tetano
Editor, Senior Moderator
Virology. 2016 Mar 28;493:128-135. doi: 10.1016/j.virol.2016.03.011. [Epub ahead of print]
[h=1]Capture and characterization of influenza A virus from primary samples using glycan bead arrays.[/h] Cohen M[SUP]1[/SUP], Fisher CJ[SUP]2[/SUP], Huang ML[SUP]2[/SUP], Lindsay LL[SUP]3[/SUP], Plancarte M[SUP]3[/SUP], Boyce WM[SUP]3[/SUP], Godula K[SUP]2[/SUP], Gagneux P[SUP]4[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] Influenza A viruses (IAVs) utilize sialylated host glycans as ligands for binding and infection. The glycan-binding 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-methylumbelliferyl)-α-d-N-acetylneuraminic acid. This method eliminates the need for labeling the virus and significantly enhances the sensitivity of detection.
Copyright ? 2016 Elsevier Inc. All rights reserved.
[h=4]KEYWORDS:[/h] Glycan array; Glycans; Influenza A; Magnetic beads; Neuraminidase; Sialic acids
PMID: 27031581 [PubMed - as supplied by publisher]
[h=1]Capture and characterization of influenza A virus from primary samples using glycan bead arrays.[/h] Cohen M[SUP]1[/SUP], Fisher CJ[SUP]2[/SUP], Huang ML[SUP]2[/SUP], Lindsay LL[SUP]3[/SUP], Plancarte M[SUP]3[/SUP], Boyce WM[SUP]3[/SUP], Godula K[SUP]2[/SUP], Gagneux P[SUP]4[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] Influenza A viruses (IAVs) utilize sialylated host glycans as ligands for binding and infection. The glycan-binding 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-methylumbelliferyl)-α-d-N-acetylneuraminic acid. This method eliminates the need for labeling the virus and significantly enhances the sensitivity of detection.
Copyright ? 2016 Elsevier Inc. All rights reserved.
[h=4]KEYWORDS:[/h] Glycan array; Glycans; Influenza A; Magnetic beads; Neuraminidase; Sialic acids
PMID: 27031581 [PubMed - as supplied by publisher]