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Delineation of the epitope recognized by an antibody specific for N-glycolylneuraminic acid—containing gangliosides

Delineation of the epitope recognized by an antibody specific for N-glycolylneuraminic... P3 is a mouse monoclonal antibody (mAb) that binds to several NeuGc-containing gangliosides. It also reacts with antigens expressed in human breast tumors ( Vázquez et al. (1995) Hybridoma , 14, 551–556 ). In this work, the binding specificity of P3 has been characterized in more detail using a panel of glycolipids that included several disialylated gangliosides and several chemical derivatives of NeuGc-GM3. The carboxyl group and the nitrogen function of sialic acid were found to play important roles in the antibody binding, whereas the glycerol tail appears to be nonrelevant. Molecular modeling was used to analyze the binding data, including the finding that P3 selectively recognizes the internal NeuGc in GD3. For this purpose, conformational studies of GD3 were performed using molecular dynamics. It was concluded that sialic acid binds the P3 antibody through its upper face (the one on which the carboxyl group is exposed) and the C4-C5 side of the sugar ring, whereas none or very little contact between the galactose residue and the protein is evident. Conformational analysis of GD3 revealed that, despite the large flexibility of the NeuGcα8NeuGc linkage, the P3 binding epitope on the external sialic acid is not well exposed for any of the possible conformations this linkage can adopt, whereas the internal sialic acid presents the epitope in a proper way for several of these conformations. As a final result, a coherent picture of the epitope that fits the wide binding data was obtained. Key words Key words epitope ganglioside molecular modeling monoclonal antibody NeuGc © 1998 Oxford University Press « Previous | Next Article » Table of Contents This Article Glycobiology (1998) 8 (7): 695-705. » Abstract Free Full Text (HTML) Free Full Text (PDF) Free Classifications Article Services Article metrics Alert me when cited Alert me if corrected Find similar articles Similar articles in Web of Science Similar articles in PubMed Add to my archive Download citation Request Permissions Disclaimer Citing Articles Load citing article information Citing articles via CrossRef Citing articles via Scopus Citing articles via Web of Science Citing articles via Google Scholar Google Scholar Articles by Moreno, E. Articles by Pérez, R. Search for related content PubMed PubMed citation Articles by Moreno, E. Articles by Lanne, B. Articles by Vázquez, A. M. Articles by Kawashima, I. Articles by Tai, T. Articles by Fernández, L. E. Articles by Karlsson, K. A. Articles by Ångström, J. Articles by Pérez, R. Related Content Load related web page information Share Email this article CiteULike Delicious Facebook Google+ Mendeley Twitter What's this? Search this journal: Advanced » Current Issue November 2015 25 (11) Alert me to new issues The Journal Submit now! About this journal Rights & Permissions Manuscript submission & review Dispatch date of the next issue This journal is a member of the Committee on Publication Ethics (COPE) We are mobile – find out more Journals Career Network Glycoscience resources Consortium for Functional Glycomics The Official Journal of The Society for Glycobiology Impact factor: 3.147 5-Yr impact factor: 3.212 Editor-in-Chief Robert S. Haltiwanger View full editorial board For Authors Instructions to authors Self-archiving policy Online submission Open access options for authors - visit Oxford Open This journal enables compliance with the NIH Public Access Policy Alerting Services Email table of contents Email Advance Access CiteTrack XML RSS feed Corporate Services Advertising sales Classified Advertising Reprints Supplements var taxonomies = ("SCI01000"); Most Most Read Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds A "Glyconutrient Sham" Formation of the glycan chains in the synthesis of bacterial peptidoglycan Fucose: biosynthesis and biological function in mammals Optimal and consistent protein glycosylation in mammalian cell culture » View all Most Read articles Most Cited Biological roles of oligosaccharides: all of the theories are correct Prediction, conservation analysis, and structural characterization of mammalian mucin-type O-glycosylation sites An evolving view of the eukaryotic oligosaccharyltransferase Evolutionary considerations in relating oligosaccharide diversity to biological function Glycosidases of the asparagine-linked oligosaccharide processing pathway » View all Most Cited articles Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department. Online ISSN 1460-2423 - Print ISSN 0959-6658 Copyright © 2015 Oxford University Press Oxford Journals Oxford University Press Site Map Privacy Policy Cookie Policy Legal Notices Frequently Asked Questions Other Oxford University Press sites: Oxford University Press Oxford Journals China Oxford Journals Japan Academic & Professional books Children's & Schools Books Dictionaries & Reference Dictionary of National Biography Digital Reference English Language Teaching Higher Education Textbooks International Education Unit Law Medicine Music Online Products & Publishing Oxford Bibliographies Online Oxford Dictionaries Online Oxford English Dictionary Oxford Language Dictionaries Online Oxford Scholarship Online Reference Rights and Permissions Resources for Retailers & Wholesalers Resources for the Healthcare Industry Very Short Introductions World's Classics function fnc_onDomLoaded() { var query_context = getQueryContext(); PF_initOIUnderbar(query_context,":QS:default","","JRN"); PF_insertOIUnderbar(0); }; if (window.addEventListener) { window.addEventListener('load', fnc_onDomLoaded, false); } else if (window.attachEvent) { window.attachEvent('onload', fnc_onDomLoaded); } var gaJsHost = (("https:" == document.location.protocol) ? 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Delineation of the epitope recognized by an antibody specific for N-glycolylneuraminic acid—containing gangliosides

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Publisher
Oxford University Press
Copyright
Copyright © 2015 Oxford University Press
ISSN
0959-6658
eISSN
1460-2423
DOI
glycob;8/7/695
Publisher site
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Abstract

P3 is a mouse monoclonal antibody (mAb) that binds to several NeuGc-containing gangliosides. It also reacts with antigens expressed in human breast tumors ( Vázquez et al. (1995) Hybridoma , 14, 551–556 ). In this work, the binding specificity of P3 has been characterized in more detail using a panel of glycolipids that included several disialylated gangliosides and several chemical derivatives of NeuGc-GM3. The carboxyl group and the nitrogen function of sialic acid were found to play important roles in the antibody binding, whereas the glycerol tail appears to be nonrelevant. Molecular modeling was used to analyze the binding data, including the finding that P3 selectively recognizes the internal NeuGc in GD3. For this purpose, conformational studies of GD3 were performed using molecular dynamics. It was concluded that sialic acid binds the P3 antibody through its upper face (the one on which the carboxyl group is exposed) and the C4-C5 side of the sugar ring, whereas none or very little contact between the galactose residue and the protein is evident. Conformational analysis of GD3 revealed that, despite the large flexibility of the NeuGcα8NeuGc linkage, the P3 binding epitope on the external sialic acid is not well exposed for any of the possible conformations this linkage can adopt, whereas the internal sialic acid presents the epitope in a proper way for several of these conformations. As a final result, a coherent picture of the epitope that fits the wide binding data was obtained. Key words Key words epitope ganglioside molecular modeling monoclonal antibody NeuGc © 1998 Oxford University Press « Previous | Next Article » Table of Contents This Article Glycobiology (1998) 8 (7): 695-705. » Abstract Free Full Text (HTML) Free Full Text (PDF) Free Classifications Article Services Article metrics Alert me when cited Alert me if corrected Find similar articles Similar articles in Web of Science Similar articles in PubMed Add to my archive Download citation Request Permissions Disclaimer Citing Articles Load citing article information Citing articles via CrossRef Citing articles via Scopus Citing articles via Web of Science Citing articles via Google Scholar Google Scholar Articles by Moreno, E. Articles by Pérez, R. Search for related content PubMed PubMed citation Articles by Moreno, E. Articles by Lanne, B. Articles by Vázquez, A. M. Articles by Kawashima, I. Articles by Tai, T. Articles by Fernández, L. E. Articles by Karlsson, K. A. Articles by Ångström, J. Articles by Pérez, R. Related Content Load related web page information Share Email this article CiteULike Delicious Facebook Google+ Mendeley Twitter What's this? Search this journal: Advanced » Current Issue November 2015 25 (11) Alert me to new issues The Journal Submit now! About this journal Rights & Permissions Manuscript submission & review Dispatch date of the next issue This journal is a member of the Committee on Publication Ethics (COPE) We are mobile – find out more Journals Career Network Glycoscience resources Consortium for Functional Glycomics The Official Journal of The Society for Glycobiology Impact factor: 3.147 5-Yr impact factor: 3.212 Editor-in-Chief Robert S. Haltiwanger View full editorial board For Authors Instructions to authors Self-archiving policy Online submission Open access options for authors - visit Oxford Open This journal enables compliance with the NIH Public Access Policy Alerting Services Email table of contents Email Advance Access CiteTrack XML RSS feed Corporate Services Advertising sales Classified Advertising Reprints Supplements var taxonomies = ("SCI01000"); Most Most Read Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds A "Glyconutrient Sham" Formation of the glycan chains in the synthesis of bacterial peptidoglycan Fucose: biosynthesis and biological function in mammals Optimal and consistent protein glycosylation in mammalian cell culture » View all Most Read articles Most Cited Biological roles of oligosaccharides: all of the theories are correct Prediction, conservation analysis, and structural characterization of mammalian mucin-type O-glycosylation sites An evolving view of the eukaryotic oligosaccharyltransferase Evolutionary considerations in relating oligosaccharide diversity to biological function Glycosidases of the asparagine-linked oligosaccharide processing pathway » View all Most Cited articles Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department. Online ISSN 1460-2423 - Print ISSN 0959-6658 Copyright © 2015 Oxford University Press Oxford Journals Oxford University Press Site Map Privacy Policy Cookie Policy Legal Notices Frequently Asked Questions Other Oxford University Press sites: Oxford University Press Oxford Journals China Oxford Journals Japan Academic & Professional books Children's & Schools Books Dictionaries & Reference Dictionary of National Biography Digital Reference English Language Teaching Higher Education Textbooks International Education Unit Law Medicine Music Online Products & Publishing Oxford Bibliographies Online Oxford Dictionaries Online Oxford English Dictionary Oxford Language Dictionaries Online Oxford Scholarship Online Reference Rights and Permissions Resources for Retailers & Wholesalers Resources for the Healthcare Industry Very Short Introductions World's Classics function fnc_onDomLoaded() { var query_context = getQueryContext(); PF_initOIUnderbar(query_context,":QS:default","","JRN"); PF_insertOIUnderbar(0); }; if (window.addEventListener) { window.addEventListener('load', fnc_onDomLoaded, false); } else if (window.attachEvent) { window.attachEvent('onload', fnc_onDomLoaded); } var gaJsHost = (("https:" == document.location.protocol) ? "https://ssl." : "http://www."); document.write(unescape("%3Cscript src='" + gaJsHost + "google-analytics.com/ga.js' type='text/javascript'%3E%3C/script%3E")); try { var pageTracker = _gat._getTracker("UA-189672-16"); pageTracker._setDomainName(".oxfordjournals.org"); pageTracker._trackPageview(); } catch(err) {}

Journal

GlycobiologyOxford University Press

Published: Jul 1, 1998

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