alexa Immunochemical Characterization of the Specific Sequence of URG7 Protein | OMICS International | Abstract
ISSN: 2167-7956

Journal of Biomolecular Research & Therapeutics
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Immunochemical Characterization of the Specific Sequence of URG7 Protein

Ostuni A1*, Cuviello F1, Salvia AM1, D'Auria F2, Statuto T2, Di Nardoc E3, Miglionico R1, Carrettad V4, Musto P2 and Bisaccia F1

1Department of Sciences, University of Basilicata, 85100 Potenza, Italy

2Laboratory of Clinical Research and Advanced Diagnostics, IRCCS-CROB, 85028 Rionero in Vulture, Italy

3Department of Mathematics, Computer Science and Economics, University of Basilicata, 85100 Potenza, Italy

4Hospital of Venosa, Unit of Medicine, 85029 Venosa, Italy

Corresponding Author:
Ostuni A
Department of Sciences
University of Basilicata
85100 Potenza, Italy
Tel: +39-0971205453
Fax: +39-0971205678
E-mail: [email protected]

Received Date: August 11, 2016; Accepted Date: September 02, 2016; Published Date: September 10, 2016

Citation: Ostuni A, Cuviello F, Salvia AM, D'Auria F, Statuto T, et al. (2016) Immunochemical Characterization of the Specific Sequence of URG7 Protein. J Biomol Res Ther 5:146. doi:10.4172/2167-7956.1000146

Copyright: © 2016 Ostuni A, 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.


URG7 is an anti-apoptotic protein which consists of 99 amino acid residues up regulated by antigen x during the HBV infection. The first 74 amino acids are identical to those of the multidrug resistance protein 6 (MRP6), while the amino acid residues from 75 to 99 are specific for URG7 protein. Immuno-informatics tools and secondary structure analysis were carried out to identify the antigenic properties of this URG7 sequence. The 75-99 peptide was synthesized by the solid-phase method, structurally characterized by CD spectroscopy and conjugated to a protein carrier. New Zealand white rabbits were immunized and sera were tested for anti-peptide specific antibodies by ELISA and western blot analysis. Finally ELISA test with human sera was performed.

Rabbits immunized with the 75-99 peptide produce antibodies that recognize both the 75-99 peptide and the URG7 recombinant polypeptide. Moreover, both antigens allowed for the detection of the anti-URG7 antibodies in sera of healthy and HBV infected subjects although with a different discriminant threshold. Our data suggested that peptide ELISA assay against the specific sequence of the URG7 protein allows with good sensitivity and specificity for the detection of anti-URG7 antibodies in sera from HBV infected patients.


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