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<title>Role of ganglioside GM1a in infection by human rotaviruses - Glycoscience Protocols (GlycoPODv2) - NCBI Bookshelf</title>
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<meta name="robots" content="INDEX,FOLLOW,NOARCHIVE" /><meta name="citation_inbook_title" content="Glycoscience Protocols (GlycoPODv2) [Internet]" /><meta name="citation_title" content="Role of ganglioside GM1a in infection by human rotaviruses" /><meta name="citation_publisher" content="Japan Consortium for Glycobiology and Glycotechnology" /><meta name="citation_date" content="2022/03/20" /><meta name="citation_author" content="Yasuo Suzuki" /><meta name="citation_author" content="Chao-Tan Guo" /><meta name="citation_pmid" content="37590757" /><meta name="citation_fulltext_html_url" content="https://www.ncbi.nlm.nih.gov/books/NBK594034/" /><meta name="citation_keywords" content="rotavirus" /><meta name="citation_keywords" content="receptor" /><meta name="citation_keywords" content="ganglioside" /><link rel="schema.DC" href="http://purl.org/DC/elements/1.0/" /><meta name="DC.Title" content="Role of ganglioside GM1a in infection by human rotaviruses" /><meta name="DC.Type" content="Text" /><meta name="DC.Publisher" content="Japan Consortium for Glycobiology and Glycotechnology" /><meta name="DC.Contributor" content="Yasuo Suzuki" /><meta name="DC.Contributor" content="Chao-Tan Guo" /><meta name="DC.Date" content="2022/03/20" /><meta name="DC.Identifier" content="https://www.ncbi.nlm.nih.gov/books/NBK594034/" /><meta name="description" content="Rotaviruses are the major cause of severe gastroenteritis in infants and children in developed and developing countries. Based on their ability to infect host cells treated with sialidase, rotaviruses are classified into two types: sialidase-sensitive strains and sialidase-insensitive strains (1). In the sialidase-insensitive strains, neither infection nor hemagglutination of most human rotaviruses was inhibited by pretreatment of target cells with sialidase from Arthrobacter ureafaciens (2). The mechanism of the feature of carbohydrate residues through which human rotaviruses enter the host cells has been studied (3–5). This protocol was focused on the inhibitory activity of exogenous sialidase-resistant gangliosides GM1a on the infection of host cells by sialidase-insensitive human rotaviruses (KUN and MO strains) (3)." /><meta name="og:title" content="Role of ganglioside GM1a in infection by human rotaviruses" /><meta name="og:type" content="book" /><meta name="og:description" content="Rotaviruses are the major cause of severe gastroenteritis in infants and children in developed and developing countries. Based on their ability to infect host cells treated with sialidase, rotaviruses are classified into two types: sialidase-sensitive strains and sialidase-insensitive strains (1). In the sialidase-insensitive strains, neither infection nor hemagglutination of most human rotaviruses was inhibited by pretreatment of target cells with sialidase from Arthrobacter ureafaciens (2). The mechanism of the feature of carbohydrate residues through which human rotaviruses enter the host cells has been studied (3–5). This protocol was focused on the inhibitory activity of exogenous sialidase-resistant gangliosides GM1a on the infection of host cells by sialidase-insensitive human rotaviruses (KUN and MO strains) (3)." /><meta name="og:url" content="https://www.ncbi.nlm.nih.gov/books/NBK594034/" /><meta name="og:site_name" content="NCBI Bookshelf" /><meta name="og:image" content="https://www.ncbi.nlm.nih.gov/corehtml/pmc/pmcgifs/bookshelf/thumbs/th-glycopodv2-lrg.png" /><meta name="twitter:card" content="summary" /><meta name="twitter:site" content="@ncbibooks" /><meta name="bk-non-canon-loc" content="/books/n/glycopodv2/g178-gm1arota/" /><link rel="canonical" href="https://www.ncbi.nlm.nih.gov/books/NBK594034/" /><link rel="stylesheet" href="/corehtml/pmc/css/figpopup.css" type="text/css" media="screen" /><link rel="stylesheet" href="/corehtml/pmc/css/bookshelf/2.26/css/books.min.css" type="text/css" /><link rel="stylesheet" href="/corehtml/pmc/css/bookshelf/2.26/css/books_print.min.css" type="text/css" /><style type="text/css">p a.figpopup{display:inline !important} .bk_tt {font-family: monospace} .first-line-outdent .bk_ref {display: inline} </style><script type="text/javascript" src="/corehtml/pmc/js/jquery.hoverIntent.min.js"> </script><script type="text/javascript" src="/corehtml/pmc/js/common.min.js?_=3.18"> </script><script type="text/javascript">window.name="mainwindow";</script><script type="text/javascript" src="/corehtml/pmc/js/bookshelf/2.26/book-toc.min.js"> </script><script type="text/javascript" src="/corehtml/pmc/js/bookshelf/2.26/books.min.js"> </script>
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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="_NBK594034_"><span class="title" itemprop="name">Role of ganglioside GM1a in infection by human rotaviruses</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">Chao-Tan Guo</span>, Ph.D.<div class="affiliation small">Institute of Bioengineering, Zhejiang Academy of Medical Sciences<div><span class="email-label">Email: </span><a href="mailto:dev@null" data-email="pj.oc.oohay@0002natoahcg" class="oemail">pj.oc.oohay@0002natoahcg</a></div></div></div><p class="small">Created: <span itemprop="datePublished">November 24, 2021</span>; Last Revision: <span itemprop="dateModified">March 20, 2022</span>.</p></div><div class="body-content whole_rhythm" itemprop="text"><div id="g178-gm1arota.Introduction"><h2 id="_g178-gm1arota_Introduction_">Introduction</h2><p>Rotaviruses are the major cause of severe gastroenteritis in infants and children in developed and developing countries. Based on their ability to infect host cells treated with sialidase, rotaviruses are classified into two types: sialidase-sensitive strains and sialidase-insensitive strains (<a class="bk_pop" href="#g178-gm1arota.REF.1">1</a>). In the sialidase-insensitive strains, neither infection nor hemagglutination of most human rotaviruses was inhibited by pretreatment of target cells with sialidase from <i>Arthrobacter ureafaciens</i> (<a class="bk_pop" href="#g178-gm1arota.REF.2">2</a>). The mechanism of the feature of carbohydrate residues through which human rotaviruses enter the host cells has been studied (<a class="bk_pop" href="#g178-gm1arota.REF.3">3</a>–<a class="bk_pop" href="#g178-gm1arota.REF.5">5</a>). This protocol was focused on the inhibitory activity of exogenous sialidase-resistant gangliosides GM1a on the infection of host cells by sialidase-insensitive human rotaviruses (KUN and MO strains) (<a class="bk_pop" href="#g178-gm1arota.REF.3">3</a>).</p></div><div id="g178-gm1arota.Protocol"><h2 id="_g178-gm1arota_Protocol_">Protocol</h2><p>The protocol for testing inhibitory activity of GM1a for rotavirus infection of MA104 cells is divided into three steps: 1. preparation of cells, rotaviruses, and gangliosides; 2. pretreatment, viral adsorption, and treatment; and 3. determination of GM1a inhibitory activity by an indirect immunostaining procedure.</p><div id="g178-gm1arota.Materials"><h3>Materials</h3><dl class="temp-labeled-list"><dt>1.</dt><dd><p class="no_top_margin">Rotaviruses: Human (KUN and MO strains) and feline (FRV64 strain) rotaviruses were propagated in embryonic rhesus monkey kidney cells (MA104 cells) as described previously (<a class="bk_pop" href="#g178-gm1arota.REF.3">3</a>) (<b>Note 1</b>).</p></dd><dt>2.</dt><dd><p class="no_top_margin">Gangliosides: Native gangliosides can be isolated from various tissues. Ganglio-series gangliosides, such as GM1a, GM1b, GD1a, GD1b, GT1a, GT1b, and GQ1b are mainly found in and taken from brains of mammals, including bovine, pig, and horse using anion-exchange and iatrobeads column chromatography (<a class="bk_pop" href="#g178-gm1arota.REF.3">3</a>). GA1 was prepared from GM1a.</p></dd><dt>3.</dt><dd><p class="no_top_margin">Antibodies: Guinea pig anti-FRV-64 antiserum was prepared as follows: Four weeks-old pathogen-free guinea pigs were immunized with purified feline rotavirus FRV64 strain by intramuscular injection. One month later, the guinea pigs were boosted with a similar intraperitoneal injection. The sera of immunized guinea pigs (anti-FRV64 antisera) were harvested and purified after one week. The antisera crossreacted with human rotaviruses KUN and MO strains (<a class="bk_pop" href="#g178-gm1arota.REF.3">3</a>).</p></dd><dt>4.</dt><dd><p class="no_top_margin">Horse radish peroxidase (HRP)-conjugated protein A was purchased from Organon Teknika N.V. Cappel Products.</p></dd></dl></div><div id="g178-gm1arota.Instruments"><h3>Instruments</h3><dl class="temp-labeled-list"><dt>1.</dt><dd><p class="no_top_margin">Microscopy</p></dd><dt>2.</dt><dd><p class="no_top_margin">CO<sub>2</sub> incubator</p></dd></dl></div><div id="g178-gm1arota.Methods"><h3>Methods</h3><dl class="temp-labeled-list"><dt>1.</dt><dd><p class="no_top_margin">Preparation of cells, rotaviruses, and gangliosides</p><dl class="temp-labeled-list"><dt>a.</dt><dd><p class="no_top_margin">MA104 cells were grown in MEM supplemented with 10% fetal bovine serum (FBS) at 37°C in a humidified 95% air, 5% CO<sub>2</sub> incubator.</p></dd><dt>b.</dt><dd><p class="no_top_margin">The viruses were titrated to determine a dilution giving ~200 staining focus-forming units per well of 96-well microtiter tray.</p></dd><dt>c.</dt><dd><p class="no_top_margin">Exogenous ganglioside GM1a (starting concentration, 50 μM) was serially diluted with PBS (20 mM of phosphate-buffered saline, pH 7.0).</p></dd></dl></dd><dt>2.</dt><dd><p class="no_top_margin">Pretreatment, viral adsorption, and treatment</p><dl class="temp-labeled-list"><dt>a.</dt><dd><p class="no_top_margin">Mix ganglioside GM1a with an equal volume of trypsin-activated viruses (preincubated with 10 μg/mL of trypsin for 30 min at 37°C) and maintain for 1 h at 37°C.</p></dd><dt>b.</dt><dd><p class="no_top_margin">Add the ganglioside GM1a/virus mixture to MA104 cells and adsorb for 1 h at 37°C.</p></dd><dt>c.</dt><dd><p class="no_top_margin">Replace the ganglioside GM1a/virus mixture with the maintenance medium (MEM supplemented with 2% FBS) and leave for 16 h at 37°C. Then, wash the cells with PBS.</p></dd></dl></dd><dt>3.</dt><dd><p class="no_top_margin">Determination of GM1a inhibitory activity by an indirect immunostaining procedure (for example data, see <a class="figpopup" href="/books/NBK594034/figure/g178-gm1arota.F1/?report=objectonly" target="object" rid-figpopup="figg178gm1arotaF1" rid-ob="figobg178gm1arotaF1">Figure 1</a>)</p><dl class="temp-labeled-list"><dt>a.</dt><dd><p class="no_top_margin">Fix the infected MA104 cells 80% acetone for 10 min and wash thrice with PBS.</p></dd><dt>b.</dt><dd><p class="no_top_margin">Incubate the fixed cells with PBS containing anti-FRV64 antiserum at 37°C for 30 min. Then, wash the cells with PBS.</p></dd><dt>c.</dt><dd><p class="no_top_margin">Incubate the cells with PBS containing HRP-conjugated protein A at 37°C for 30 min and stained with a solution containing 50 mM of Tris buffer (pH 7.5), 0.5 mg/mL of 3.3’-diaminobenzidine tetrahydrochloride, and 0.01% H<sub>2</sub>O<sub>2</sub> aqueous for 20 min at 4°C and wash thrice with PBS.</p></dd><dt>d.</dt><dd><p class="no_top_margin">Count the stained cells under light microscopy.</p></dd></dl></dd></dl></div><div id="g178-gm1arota.Note"><h3>Note</h3><dl class="temp-labeled-list"><dt>1.</dt><dd><p class="no_top_margin">Rotaviruses should be handled in the facility of Biological Safety Level 2 under the control of national law (<a class="bk_pop" href="#g178-gm1arota.REF.6">6</a>).</p></dd></dl></div></div><div id="g178-gm1arota.References"><h2 id="_g178-gm1arota_References_">References</h2><dl class="temp-labeled-list"><dt>1.</dt><dd><div class="bk_ref" id="g178-gm1arota.REF.1">Mendez E, Arias C.F, and Lopez S.A. Interactions between the two surface proteins of rotavirus may alter the receptor binding specificity of the virus. J Virol. 1996 Feb;70(2):1218-22. doi: 10.1128/JVI.70.2.1218-1222.1996.PMID: 8551583. [<a href="/pmc/articles/PMC189931/" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pmc">PMC free article<span class="bk_prnt">: PMC189931</span></a>] [<a href="https://pubmed.ncbi.nlm.nih.gov/8551583" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 8551583</span></a>] [<a href="http://dx.crossref.org/10.1128/JVI.70.2.1218-1222.1996.PMID" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>2.</dt><dd><div class="bk_ref" id="g178-gm1arota.REF.2">Yolken RH, Willoughby R, Wee SB, Miskuff R, Vonderfecht S. Sialic acid glycoprotein inhibits in vitro and in vivo replication of rotavirus. <span><span class="ref-journal">J Clin Invest. </span>1987 Jan;<span class="ref-vol">79</span>(1):148–54.</span> [<a href="/pmc/articles/PMC424010/" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pmc">PMC free article<span class="bk_prnt">: PMC424010</span></a>] [<a href="https://pubmed.ncbi.nlm.nih.gov/3025257" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 3025257</span></a>] [<a href="http://dx.crossref.org/10.1172/JCI112775" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>3.</dt><dd><div class="bk_ref" id="g178-gm1arota.REF.3">Guo Chao-Tan, Nakagomi O, Mochizuki M, Ishida H, Kiso M, Ohta Y, Suzuki T, Miyamoto D, Hidari KI, Suzuki Y. Ganglioside GM1a on the cell surface is involved in the infection by human rotavirus KUN and MO strains. <span><span class="ref-journal">J Biochem. </span>1999 Oct;<span class="ref-vol">126</span>(4):683–8.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/10502675" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 10502675</span></a>] [<a href="http://dx.crossref.org/10.1093/oxfordjournals.jbchem.a022503" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>4.</dt><dd><div class="bk_ref" id="g178-gm1arota.REF.4">Haselhorst T, Fleming FE, Dyason JD, Hartnell RD, Yu X, Holloway G, Santegoets K, Kiefel MJ, Blanchard H, Coulson BS, von Itzstein M. Sialic acid depencence in rotavirus host cell invasion. <span><span class="ref-journal">Nat Chem Biol. </span>2009 Feb;<span class="ref-vol">5</span>(2):91–3.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/19109595" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 19109595</span></a>] [<a href="http://dx.crossref.org/10.1038/nchembio.134" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>5.</dt><dd><div class="bk_ref" id="g178-gm1arota.REF.5">Banda K, Kang G, Varki A. Sialidase sensitivity of rotaviruses revisited. <span><span class="ref-journal">Nat Chem Biol. </span>2009 Feb;<span class="ref-vol">5</span>(2):71–2.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/19148170" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 19148170</span></a>] [<a href="http://dx.crossref.org/10.1038/nchembio0209-71" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>6.</dt><dd><div class="bk_ref" id="g178-gm1arota.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="NBK594034_footnotes">Footnotes</h2><dl class="temp-labeled-list small"><dt></dt><dd><div id="g178-gm1arota.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="g178-gm1arota.F1" class="figure bk_fig"><div class="graphic"><img src="/books/NBK594034/bin/g178-gm1arota-Image001.jpg" alt="Figure 1: . Inhibitory activity of exogenous ganglioside GM1a on the infection of MA104 cells by rotaviruses." /></div><h3><span class="label">Figure 1: </span></h3><div class="caption"><p>Inhibitory activity of exogenous ganglioside GM1a on the infection of MA104 cells by rotaviruses.</p><p>The inhibitory activity of GM1a (closed) and GA1 (asialo GM1) (open), which are used as controls for the infections KUN (triangle), MO (inverted triangle), and FRV64 (circle) strains of MA104 cells, was determined using a neutralization assay as described above.</p></div><div class="permissions">Reprinted from J. Biochem., 126, Chao-Tan Guo, et al., Ganglioside GM1a on the cell surface is involved in the infection by human rotavirus KUN and MO strains, 683–688, 1999 with permission from The Japanese Biochemical Society.</div></div></div></div><div id="bk_toc_contnr"></div></div></div>
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