Hydrophobicity of reactive site loop of SCCA1 affects its binding to HBV.
- Author:
Min CHEN
1
;
Tong CHENG
;
Chen-Yu XU
;
Ting WU
;
Shan-Hai OU
;
Tao ZHANG
;
Jun ZHANG
;
Ning-Shao XIA
Author Information
1. Fujian Research Center of Medical Molecular Virology, The Key Laboratory of Ministry of Education for Cell Biology and Tumor Cell Engineering, Xiamen University, Xiamen 361005, China.
- Publication Type:Journal Article
- MeSH:
Antigens, Neoplasm;
chemistry;
genetics;
metabolism;
Binding Sites;
Biomarkers, Tumor;
chemistry;
genetics;
metabolism;
Carcinoma, Hepatocellular;
immunology;
pathology;
Cell Line, Tumor;
Glutamic Acid;
chemistry;
Hepatitis B virus;
metabolism;
Humans;
Hydrophobic and Hydrophilic Interactions;
Liver Neoplasms;
immunology;
pathology;
Protein Binding;
Receptors, Virus;
metabolism;
Serpins;
chemistry;
genetics;
metabolism;
Valine;
chemistry
- From:
Chinese Journal of Biotechnology
2005;21(1):52-57
- CountryChina
- Language:Chinese
-
Abstract:
Squamous cell carcinoma antigen 1 (SCCA1), a member of the ovalbumin family of serine protease inhibitors, includes several variants. It was reported that expression of two SCCA1 (BP and AJ515706) in cells results in increased binding of HBV to these cells by the interaction of the expressed BP and AJ515706 with HBV pre-S1 domain. In this study, a SCCA1 (A1) was isolated from HepG2, but it appears to lack this ability. A possible role of two mutants, A1-BP and BP-A1, constructed by interchanging the carboxyl terminal of A1 and BP, was investigated. Cells expressing A1-BP rather than BP-A1 showed an increased virus binding capacity. Comparison of A1 sequence with the sequence of BP indicated the presence of only three amino acid changes in the carboxyl terminal, two of them in the reactive site loop (RSL) of SCCA1. Primary structure analysis revealed that the hydrophobicity of BP and AJ515706 in this domain is higher than that of A1. Changing the aa349 of A1 from low hydrophobic glutamic acid to high hydrophobic valine enhanced HBV binding. In contrast, changing the aa349 of BP from valine to glutamic acid reduced HBV binding. Our finding suggests that the hydrophobicity of RSL of SCCA1 may play an important role in HBV binding to cells.
