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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 references41

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          Molecular understanding and design of zwitterionic materials.

          Zwitterionic materials have moieties possessing cationic and anionic groups. This molecular structure leads to unique properties that can be the solutions of various application problems. A typical example is that zwitterionic carboxybetaine (CB) and sulfobetaine (SB) materials resist nonspecific protein adsorption in complex media. Considering the vast number of cationic and anionic groups in the current chemical inventory, there are many possible structural variations of zwitterionic materials. The diversified structures provide the possibility to achieve many desired properties and urge a better understanding of zwitterionic materials to provide design principles. Molecular simulations and modeling are a versatile tool to understand the structure-property relationships of materials at the molecular level. This progress report summarizes recent simulation and modeling studies addressing two fundamental questions regarding zwitterionic materials and their applications as biomaterials. First, what are the differences between zwitterionic and nonionic materials? Second, what are the differences among zwitterionic materials? This report also demonstrates a molecular design of new protein-resistant zwitterionic moieties beyond conventional CB and SB based on design principles developed from these simulation studies.
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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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              The sweet spot: defining virus-sialic acid interactions.

              Viral infections are initiated by attachment of the virus to host cell surface receptors, including sialic acid-containing glycans. It is now possible to rapidly identify specific glycan receptors using glycan array screening, to define atomic-level structures of virus-glycan complexes and to alter the glycan-binding site to determine the function of glycan engagement in viral disease. This Review highlights general principles of virus-glycan interactions and provides specific examples of sialic acid binding by viruses with stalk-like attachment proteins, including influenza virus, reovirus, adenovirus and rotavirus. Understanding virus-glycan interactions is essential to combating viral infections and designing improved viral vectors for therapeutic applications.
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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
                5590fae3-8bf8-488a-a899-7dc737d09a02
                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.

                History
                : 13 March 2015
                : 22 May 2015
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                la5b00944
                la-2015-009446

                Physical chemistry
                Physical chemistry

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