno>
<idno type="halauthorid">76539</idno>
<idno type="ORCID">https://orcid.org/0000-0002-4379-6139</idno>
<affiliation ref="#struct-24488"></affiliation>
</author>
<author role="aut">
<persName>
<forename type="first">François</forename>
<surname>Morvan</surname>
</persName>
<idno type="halauthorid">76541</idno>
<affiliation ref="#struct-24488"></affiliation>
</author>
</analytic>
<monogr>
<idno type="localRef">Equipe : Chimie Organique 2-Glycochimie (CO2GLYCO)</idno>
<idno type="halJournalId" status="VALID">11600</idno>
<idno type="issn">1439-4227</idno>
<idno type="eissn">1439-7633</idno>
<title level="j">ChemBioChem</title>
<imprint>
<publisher>Wiley-VCH Verlag</publisher>
<biblScope unit="volume">12</biblScope>
<biblScope unit="issue">13</biblScope>
<biblScope unit="pp">2071-2080</biblScope>
<date type="datePub">2011-09-05</date>
</imprint>
</monogr>
<idno type="doi">10.1002/cbic.201100128</idno>
<idno type="pubmed">21739555</idno>
</biblStruct>
</sourceDesc>
<profileDesc>
<langUsage>
<language ident="en">English</language>
</langUsage>
<textClass>
<classCode scheme="halDomain" n="chim.orga">Chemical Sciences/Organic chemistry</classCode>
<classCode scheme="halTypology" n="ART">Journal articles</classCode>
</textClass>
<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>
</abstract>
</profileDesc>
</hal>
</record>

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