Title | Identification of the critical regions in hepatitis B virus preS required for its stability |
Authors | Lian, Min Zhou, Xu Chen, Bin Li, Chan Gu, Xiaocheng Luo, Ming Zheng, Xiaofeng |
Affiliation | Peking Univ, Coll Life Sci, Dept Biochem & Mol Biol, Beijing 100871, Peoples R China. Peking Univ, Nat Lab Protein Engn & Plant Genet Egng, Beijing 100871, Peoples R China. Univ Alabama, Dept Microbiol, Birmingham, AL 35294 USA. |
Keywords | preS critical region stability binding affinity proper folding LARGE SURFACE PROTEIN BINDING PROTEIN INFECTION DOMAIN MYRISTYLATION HEPATOCYTES ATTACHMENT EXPRESSION CLONING SITE |
Issue Date | 2008 |
Publisher | journal of peptide science |
Citation | JOURNAL OF PEPTIDE SCIENCE.2008,14,(3),307-312. |
Abstract | As a hepatitis B virus (HBV) envelope domain, preS plays significant roles in receptor recognition and viral infection. However, the regions critical for maintaining a stable and functional conformation of preS are still unclear and require further investigation. In order to unravel these regions, serially truncated fragments of preS were constructed and expressed in Escherichia coli. Their solubility, stability, secondary structure, and affinity to polyclonal antibodies and hepatocytes were examined. The results showed that amino acids 31-36 were vital for its stable conformation, and the absence of 10-36 amino acids significantly reduced its binding to polyclonal antibodies as well as hepatocytes. The most stable fragment 1-120 (preS1 + N-terminal 12 amino acids of preS2), perhaps the core of preS, was discovered, which bound to HepG2 cells most tightly. Moreover, the availability of large amounts of well-folded and stable preS1-120 enables us to carry out further structural determination and mechanistic study on HBV infection. Copyright (C) 2007 European Peptide Society and John Wiley & Sons, |
URI | http://hdl.handle.net/20.500.11897/162628 |
ISSN | 1075-2617 |
DOI | 10.1002/psc.929 |
Indexed | SCI(E) PubMed |
Appears in Collections: | 生命科学学院 |