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      Carboxybetaine Modified Interface for Electrochemical Glycoprofiling of Antibodies Isolated from Human Serum

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          Abstract

          Impedimetric lectin biosensors capable of recognizing two different carbohydrates (galactose and sialic acid) in glycans attached to antibodies isolated from human serum were prepared. The first step entailed the modification of a gold surface by a self-assembled monolayer (SAM) deposited from a solution containing a carboxybetaine-terminated thiol applied to the subsequent covalent immobilization of lectins and to resist nonspecific protein adsorption. In the next step, Sambucus nigra agglutinin (SNA) or Ricinus communis agglutinin (RCA) was covalently attached to the SAM, and the whole process of building a bioreceptive layer was optimized and characterized using a diverse range of techniques including electrochemical impedance spectroscopy, cyclic voltammetry, quartz crystal microbalance, contact angle measurements, zeta-potential assays, X-ray photoelectron spectroscopy, and atomic force microscopy. In addition, the application of the SNA-based lectin biosensor in the glycoprofiling of antibodies isolated from the human sera of healthy individuals and of patients suffering from rheumatoid arthritis (RA) was successfully validated using an SNA-based lectin microarray. The results showed that the SNA lectin, in particular, is capable of discriminating between the antibodies isolated from healthy individuals and those from RA patients based on changes in the amount of sialic acid present in the antibodies. In addition, the results obtained by the application of RCA and SNA biosensors indicate that the abundance of galactose and sialic acid in antibodies isolated from healthy individuals is age-related.

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          Most cited references 41

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          Recognition determinants of broadly neutralizing human antibodies against dengue viruses.

          Dengue disease is caused by four different flavivirus serotypes, which infect 390 million people yearly with 25% symptomatic cases and for which no licensed vaccine is available. Recent phase III vaccine trials showed partial protection, and in particular no protection for dengue virus serotype 2 (refs 3, 4). Structural studies so far have characterized only epitopes recognized by serotype-specific human antibodies. We recently isolated human antibodies potently neutralizing all four dengue virus serotypes. Here we describe the X-ray structures of four of these broadly neutralizing antibodies in complex with the envelope glycoprotein E from dengue virus serotype 2, revealing that the recognition determinants are at a serotype-invariant site at the E-dimer interface, including the exposed main chain of the E fusion loop and the two conserved glycan chains. This 'E-dimer-dependent epitope' is also the binding site for the viral glycoprotein prM during virus maturation in the secretory pathway of the infected cell, explaining its conservation across serotypes and highlighting an Achilles' heel of the virus with respect to antibody neutralization. These findings will be instrumental for devising novel immunogens to protect simultaneously against all four serotypes of dengue virus.
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            Emerging principles for the therapeutic exploitation of glycosylation.

            Glycosylation plays a key role in a wide range of biological processes. Specific modification to a glycan's structure can directly modulate its biological function. Glycans are not only essential to glycoprotein folding, cellular homeostasis, and immune regulation but are involved in multiple disease conditions. An increased molecular and structural understanding of the mechanistic role that glycans play in these pathological processes has driven the development of therapeutics and illuminated novel targets for drug design. This knowledge has enabled the treatment of metabolic disorders and the development of antivirals and shaped cancer and viral vaccine strategies. Furthermore, an understanding of glycosylation has led to the development of specific drug glycoforms, for example, monoclonal antibodies, with enhanced potency.
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              Glycomimetics versus multivalent glycoconjugates for the design of high affinity lectin ligands.

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                Author and article information

                Journal
                Langmuir
                Langmuir
                la
                langd5
                Langmuir
                American Chemical Society
                0743-7463
                1520-5827
                05 June 2015
                30 June 2015
                : 31
                : 25
                : 7148-7157
                Affiliations
                []Department of Glycobiotechnology, Institute of Chemistry, Slovak Academy of Sciences , Dubravska cesta 9, Bratislava, 845 38, Slovak Republic
                []Centre for Advanced Materials, Qatar University , Doha 2713, Qatar
                [§ ]Department of Physical Chemistry, Faculty of Natural Sciences, Comenius University , Mlynska Dolina, Bratislava, 842 15, Slovak Republic
                []International Laser Centre , Ilkovičova 3, Bratislava 841 04, Slovak Republic
                []Laboratory of Human Endocrinology, Institute of Experimental Endocrinology, Slovak Academy of Sciences , Vlarska 3, Bratislava, 833 06, Slovak Republic
                [# ]National Institute of Rheumatic Diseases , Nábrežie I. Krasku 4, 921 12 Piešt’any, Slovak Republic
                []Department of Sensors and Detectors, Institute of Electrical Engineering, Slovak Academy of Sciences , Dubravska cesta 9, Bratislava, 841 04, Slovak Republic
                Author notes
                [* ]Tel.: +421 2 5941 0263. E-mail: jan.tkac@ 123456savba.sk .
                Article
                10.1021/acs.langmuir.5b00944
                4489201
                26048139
                Copyright © 2015 American Chemical Society

                This is an open access article published under a Creative Commons Attribution (CC-BY) License, which permits unrestricted use, distribution and reproduction in any medium, provided the author and source are cited.

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                la5b00944
                la-2015-009446

                Physical chemistry

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