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<title>Complex and Varied Structures of Glycosylphosphatidylinositol (GPI) Anchors - Essentials of Glycobiology - NCBI Bookshelf</title>
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<meta name="robots" content="INDEX,FOLLOW,NOARCHIVE" /><meta name="citation_inbook_title" content="Essentials of Glycobiology [Internet]. 4th edition" /><meta name="citation_title" content="Complex and Varied Structures of Glycosylphosphatidylinositol (GPI) Anchors" /><meta name="citation_publisher" content="Cold Spring Harbor Laboratory Press" /><meta name="citation_date" content="2022" /><meta name="citation_author" content="Sneha Sudha Komath" /><meta name="citation_author" content="Morihisa Fujita" /><meta name="citation_author" content="Gerald W Hart" /><meta name="citation_author" content="Michael AJ Ferguson" /><meta name="citation_author" content="Taroh Kinoshita" /><meta name="citation_fulltext_html_url" content="https://www.ncbi.nlm.nih.gov/books/NBK579919/" /><link rel="schema.DC" href="http://purl.org/DC/elements/1.0/" /><meta name="DC.Title" content="Complex and Varied Structures of Glycosylphosphatidylinositol (GPI) Anchors" /><meta name="DC.Type" content="Text" /><meta name="DC.Publisher" content="Cold Spring Harbor Laboratory Press" /><meta name="DC.Contributor" content="Sneha Sudha Komath" /><meta name="DC.Contributor" content="Morihisa Fujita" /><meta name="DC.Contributor" content="Gerald W Hart" /><meta name="DC.Contributor" content="Michael AJ Ferguson" /><meta name="DC.Contributor" content="Taroh Kinoshita" /><meta name="DC.Date" content="2022" /><meta name="DC.Identifier" content="https://www.ncbi.nlm.nih.gov/books/NBK579919/" /><meta name="description" content="Panels I and II represent structures of GPI anchors found in lower eukaryotes while panels III and IV represent those observed in higher eukaryotes. With the exception of Entamoeba histolytica proteophosphoglycan (PPG) (panel I), all known protein-linked GPI anchors have the same minimal core structure embellished with species- and tissue-specific side-chain and lipid variations. In mammalian cells, ethanolamine-PO4 on α1-6-linked Man (Man-2) rather than α1-2-linked Man (Man-3) is preferentially used to attach GPI to some GPI-anchored proteins. Aspergillus fumigatus galactomannan (panel II) is unusual in that it lacks the linking ethanolamine residue; instead its GPI portion is linked to the galactomannan chain via a fourth mannose residue. Those fungal GPI-APs that are present on the cell wall are normally linked to the underlying beta-glucan layer after loss of the glucosaminylphospholipid moiety. Soluble GPI structures are released from the cell surface by the action of phosphatidylinositol-specific phospholipase C (PI-PLC) or GPI-specific phospholipase D (GPI-PLD). (±) Glycosyl heterogeneity; curved arrows for the Saccharomyces examples in panel II, the two terminal αMan residues are mutually exclusive; (*) unknown lipid type or chain length. Chain lengths and degrees of unsaturation of the lipids are indicated. For the monosaccharide symbol code, see Online Appendix 1B. PSP, promastigote surface protease; VSG, variant surface glycoprotein; GARP, glutamic acid/alanine-rich protein; TS, trans-sialidase; VSA, variant surface antigen; GPI-APs, glycosylphosphatidylinositol-anchored proteins; PSA, prespore antigen; AGP, arabinogalactan protein; AChE, acetylcholinesterase; eAChE, erythrocyte acetylcholinesterase; MDP, metallodipeptidase; NCAM, neural cell adhesion molecule; PLAP, placental alkaline phosphatase." /><meta name="og:title" content="Complex and Varied Structures of Glycosylphosphatidylinositol (GPI) Anchors" /><meta name="og:type" content="book" /><meta name="og:description" content="Panels I and II represent structures of GPI anchors found in lower eukaryotes while panels III and IV represent those observed in higher eukaryotes. With the exception of Entamoeba histolytica proteophosphoglycan (PPG) (panel I), all known protein-linked GPI anchors have the same minimal core structure embellished with species- and tissue-specific side-chain and lipid variations. In mammalian cells, ethanolamine-PO4 on α1-6-linked Man (Man-2) rather than α1-2-linked Man (Man-3) is preferentially used to attach GPI to some GPI-anchored proteins. Aspergillus fumigatus galactomannan (panel II) is unusual in that it lacks the linking ethanolamine residue; instead its GPI portion is linked to the galactomannan chain via a fourth mannose residue. Those fungal GPI-APs that are present on the cell wall are normally linked to the underlying beta-glucan layer after loss of the glucosaminylphospholipid moiety. Soluble GPI structures are released from the cell surface by the action of phosphatidylinositol-specific phospholipase C (PI-PLC) or GPI-specific phospholipase D (GPI-PLD). (±) Glycosyl heterogeneity; curved arrows for the Saccharomyces examples in panel II, the two terminal αMan residues are mutually exclusive; (*) unknown lipid type or chain length. Chain lengths and degrees of unsaturation of the lipids are indicated. For the monosaccharide symbol code, see Online Appendix 1B. PSP, promastigote surface protease; VSG, variant surface glycoprotein; GARP, glutamic acid/alanine-rich protein; TS, trans-sialidase; VSA, variant surface antigen; GPI-APs, glycosylphosphatidylinositol-anchored proteins; PSA, prespore antigen; AGP, arabinogalactan protein; AChE, acetylcholinesterase; eAChE, erythrocyte acetylcholinesterase; MDP, metallodipeptidase; NCAM, neural cell adhesion molecule; PLAP, placental alkaline phosphatase." /><meta name="og:url" content="https://www.ncbi.nlm.nih.gov/books/NBK579919/" /><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-glyco4-lrg.png" /><meta name="twitter:card" content="summary" /><meta name="twitter:site" content="@ncbibooks" /><meta name="bk-non-canon-loc" content="/books/n/glyco4/a12B_app_gpi_anchor_struct-IV/" /><link rel="canonical" href="https://www.ncbi.nlm.nih.gov/books/NBK579919/" /><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>Varki A, Cummings RD, Esko JD, et al., editors. Essentials of Glycobiology [Internet]. 4th edition. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 2022. </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="_NBK579919_"><span class="label">Online Appendix 12B-IV</span><span class="title" itemprop="name">Complex and Varied Structures of Glycosylphosphatidylinositol (GPI) Anchors</span></h1><p class="contrib-group"><h4>Authors</h4><span itemprop="author">Sneha Sudha Komath</span>, <span itemprop="author">Morihisa Fujita</span>, <span itemprop="author">Gerald W Hart</span>, <span itemprop="author">Michael AJ Ferguson</span>, and <span itemprop="author">Taroh Kinoshita</span><sup><img src="/corehtml/pmc/pmcgifs/corrauth.gif" alt="corresponding author" /></sup><sup>1</sup>.</p><h4>Contact</h4><div class="affiliation"><sup>1</sup> <span class="email-label">Email: </span><a href="mailto:dev@null" data-email="pj.ca.u-akaso.nekib@ihsonikt" class="oemail">pj.ca.u-akaso.nekib@ihsonikt</a></div><div><sup><img src="/corehtml/pmc/pmcgifs/corrauth.gif" alt="corresponding author" /></sup>Corresponding author.</div></div><div class="body-content whole_rhythm" itemprop="text"><p>
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</p><p>Panels I and II represent structures of GPI anchors found in lower eukaryotes while panels III and IV represent those observed in higher eukaryotes. With the exception of <i>Entamoeba histolytica</i> proteophosphoglycan (PPG) (panel I), all known protein-linked GPI anchors have the same minimal core structure embellished with species- and tissue-specific side-chain and lipid variations. In mammalian cells, ethanolamine-PO<sub>4</sub> on α1-6-linked Man (Man-2) rather than α1-2-linked Man (Man-3) is preferentially used to attach GPI to some GPI-anchored proteins. <i>Aspergillus fumigatus</i> galactomannan (panel II) is unusual in that it lacks the linking ethanolamine residue; instead its GPI portion is linked to the galactomannan chain via a fourth mannose residue. Those fungal GPI-APs that are present on the cell wall are normally linked to the underlying beta-glucan layer after loss of the glucosaminylphospholipid moiety. Soluble GPI structures are released from the cell surface by the action of phosphatidylinositol-specific phospholipase C (PI-PLC) or GPI-specific phospholipase D (GPI-PLD). (±) Glycosyl heterogeneity; <i>curved arrows</i> for the <i>Saccharomyces</i> examples in panel <i>II</i>, the two terminal αMan residues are mutually exclusive; (*) unknown lipid type or chain length. Chain lengths and degrees of unsaturation of the lipids are indicated. For the monosaccharide symbol code, see <a href="/books/n/glyco4/a1A_app_discoveries/">Online Appendix 1B</a>. PSP, promastigote surface protease; VSG, variant surface glycoprotein; GARP, glutamic acid/alanine-rich protein; TS, <i>trans</i>-sialidase; VSA, variant surface antigen; GPI-APs, glycosylphosphatidylinositol-anchored proteins; PSA, prespore antigen; AGP, arabinogalactan protein; AChE, acetylcholinesterase; eAChE, erythrocyte acetylcholinesterase; MDP, metallodipeptidase; NCAM, neural cell adhesion molecule; PLAP, placental alkaline phosphatase.</p><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</a> © 2022 by the Consortium of Glycobiology Editors, La Jolla, California. Published by Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York. All rights reserved.<p class="small">The content of this book is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 4.0 Unported license. To view the terms and conditions of this license, visit <a href="https://creativecommons.org/licenses/by-nc-nd/4.0/" ref="pagearea=meta&targetsite=external&targetcat=link&targettype=uri">https://creativecommons.org/licenses/by-nc-nd/4.0/</a></p></div><div class="small"><span class="label">Bookshelf ID: NBK579919</span></div><div style="margin-top:2em" class="bk_noprnt"><a class="bk_cntns" href="/books/n/glyco4/">Contents</a><div class="pagination bk_noprnt"><a class="active page_link prev" href="/books/n/glyco4/a12B_app_gpi_anchor_struct-III/" title="Previous page in this title">< Prev</a><a class="active page_link next" href="/books/n/glyco4/a12B_app_gpi_anchor_struct-V/" title="Next page in this title">Next ></a></div></div></div></div>
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