alexa In situ Monitoring of In vitro Sialylation by Inclusion Bodies
ISSN: 2153-0637

Journal of Glycomics & Lipidomics
Open Access

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Research Article

In situ Monitoring of In vitro Sialylation by Inclusion Bodies

Klaudia Talafová1,2 and Jozef Nahálka1,2*

1Institute of Chemistry, Centre for Glycomics, Slovak Academy of Sciences, Dúbravská cesta 9, SK-84538 Bratislava, Slovak Republic

2Institute of Chemistry, Centre of excellence for white-green biotechnology, Slovak Academy of Sciences, Trieda Andreja Hlinku 2, SK-94976 Nitra, Slovak Republic

*Corresponding Author:
Jozef Nahálka
Institute of Chemistry, Centre for Glycomics,
Slovak Academy of Sciences, Dúbravská cesta 9
SK-84538 Bratislava, Slovak Republic
E-mail: [email protected]

Received Date: August 02, 2012; Accepted Date: September 11, 2012; Published Date: September 14, 2012

Citation: Talafová K, Nahálka J (2012) In situ Monitoring of in vitro Sialylation by Inclusion Bodies. J Glycomics Lipidomics 2:105. doi: 10.4172/2153-0637.1000105

Copyright: © 2012 Talafová K, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.



Sialic acids usually terminate oligosaccharide chains expressed on the cell surfaces and glycoproteins of vertebrates, higher invertebrates and some microorganisms. They have various important biological roles. Two of these roles, determination of anti-inflammatory activity of IgG antibodies and increasing the circulating half-life of glycoproteins and blood cells, can find application in pharmaceutical industry and medicine. For this reason, there is a need for efficient in vitro protein sialylation processes. To evaluate the efficiency of in vitro sialylation, a method for in situ monitoring in high throughput screens has been developed. It is represented by hemagglutination caused by inclusion bodies of SabA lectin. SabA lectins are proteins expressed on the cell surface of bacteria Helicobacter pylori and bind to sialic acids on the host cell surfaces. They are responsible for H. pylori mediated agglutination of erythrocytes in vitro. This presented method is fast, simple and one can avoid time-consuming purification of analyzed glycoprotein. In addition, it could provide a basic diagnostic method for determination of sialylation level of erythrocytes.

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