Abstract
We describe a method to detect influenza virus using an evanescent-field-activated fluorescence scanner type glycan array and ELISA system. Neoglycoprotein was prepared by combination of organic chemistry and biomaterial preparation. These ligands were spotted on a glass plate or plastic well to make a glycan array and ELISA plate. We detected cultured influenza virus using glycan array and ELISA. Then, we showed that the neoglycoprotein binds to Cy3-labeled hemagglutinins (H1 and H5), a NeuAcα2,6LacNAc or NeuAcα2,3LacNAc recognized protein, as detected.
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References
Stevens J, Blixt O, Paulson JC, Wilson IA (2006) Glycan microarray technologies: tools to survey host specificity of influenza viruses. Nat Rev Microbiol 4:857–864
Carvalho SB, Moleirinho MG, Wheatley D et al (2017) Universal label-free in-process quantification of influenza virus-like particles. Biotechnol J 12:1700031
Guo H, Rabouw H, Slomp A et al (2018) Kinetic analysis of the influenza A virus HA/NA balance reveals contribution of NA to virus-receptor binding and NA-dependent rolling on receptor-containing surfaces. PLoS Pathog 14:e1007233
Benton DJ, Martin SR, Wharton SA et al (2015) Biophysical measurement of the balance of influenza a hemagglutinin and neuraminidase activities. J Biol Chem 290:6516–6521
Wright ZVF, Wu NC, Kadam RU et al (2017) Structure-based optimization and synthesis of antiviral drug Arbidol analogues with significantly improved affinity to influenza hemagglutinin. Bioorg Med Chem Lett 27:3744–3748
Rillahan CD, Paulson JC (2011) Glycan microarrays for decoding the glycome. Annu Rev Biochem 80:797–823
Oyelaran O, Gildersleeve JC (2009) Glycan array. Recent advances and future challenges. Curr Opin Chem Biol 13:406–413
Fukui S, Feizi T, Galustian C et al (2002) Oligoglycan microarrays for high-throughput detection and specificity assignments of carbohydrate-protein interaction. Nat Biotechnol 20:1011–1017
Wang D, Liu S, Trummer BJ et al (2002) Carbohydrate microarrays for the recognition of cross-reactive molecular markers of microtubes and host cells. Nat Biotechnol 20:275–281
Nemanichvili N, Tomris I, Turner HL et al (2019) Fluorescent trimeric hemagglutinins reveal multivalent receptor binding properties. J Mol Biol 431:842–856
Takahashi T, Kawakami T, Mizuno T et al (2013) Sensitive and direct detection of receptor binding specificity of highly pathogenic avian influenza A virus in clinical samples. PLoS One 8:e78125
Tateno H, Mori A, Uchiyama N et al (2008) Glycoconjugate microarray based on an evanescent-field fluorescence-assisted detection principle for investigation of glycan-binding proteins. Glycobiology 18:789–798
Nakakita S, Hirabayashi J (2016) Preparation of glycan arrays using pyridylaminated glycans. Methods Mol Biol 1368:225–235
Kuno A, Uchiyama N, Koseki-Kuno S et al (2005) Evanescent-field fluorescence-assisted lectin microarray: a new strategy for glycan profiling. Nat Methods 2:851–856
http://www.who.int/csr/resources/publications/biosafety/WHO_CDS_CSR_LYO_2004_11/en/
Sriwilaijaroen N, Suzuki Y (2012) Molecular basis of the structure and function of H1 hemagglutinin of influenza virus. Proc Jpn Acad Ser B Phys Biol Sci 88:226–249
Burnet F, Bull DH (1943) Changes in influenza virus associated with adaptation to passage in chick embryos. Aust J Exp Biol Med Sci 21:55–69
Ito T, Suzuki Y, Takada A et al (1997) Differences in sialic acid-galactose linkages in the chicken egg amnion and allantois influence human influenza virus receptor specificity and variant selection. J Virol 71:3357–3362
Gambaryan AS, Robertson JS, Matrosovich MN (1999) Effects of egg-adaptation on the receptor-binding properties of human influenza A and B viruses. Virology 258:232–239
Widjaja L, Ilyushina N, Webster RG et al (2006) Molecular changes associated with adaptation of human influenza A virus in embryonated chicken eggs. Virology 350:137–145
Sriwilaijaroen N, Kondo S, Yagi H et al (2009) Analysis of N-glycans in embryonated chicken egg chorioallantoic and amniotic cells responsible for binding and adaptation of human and avian influenza viruses. Glycoconj J 26:433–443
Rocha EP, Xu X, Hall HE et al (1993) Comparison of 10 influenza A (H1N1 and H3N2) haemagglutinin sequences obtained directly from clinical specimens to those of MDCK cell- and egg-grown viruses. J Gen Virol 74:2513–2518
Takemae N, Ruttanapumma R, Parchariyanon S et al (2010) Alterations in receptor-binding properties of swine influenza viruses of the H1 subtype after isolation in embryonated chicken eggs. J Gen Virol 91:938–948
Dukes JD, Whitley P, Chalmers AD (2011) The MDCK variety pack: choosing the right strain. BMC Cell Biol 12:43
Matrosovich M, Matrosovich T, Carr J et al (2003) Overexpression of the alpha-2,6-sialyltransferase in MDCK cells increases influenza virus sensitivity to neuraminidase inhibitors. J Virol 77:8418–8425
Hatakeyama S, Sakai-Tagawa Y, Kiso M et al (2005) Enhanced expression of an alpha2,6-linked sialic acid on MDCK cells improves isolation of human influenza viruses and evaluation of their sensitivity to a neuraminidase inhibitor. J Clin Microbiol 43:4139–4146
Ito T, Suzuki Y, Mitnaul L et al (1997) Receptor specificity of influenza A viruses correlates with the agglutination of erythrocytes from different animal species. Virology 227:493–499
Xu R, de Vries RP, Zhu X et al (2013) Preferential recognition of avian-like receptors in human influenza A H7N9 viruses. Science 342:1230–1235
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Nakakita, Si., Sriwilaijaroen, N., Suzuki, Y., Hirabayashi, J. (2020). Preparation and Detection of Glycan-Binding Activity of Influenza Virus. In: Hirabayashi, J. (eds) Lectin Purification and Analysis. Methods in Molecular Biology, vol 2132. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-0430-4_49
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DOI: https://doi.org/10.1007/978-1-0716-0430-4_49
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