A phage-displayed cyclic peptide that interacts tightly with the immunodominant region of hepatitis B surface antigen.
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 (KDrel) 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.
Tan
Wen Siang
WS
Department of Microbiology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400 UPM Serdang, Selangor, Malaysia. wstan@fsas.upm.edu.my
Tan
Geok Hun
GH
Yusoff
Khatijah
K
Seow
Heng Fong
HF
D000595:Amino Acid Sequence; D001435:Bacteriophages / Q000235:genetics; D001665:Binding Sites; D004797:Enzyme-Linked Immunosorbent Assay; D006514:Hepatitis B Surface Antigens / Q000097:blood / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D019151:Peptide Library; D010456:Peptides, Cyclic / Q000737:chemistry / Q000378:metabolism*
D006514:Hepatitis B Surface Antigens; D019151:Peptide Library; D010456:Peptides, Cyclic