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

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

Research output: Contribution to journalArticle

10 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)2071-2080
Number of pages10
JournalChemBioChem
Volume12
Issue number13
DOIs
StatePublished - Sep 5 2011

Fingerprint

Influenza in Birds
Matrix-Assisted Laser Desorption-Ionization Mass Spectrometry
Neuraminidase
Viruses
Human Influenza
Mass spectrometry
Mass Spectrometry
H5N2 Subtype Influenza A Virus
N-Acetylneuraminic Acid
Galactose
Virion
Assays
Substrates
Enzymes
Proteins

Keywords

  • Analytical methods
  • Glycochips
  • Influenza
  • MALDI
  • Neuraminidases
  • Viruses

ASJC Scopus subject areas

  • Biochemistry
  • Organic Chemistry
  • Molecular Medicine
  • Molecular Biology

Cite this

Measurement of enzymatic activity and specificity of human and avian influenza neuraminidases from whole virus by glycoarray and MALDI-TOF mass spectrometry. / Pourceau, Gwladys; Chevolot, Yann; Goudot, Alice; Giroux, Fabienne; Meyer, Albert; Moulés, Vincent; Lina, Bruno; Cecioni, Samy; Vidal, Sébastien; Yu, Hai; Chen, Xi; Ferraris, Olivier; Praly, Jean Pierre; Souteyrand, Eliane; Vasseur, Jean Jacques; Morvan, François.

In: ChemBioChem, Vol. 12, No. 13, 05.09.2011, p. 2071-2080.

Research output: Contribution to journalArticle

Pourceau, G, Chevolot, Y, Goudot, A, Giroux, F, Meyer, A, Moulés, V, Lina, B, Cecioni, S, Vidal, S, Yu, H, Chen, X, Ferraris, O, Praly, JP, Souteyrand, E, Vasseur, JJ & Morvan, F 2011, 'Measurement of enzymatic activity and specificity of human and avian influenza neuraminidases from whole virus by glycoarray and MALDI-TOF mass spectrometry', ChemBioChem, vol. 12, no. 13, pp. 2071-2080. https://doi.org/10.1002/cbic.201100128
Pourceau, Gwladys ; Chevolot, Yann ; Goudot, Alice ; Giroux, Fabienne ; Meyer, Albert ; Moulés, Vincent ; Lina, Bruno ; Cecioni, Samy ; Vidal, Sébastien ; Yu, Hai ; Chen, Xi ; Ferraris, Olivier ; Praly, Jean Pierre ; Souteyrand, Eliane ; Vasseur, Jean Jacques ; Morvan, François. / Measurement of enzymatic activity and specificity of human and avian influenza neuraminidases from whole virus by glycoarray and MALDI-TOF mass spectrometry. In: ChemBioChem. 2011 ; Vol. 12, No. 13. pp. 2071-2080.
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