期刊
VIROLOGY
卷 493, 期 -, 页码 128-135出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2016.03.011
关键词
Influenza A; Sialic acids; Glycan array; Magnetic beads; Neuraminidase; Glycans
类别
资金
- NIH: CEIRS [HHSN272201400008C, HHSN266200700010C]
- NIH: NIBIB [5 R00 EB013446-05]
- G. Harold and Leila Y. Mathers Foundation of Mount Kisco, New York
- UCSD Graduate Training Program in Molecular Biophysics through an institutional training Grant from the National Institute of General Medical Sciences [T32 GM08326]
Influenza A viruses (IAVs) utilize sialylated host glycans as ligands for binding and infection. The glycanbinding preference of IAV hemagglutinin (HA) is an important determinant of host specificity. Propagation of IAV in embryonated chicken eggs and cultured mammalian cells yields viruses with amino acid substitutions in the HA that can alter the binding specificity. Therefore, it is important to determine the binding specificity of IAV directly in primary samples since it reflects the actual tropism of virus in nature. We developed a novel platform for analysis of IAV binding specificity in samples that contain very low virus titers. This platform consists of a high-density flexible glycan display on magnetic beads, which promotes multivalent interactions with the viral HA. Glycan-bound virus is detected by quantifying the viral neuraminidase activity via a fluorogenic reporter, 2'-(4-methylumbelliferyI)-alpha-D-N-acetylneuraminic acid. This method eliminates the need for labeling the virus and significantly enhances the sensitivity of detection. (C) 2016 Elsevier Inc. All rights reserved.
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