Abstract
Hepatitis B surface antigen (HBsAg) is the major component of the envelope of hepatitis B virus (HBV). As a resident membrane protein in the endoplasmic reticulum, it plays a key role in the viral morphogenesis. Little is known about cellular proteins that interact with HBsAg and thereby contributing to HBV morphogenesis. Using the yeast split-ubiquitin system, a number of cellular membrane proteins have been isolated in this study. These include a resident protein of endoplasmic reticulum (thioredoxin-related transmembrane protein 2), an adaptor protein involved in clathrin-mediated endocytosis and HIV-mediated downregulation of CD4, and a co-receptor of coxsakie B virus. The significance of our findings is suggested by the identification of cellular membrane proteins interacting with other virus proteins. Further functional analysis of these HBsAg-interacting cellular membrane proteins should shed new insights on their role in HBV morphogenesis. Copyright
| Original language | English |
|---|---|
| Pages (from-to) | 114-117 |
| Number of pages | 4 |
| Journal | International Journal of Medical Sciences |
| Volume | 2 |
| Issue number | 3 |
| Publication status | Published - Jul 5 2005 |
| Externally published | Yes |
ASJC Scopus Subject Areas
- General Medicine
Keywords
- Cellular membrane proteins
- HBsAg
- Morphogenesis
- Split-ubiquitin Screening System
