title: Identification of aptamer-binding sites in hepatitis C virus envelope glycoprotein e2.
abstract: Hepatitis C Virus (HCV) encodes two envelope glycoproteins, E1 and E2. Our previous work selected a specific aptamer ZE2, which could bind to E2 with high affinity, with a great potential for developing new molecular probes as an early diagnostic reagents or therapeutic drugs targeting HCV. In this study, the binding sites between E2 and aptamer ZE2 were further explored. E2 was truncated to 15 peptides (P1 to P15) and these peptides were used to detect the affinity with ZE2 by ELISA respectively. The peptide with high affinity was then further truncated, detected and compared with six kinds of HCV genotypes. The basic amino acid in 500 aa bound to ZE2 with high affinity, while acidic amino acid in 501 aa reduced the reaction between E2 and ZE2. The results showed the 500 aa and 501 aa of E2 were the key sites that bound to ZE2.
authors: Department of Biochemistry and Molecular Biology, Life Sciences School of Hubei University, Wuhan, China;
authors: Fan
authors: F
authors: Chen
authors: Evolution and Ecology Research Centre, School of Biological, Earth and Environmental Sciences, The University of New South Wales, Sydney, Australia;
authors: Si-Chong
authors: SC
authors: Chen
authors: Clinical laboratory, Wuhan Tuberculosis Dispensary, Wuhan Health Bureau, Wuhan, China;
authors: Jing
authors: J
authors: Zhou
authors: Department of Biochemistry and Molecular Biology, Life Sciences School of Hubei University, Wuhan, China;
authors: Zhi-De
authors: ZD
authors: Chen
authors: Department of Biochemistry and Molecular Biology, School of Basic Medical Science, Wuhan University, Wuhan, China.
authors: Fang
authors: F
authors: Chen
keywords: Aptamer; Binding site; Glycoprotein E2; Hepatitis C virus
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