Development of HBsAg-binding aptamers that bind HepG2.2.15 cells via HBV surface antigen

Virol Sin. 2010 Feb;25(1):27-35. doi: 10.1007/s12250-010-3091-7. Epub 2010 Feb 12.

Abstract

Hepatitis B virus surface antigen (HBsAg), a specific antigen on the membrane of Hepatitis B virus (HBV)-infected cells, provides a perfect target for therapeutic drugs. The development of reagents with high affinity and specificity to the HBsAg is of great significance to the early-stage diagnosis and treatment of HBV infection. Herein, we report the selection of RNA aptamers that can specifically bind to HBsAg protein and HBsAg-positive hepatocytes. One high affinity aptamer, HBs-A22, was isolated from an initial 115 mer library of ~1.1 x 10¹⁵ random-sequence RNA molecules using the SELEX procedure. The selected aptamer HBs-A22 bound specifically to hepatoma cell line HepG2.2.15 that expresses HBsAg but did not bind to HBsAg-devoid HepG2 cells. This is the first reported RNA aptamer which could bind to a HBV specific antigen. This newly isolated aptamer could be modified to deliver imaging, diagnostic, and therapeutic agents targeted at HBV-infected cells.

Publication types

  • Evaluation Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aptamers, Nucleotide / isolation & purification
  • Aptamers, Nucleotide / metabolism*
  • Cell Line
  • Hepatitis B / diagnosis*
  • Hepatitis B Surface Antigens / analysis*
  • Hepatocytes / chemistry*
  • Hepatocytes / virology*
  • Humans
  • Protein Binding
  • SELEX Aptamer Technique
  • Sensitivity and Specificity

Substances

  • Aptamers, Nucleotide
  • Hepatitis B Surface Antigens