Journal of Biomolecular Research & Therapeutics

D'Auria F

Publications

• Rapid Communication
  Immunochemical Characterization of the Specific Sequence of URG7 Protein
  Author(s): Ostuni A, Cuviello F, Salvia AM, D'Auria F, Statuto T, Di Nardoc E, Miglionico R, Carrettad V, Musto P and Bisaccia FOstuni A, Cuviello F, Salvia AM, D'Auria F, Statuto T, Di Nardoc E, Miglionico R, Carrettad V, Musto P and Bisaccia F
  
  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 polype.. View More»
  DOI: 10.4172/2167-7956.1000146

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