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Nilsson C. L. (Ed.) Else_AT-NILSSON_prelims.qxd 6/8/2007 06:29 PM Page i Lectins Analytical Technologies This page intentionally left blank Else_AT-NILSSON_prelims.qxd 6/8/2007 06:29 PM Page iii Lectins Analytical Technologies Edited by Carol L. Nilsson National High Magnetic Field Laboratory Florida State University Tallahassee, FL, USA Amsterdam – Boston – Heidelberg – London – New York – Oxford – Paris San Diego – San Francisco – Singapore – Sydney – Tokyo Else_AT-NILSSON_prelims.qxd 6/8/2007 06:29 PM Page iv Elsevier Radarweg 29, PO Box 211, 1000 AE Amsterdam, The Netherlands Linacre House, Jordan Hill, Oxford OX2 8DP, UK First edition 2007 Copyright © 2007 Elsevier B.V. All rights reserved No part of this publication may be reproduced, stored in a retrieval system or transmitted in any form or by any means electronic, mechanical, photocopying, recording or otherwise without the prior written permission of the publisher Permissions may be sought directly from Elsevier’s Science & Technology Rights Department in Oxford, UK: phone (+44) (0) 1865 843830; fax (+44) (0) 1865 853333; email: [email protected]. Alternatively you can submit your request online by visiting the Elsevier web site at http://www.elsevier.com/locate/permissions, and selecting Obtaining permission to use Elsevier material Notice No responsibility is assumed by the publisher for any injury and/or damage to persons or property as a matter of products liability, negligence or otherwise, or from any use or operation of any methods, products, instructions or ideas contained in the material herein. Because of rapid advances in the medical sciences, in particular, independent verification of diagnoses and drug dosages should be made Library of Congress Cataloging-in-Publication Data A catalog record for this book is available from the Library of Congress British Library Cataloguing in Publication Data A catalogue record for this book is available from the British Library ISBN: 978-0-444-53077-6 For information on all Elsevier publications visit our website at books.elsevier.com Printed and bound in The Netherlands 070809101110987654321 Else_AT-NILSSON_contents.qxd 6/12/2007 16:40 Page v Table of Contents Preface . vii List of Contributors . ix Chapter 1 Lectins: Analytical Tools from Nature . 1 Carol L. Nilsson Chapter 2 Crystallography and Lectin Structure Database . 15 Ute Krengel and Anne Imberty Chapter 3 NMR Investigations of Lectin–Carbohydrate Interactions . 51 Patrick Groves, Angeles Canales, M. Isabel Chávez, MaAgorzata Palczewska, Dolores Díaz, F. Javier Cañada and Jesús Jiménez-Barbero Chapter 4 Applications of Isothermal Titration Calorimetry to Lectin–Carbohydrate Interactions . 75 Tarun K. Dam and C. Fred Brewer Chapter 5 Bioanalytical Studies Based on Lectin–Carbohydrate Interactions Measured by Ellipsometry and Surface Plasmon Resonance Techniques . 103 Jana Masárová, Fredrik Winquist and Bengt Danielsson Chapter 6 Use of Natural and Synthetic Oligosaccharide, Neoglycolipid and Glycolipid Libraries in Defining Lectins from Pathogens . 129 Krista Weikkolainen, Jari Helin, Ritva Niemelä, Halina Miller-Podraza and Jari Natunen Chapter 7 Carbohydrate Microarrays for Lectin Characterization and Glyco-Epitope Identification . 167 Denong Wang and Albert M. Wu Else_AT-NILSSON_contents.qxd 6/12/2007 16:40 Page vi vi Table of Contents Chapter 8 Glycoproteomics Based on Lectin Affinity Chromatographic Selection of Glycoforms . 193 Fred E. Regnier, Kwanyoung Jung, Stephen B. Hooser and Christina R. Wilson Chapter 9 Miniaturized Lectin Affinity Chromatography . 213 Xiuli Mao, Jianhua Qin and Bingcheng Lin Chapter 10 Frontal Affinity Chromatography: Systematization for Quantitative Interaction Analysis Between Lectins and Glycans . 239 Sachiko Nakamura-Tsuruta, Noboru Uchiyama, Junko Kominami and Jun Hirabayashi Chapter 11 Technical Aspects of Glycoprotein Enrichment . 267 Yehia Mechref, Milan Madera and Milos V. Novotny Chapter 12 Proteomic Techniques for Functional Identification of Bacterial Adhesins . 299 Elisabet Carlsohn and Carol L. Nilsson Chapter 13 The Use of Lectins in Bioaffinity MALDI Probes . 327 Crystal Kirmiz, Caroline S. Chu and Carlito B. Lebrilla Chapter 14 Electrospray Ionization Fourier Transform Ion Cyclotron Resonance Mass Spectrometry for Lectin Analysis . 343 Julie T. Adamson and Kristina Håkansson Chapter 15 Catalytically Inactive Endoglycosidases as Microbial Diagnostic Reagents: Chitinases and Lysozymes as Fungal and Bacterial Capture/Label Agents . 373 Roger A. Laine, Jennifer W.-C. Lo and Betty C.-R. Zhu Chapter 16 Generation of Lectins from Enzymes: Use of Inactive Endosialidase for Polysialic Acid Detection . 385 Anne Jokilammi, Miikka Korja, Elina Jakobsson and Jukka Finne Chapter 17 Probing Cell Surface Lectins with Neoglycoconjugates . 397 Eugenia M. Rapoport, Elena I. Kovalenko, Ivan M. Belyanchikov and Nicolai V. Bovin Appendix 1 Table of Lectin Affinities . 417 Carol L. Nilsson Appendix 2 List of Abbreviations . 427 Carol L. Nilsson Subject Index . 435 Else_AT-NILSSON_preface.qxd 5/31/2007 05:51 PM Page vii Preface The intention with the production of this volume is to provide a toolbox of new and classical techniques for lectin and lectin–carbohydrate characterization. New lectins are still being discovered and new ways to exploit the specificity of lectin binding properties are being developed. The number of recent publications in which lectins are either described or used as biochemical tools points to a large and diverse group of scientific activities. Between January 1, 2004 and January 1, 2007, nearly 6,000 research articles that contained the search term “lectin” were posted in the PubMed database (http://www.ncbi.nlm.nih.gov/entrez/query.fcgi). During this short period, new analytical techniques have appeared and existing ones have been refined to meet the demands of higher sensitivity and expanding applica- tions. It is expected that the number of citations will continue to rise along with the pace of future developments. Because lectins are translators of the sugar code, they appear in important biological settings and can be extremely useful analytical tools in organism-wide studies (i.e. proteomics and glycomics). The trend towards miniaturized assays is also very strong. From structural characterization of lectins to technical aspects of glycoprotein enrichment, this volume offers an in-depth guide to essential modern methodologies. A handbook for the study of lectin structure and protein–carbohydrate energetics, use of lectins as analytical tools, and even the design of new lectins from other proteins is offered. It is designed with both the novice and advanced researcher in mind, who work in fields such as biology (including glycobiology), biomedicine, and analytical biology and analytical chemistry. Because the study of lectins and their employment in analytical settings is quite diverse, a large number of techniques are presented by experts in the field. The beginning chapters offer up-to-date descriptions of classical techniques employed in lectinology, including X-ray crystallography, NMR spectroscopy, microcalorimetry, and surface plasmon resonance. The following chapters present a wide variety of useful methods, including the use of carbohydrate microarrays, lectin affinity chromatography, proteomic identification of adhesins, development of bioaffinity mass spectrometry probes, and frontal affinity chromatography, to name a few. Many of the chapters include practical, hands-on tips for the experimentalist. The introductory chapter includes references to web-based lectin resources, which have the advantage of changing quickly with the pace of new developments, unlike the printed word. Descriptions of many analytically useful lectins are provided in one appendix. Lastly, because abbreviations have become commonplace in most specialty areas, the reader is provided with an explanatory list at the end of the book for easy reference. Else_AT-NILSSON_preface.qxd 5/31/2007 05:51 PM Page viii viii Preface In conclusion, the future of lectin science appears extremely bright. The chapters that follow have been written by fellow enthusiasts in the field and provide invaluable information through their expertise. Without my co-authors’ time and dedication, this book could not have been produced; therefore, I offer each contributor my sincere gratitude for joining me in this project. Carol L. Nilsson National High Magnetic Field Laboratory, Florida State University, 1800 E. Paul Dirac Dr., Tallahassee, FL 32310, USA Else_AT-NILSSON_loc.qxd 6/12/2007 6:21 PM Page ix List of Contributors Julie T. Adamson Department of Chemistry, University of Michigan, 930 North University Avenue, Ann Arbor, MI 48109-1055, USA Ivan M. Belyanchikov Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry RAS, 117997, ul. Miklukho-Maklaya 16/10, Moscow, Russia Nicolai V. Bovin Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry RAS, 117997, ul. Miklukho-Maklaya 16/10, Moscow, Russia C. Fred Brewer Department of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, New York 10461, USA F. Javier Cañada Department of Protein Science, Centro Investigaciones Biológicas – CSIC, Ramiro de Maeztu 9, 28040 Madrid, Spain Angeles Canales Department of Protein Science, Centro Investigaciones Biológicas – CSIC, Ramiro de Maeztu 9, 28040 Madrid, Spain Elisabet Carlsohn Proteomics Core Facility at Göteborg University, Box 435, SE 405 30 Göteborg, Sweden National High Magnetic Field Laboratory, Florida State University, 1800 E. Paul
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