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

Full text for this resource is not available from the Research Repository.

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.

Dimensions Badge

Altmetric Badge

Item type Article
URI https://vuir.vu.edu.au/id/eprint/2854
DOI 10.1016/j.jcv.2005.01.007
Official URL http://www.sciencedirect.com/science?_ob=MImg&_ima...
Subjects Historical > 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 18 - View on Scopus
Download/View statistics View download statistics for this item

Search Google Scholar

Repository staff login