A phage-displayed cyclic peptide that interacts tightly with the immunodominant region of hepatitis B surface antigen

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Tan, Wen Siang, Tan, Geok Hun, Yusoff, Khatijah and Seow, Heng Fong (2005) A phage-displayed cyclic peptide that interacts tightly with the immunodominant region of hepatitis B surface antigen. Journal of Clinical Virology, 34 (1). pp. 35-41. ISSN 1386-6532

Abstract

The surface antigen (HBsAg) of hepatitis B virus (HBV) is highly conformational and generally evokes protective humoral immune response in human. A disulfide constrained random heptapeptide library displayed on the coat protein III of filamentous bacteriophage M13 was employed to select specific ligands that interact with HBsAg subtype ad. Fusion phages carrying the amino acid sequence ETGAKPH and other related sequences were isolated. The binding site of peptide ETGAKPH was located on the immunodominant region of HBsAg. An equilibrium binding assay in solution showed that the phage binds tightly to HBsAg with a relative dissociation constant () of 2.9 ± 0.9 nM. The phage bearing this peptide has the potential to be used as a diagnostic reagent and two assays for detecting HBsAg in blood samples are described.

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Item type Article
URI https://vuir.vu.edu.au/id/eprint/2854
DOI https://doi.org/10.1016/j.jcv.2005.01.007
Official URL http://www.sciencedirect.com/science?_ob=MImg&_ima...
Subjects Current > FOR Classification > 1108 Medical Microbiology
Historical > Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences
Keywords ResPubID19021. filamentous bacteriophage, biopanning, HBsAg, dissociation constant, immunodominant region
Citations in Scopus 16 - View on Scopus
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