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<div class="pre-content"><div><div class="bk_prnt"><p class="small">NCBI Bookshelf. A service of the National Library of Medicine, National Institutes of Health.</p><p>Nishihara S, Angata K, Aoki-Kinoshita KF, et al., editors. Glycoscience Protocols (GlycoPODv2) [Internet]. Saitama (JP): Japan Consortium for Glycobiology and Glycotechnology; 2021-. </p></div></div></div>
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<div class="main-content lit-style" itemscope="itemscope" itemtype="http://schema.org/CreativeWork"><div class="meta-content fm-sec"><h1 id="_NBK593945_"><span class="title" itemprop="name">Enzyme-linked immunosorbent assay (ELISA)-based method for determination of influenza virus-host receptor binding specificity</span></h1><div class="contrib half_rhythm"><span itemprop="author">Yasuo Suzuki</span>, Ph,D<div class="affiliation small">University of Shizuoka, School of Pharmaceutical Sciences<div><span class="email-label">Email: </span><a href="mailto:dev@null" data-email="pj.ca.nek-akouzihs-u@5402pg" class="oemail">pj.ca.nek-akouzihs-u@5402pg</a></div></div><div class="small">Corresponding author.</div></div><div class="contrib half_rhythm"><span itemprop="author">Nongluk Sriwilaijaroen</span>, Ph.D.<div class="affiliation small">Faculty of Medicine, Thammasat University<div><span class="email-label">Email: </span><a href="mailto:dev@null" data-email="moc.liamtoh@kulgnons" class="oemail">moc.liamtoh@kulgnons</a></div></div></div><p class="small">Created: <span itemprop="datePublished">November 24, 2021</span>; Last Revision: <span itemprop="dateModified">March 23, 2022</span>.</p></div><div class="body-content whole_rhythm" itemprop="text"><div id="g110-ELISAinfluenza.Introduction"><h2 id="_g110-ELISAinfluenza_Introduction_">Introduction</h2><p>To initiate infection, H1-H16 influenza A viruses use their hemagglutinins (HAs) for attachment to sialoglycoconjugates on the host cell surface. Specific binding of the influenza viruses to sialoglycoconjugates on the host cell surface is critical for efficient transmission among a host species (<a class="bk_pop" href="#g110-ELISAinfluenza.REF.1">1</a>–<a class="bk_pop" href="#g110-ELISAinfluenza.REF.5">5</a>). Here, ELISA-based method for assay of binding specificity of influenza viruses to sialoglycosphingolipids (gangliosides) (<a class="bk_pop" href="#g110-ELISAinfluenza.REF.1">1</a>–<a class="bk_pop" href="#g110-ELISAinfluenza.REF.3">3</a>) is described.</p></div><div id="g110-ELISAinfluenza.Protocol"><h2 id="_g110-ELISAinfluenza_Protocol_">Protocol</h2><p>The protocol consists of the following three steps: 1) preparation of a ganglioside-coated plate; 2) blocking nonspecific interaction sites on the plate and binding of viruses to specific gangliosides; and 3) detection of binding specificity of influenza viruses to gangliosides.</p><div id="g110-ELISAinfluenza.Materials"><h3>Materials</h3><dl class="temp-labeled-list"><dt>1.</dt><dd><p class="no_top_margin">Ethanol</p></dd><dt>2.</dt><dd><p class="no_top_margin">Plastic plate: F96 polysorp (Nalge Nunc International, Thermo Fisher Scientific, Inc. Massachusetts, USA)</p></dd><dt>3.</dt><dd><p class="no_top_margin">Blocking solution: 1 g of defatted bovine serum albumin (BSA) in 100 mL of PBS</p></dd><dt>4.</dt><dd><p class="no_top_margin">Dilution buffer: 0.5 g of defatted BSA in 100 mL of PBS</p></dd><dt>5.</dt><dd><p class="no_top_margin">Substrate solution: 2 mg of <i>o</i>-phenylenediamine (Sigma-Aldrich, St. Louis, MO) is dissolved in 10 mL of 100 mM of citrate-phosphate buffer (pH 5.5) before addition of 3.3 μL of 30% H<sub>2</sub>O<sub>2</sub></p></dd></dl></div><div id="g110-ELISAinfluenza.Instruments"><h3>Instruments</h3><dl class="temp-labeled-list"><dt>1.</dt><dd><p class="no_top_margin">96-well Polysorp flat-bottomed plates</p></dd><dt>2.</dt><dd><p class="no_top_margin">37°C incubator</p></dd><dt>3.</dt><dd><p class="no_top_margin">ELISA plate reader (BIORAD, California, USA)</p></dd></dl></div><div id="g110-ELISAinfluenza.Methods"><h3>Methods</h3><dl class="temp-labeled-list"><dt>1.</dt><dd><p class="no_top_margin">Preparation of a ganglioside-coated plate</p><dl class="temp-labeled-list"><dt>a.</dt><dd><p class="no_top_margin">Dissolve ganglioside (3–50 pmol/10 μL/well) in ethanol or another organic solvent that has no effect on a plastic plate and serially dilute two-fold with ethanol (<b>Notes 1</b> and <b>2</b>).</p></dd><dt>b.</dt><dd><p class="no_top_margin">Evaporate ethanol at 37°C for several minutes and dry completely with warm air.</p></dd></dl></dd><dt>2.</dt><dd><p class="no_top_margin">Blocking nonspecific interaction sites on the plate and binding of viruses to specific gangliosides</p><dl class="temp-labeled-list"><dt>a.</dt><dd><p class="no_top_margin">Add 250 μL of blocking solution to each well and incubate for 2 h at 37°C.</p></dd><dt>b.</dt><dd><p class="no_top_margin">Wash the wells five times with PBS, add 100 μL of 25 HAUs of influenza virus in PBS, and maintain at 4°C overnight with gentle shaking.</p></dd></dl></dd><dt>3.</dt><dd><p class="no_top_margin">Detection of binding specificity of influenza viruses to gangliosides (<b>Notes 3–5</b>)</p><dl class="temp-labeled-list"><dt>a.</dt><dd><p class="no_top_margin">Wash unbound virus five times with cold PBS, add 100 μL of primary antibody directed to the virus diluted in 0.5% defatted BSA, and maintain for 2 h at 4°C.</p></dd><dt>b.</dt><dd><p class="no_top_margin">Wash five times with PBS to eliminate free primary antibody, add 100 μL of HRP-conjugate secondary antibody in 0.5% defatted BSA, and maintain for 2 h at 4°C.</p></dd><dt>c.</dt><dd><p class="no_top_margin">Wash away unbound conjugate five times with PBS, add 100 μL of coloring solution, and maintain at room temperature until a yellow color develops.</p></dd><dt>d.</dt><dd><p class="no_top_margin">Stop the reaction by adding 50 μL of 1 N H<sub>2</sub>SO<sub>4</sub>. This acidic solution will change color from yellow to orange.</p></dd><dt>e.</dt><dd><p class="no_top_margin">Record the absorbance at 490 nm with a reference wavelength of 630 nm. Before plotting a graph, subtract OD490 from OD630 to obtain the actual values of virus binding activity (for example data, <i>see</i>
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<a class="figpopup" href="/books/NBK593945/figure/g110-ELISAinfluenza.F1/?report=objectonly" target="object" rid-figpopup="figg110ELISAinfluenzaF1" rid-ob="figobg110ELISAinfluenzaF1">Figure 1</a>).</p></dd></dl></dd></dl></div><div id="g110-ELISAinfluenza.Notes"><h3>Notes</h3><dl class="temp-labeled-list"><dt>1.</dt><dd><p class="no_top_margin">For an ELISA-based assay, gangliosides must be purified to coat wells of a flat-bottomed microtiter plate.</p></dd><dt>2.</dt><dd><p class="no_top_margin">The ELISA technique can be used for the quantitative detection of the activity of virus binding to the gangliosides.</p></dd><dt>3.</dt><dd><p class="no_top_margin">The gangliosides and influenza virus materials can be obtained from the same sources as those of the TLC test described in the chapter “Thin-layer chromatography (TLC)-based assay for the determination of influenza virus-host receptor binding specificity,” but a smaller amount (25 HAU, influenza virus: 3–50 pmol/well, ganglioside) can be detected by ELISA. The other reagents are similar to those of TLC except for the abovementioned reagents.</p></dd><dt>4.</dt><dd><p class="no_top_margin">Substrate solution should be freshly mixed before use.</p></dd><dt>5.</dt><dd><p class="no_top_margin">Influenza viruses should be handled in the facility of Biological Safety Level 2 or 3 under the control of national law (<a class="bk_pop" href="#g110-ELISAinfluenza.REF.6">6</a>).</p></dd></dl></div></div><div id="g110-ELISAinfluenza.References"><h2 id="_g110-ELISAinfluenza_References_">References</h2><dl class="temp-labeled-list"><dt>1.</dt><dd><div class="bk_ref" id="g110-ELISAinfluenza.REF.1">Suzuki Y, Nakao T, Ito T, Watanabe N, Toda Y, Xu G, Suzuki T, Kobayashi T, Kimura Y, Yamada A. Structural determination of gangliosides that bind to influenza A, B, and C viruses by an improved binding assay: strain-specific receptor epitopes in sialo-sugar chains. <span><span class="ref-journal">Virology. </span>1992 Jul;<span class="ref-vol">189</span>(1):121–31.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/1376537" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 1376537</span></a>] [<a href="http://dx.crossref.org/10.1016/0042-6822(92)90687-k" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>2.</dt><dd><div class="bk_ref" id="g110-ELISAinfluenza.REF.2">Suzuki T, Portner A, Scroggs RA, Uchikawa M, Koyama N, Matsuo K, Suzuki Y, Takimoto T. Receptor specificities of human respiroviruses. <span><span class="ref-journal">J Virol. </span>2001 May;<span class="ref-vol">75</span>(10):4604–13.</span> [<a href="/pmc/articles/PMC114213/" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pmc">PMC free article<span class="bk_prnt">: PMC114213</span></a>] [<a href="https://pubmed.ncbi.nlm.nih.gov/11312330" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 11312330</span></a>] [<a href="http://dx.crossref.org/10.1128/JVI.75.10.4604-4613.2001" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>3.</dt><dd><div class="bk_ref" id="g110-ELISAinfluenza.REF.3">Shinya K, Hatta M, Yamada S, Takada A, Watanabe S, Halfmann P, Horimoto T, Neumann G, Kim J.H, Lim W, Guan Y, Peiris M, Kiso M, Suzuki T, Suzuki Y, Kawaoka Y. Characterization of a Human H5N1 Influenza A Virus Isolated in 2003. <span><span class="ref-journal">J Virol. </span>2005 Aug;<span class="ref-vol">79</span>(15):9926–32.</span> [<a href="/pmc/articles/PMC1181571/" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pmc">PMC free article<span class="bk_prnt">: PMC1181571</span></a>] [<a href="https://pubmed.ncbi.nlm.nih.gov/16014953" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 16014953</span></a>] [<a href="http://dx.crossref.org/10.1128/JVI.79.15.9926-9932.2005" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>4.</dt><dd><div class="bk_ref" id="g110-ELISAinfluenza.REF.4">Takemae N, Ruttanapumma R, Parchariyanon S, Yoneyama S, Hayashi T, Hiramatsu H, Sriwilaijaroen N, Uchida Y, Kondo S, Yagi H, Kato K, Suzuki Y, Saito T. Alterations in receptor binding properties of swine influenza viruses of H1 subtype after isolation in embryonated chicken eggs. <span><span class="ref-journal">J Gen Virol. </span>2010 Apr;<span class="ref-vol">91</span>(Pt 4):938–48.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/20007353" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 20007353</span></a>] [<a href="http://dx.crossref.org/10.1099/vir.0.016691-0" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>5.</dt><dd><div class="bk_ref" id="g110-ELISAinfluenza.REF.5">Sriwilaijaroen N, Kondo S, Yagi H, Wilairat P, Hiramatsu H, Ito M, Ito Y, Kato K, Suzuki Y. Analysis of N-glycans in embryonated chicken egg chorioallantoic and amniotic cells responsible for binding and adaptation of influenza viruses. <span><span class="ref-journal">Glycoconj J. </span>2009 May;<span class="ref-vol">26</span>(4):433–43.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/18853253" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 18853253</span></a>] [<a href="http://dx.crossref.org/10.1007/s10719-008-9193-x" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>6.</dt><dd><div class="bk_ref" id="g110-ELISAinfluenza.REF.6">
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<a href="https://www.who.int/csr/resources/publications/biosafety/en/Biosafety7.pdf" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">https://www<wbr style="display:inline-block"></wbr>.who.int/csr<wbr style="display:inline-block"></wbr>/resources/publications<wbr style="display:inline-block"></wbr>/biosafety/en/Biosafety7.pdf</a>
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.</div></dd></dl></div><h2 id="NBK593945_footnotes">Footnotes</h2><dl class="temp-labeled-list small"><dt></dt><dd><div id="g110-ELISAinfluenza.FN1"><p class="no_top_margin">The authors declare no competing or financial interests.</p></div></dd></dl><div class="bk_prnt_sctn"><h2>Figures</h2><div class="whole_rhythm bk_prnt_obj bk_first_prnt_obj"><div id="g110-ELISAinfluenza.F1" class="figure bk_fig"><div class="graphic"><img src="/books/NBK593945/bin/g110-ELISAinfluenza-Image001.jpg" alt="Figure 1: . Receptor binding specificity of a highly pathogenic avian influenza virus, A/KongKong/213/03 (H5N1), isolated from humans." /></div><h3><span class="label">Figure 1: </span></h3><div class="caption"><p>Receptor binding specificity of a highly pathogenic avian influenza virus, A/KongKong/213/03 (H5N1), isolated from humans.</p><p>The direct binding activity of viruses to sialylparagloboside (IV<sup>3</sup>(Neu5Ac)Lc4Cer, IV<sup>6</sup>(Neu5Ac)Lc4Cer) was determined as described in this protocol. A/HongKong/213/03 (H5N1) bound to both Neu5Acα2-3paragloboside (IV<sup>3</sup>(Neu5Ac)Lc4Cer) and Neu5Acα2-6paragloboside (IV<sup>6</sup>(Neu5Ac)Lc4Cer), but A/Duck/HongKong/200/01 isolated from duck bound preferentially to Neu5Acα2-3paragloboside (IV<sup>3</sup>(Neu5Ac)Lc4Cer), and A/Memphis/1/71 isolated from human bound preferentially to Neu5Acα2-6paragloboside (IV<sup>6</sup>(Neu5Ac)Lc4Cer).</p></div><div class="permissions">Reprinted from Journal of Virology, 79(15), Shinya K. et al., Characterization of a Human H5N1 Influenza A Virus Isolated in 2003, 9926–32, 2005, with permission from American Society for Microbiology.</div></div></div></div><div id="bk_toc_contnr"></div></div></div>
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<div class="post-content"><div><div class="half_rhythm"><a href="/books/about/copyright/">Copyright Notice</a><p class="small">Licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 4.0 Unported license. To view a copy of this license, visit <a href="http://creativecommons.org/licenses/by-nc-nd/4.0/" ref="pagearea=meta&targetsite=external&targetcat=link&targettype=uri">http://creativecommons.org/licenses/by-nc-nd/4.0/</a>.</p></div><div class="small"><span class="label">Bookshelf ID: NBK593945</span><span class="label">PMID: <a href="https://pubmed.ncbi.nlm.nih.gov/37590682" title="PubMed record of this page" ref="pagearea=meta&targetsite=entrez&targetcat=link&targettype=pubmed">37590682</a></span></div><div style="margin-top:2em" class="bk_noprnt"><a class="bk_cntns" href="/books/n/glycopodv2/">Contents</a><div class="pagination bk_noprnt"><a class="active page_link prev" href="/books/n/glycopodv2/g109-HAassay/" title="Previous page in this title">< Prev</a><a class="active page_link next" href="/books/n/glycopodv2/transporters/" title="Next page in this title">Next ></a></div></div></div></div>
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