Measurement of Enzymatic Activity and Specificity of Human and Avian Influenza Neuraminidases from Whole Virus by Glycoarray and MALDI-TOF Mass Spectrometry (pages 2071–2080)
Dr. Gwladys Pourceau, Dr. Yann Chevolot, Alice Goudot, Fabienne Giroux, Albert Meyer, Dr. Vincent Moulés, Prof. Bruno Lina, Dr. Samy Cecioni, Dr. Sébastien Vidal, Dr. Hai Yu, Prof. Xi Chen, Dr. Olivier Ferraris, Dr. Jean-Pierre Praly, Dr. Eliane Souteyrand, Dr. Jean-Jacques Vasseur and Dr. François Morvan
Article first published online: 7 JUL 2011 | DOI: 10.1002/cbic.201100128
Catching the 'flu: A DDI glycoarray-based assay and MALDI-TOF monitoring for assessing the activity and specificity of two influenza neuraminidases with whole viruses: human A(H3N2) and avian A(H5N2) are described. 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.