- Abstract:
-
The hepatitis C virus glycoproteins E1 and 2 have been expressed using recombinant baculoviruses following fusion to the carrier protein glutathione S-transferase (GST). Proteins were expressed singly and as an E1E2 polyprotein with and without an N-terminal affinity tag. Expression of the E1E2 polyprotein, even when preceded by GST, led to processing in insect cells and detection of an E1E2 complex that could be specifically purified by glutathione affinity chromatography. Baculovirus expres...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Publisher copy:
- 10.1006/viro.2000.0407
-
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- Publisher:
- Elsevier Publisher's website
- Journal:
- Virology Journal website
- Volume:
- 273
- Issue:
- 1
- Pages:
- 60-66
- Publication date:
- 2000-01-01
- DOI:
- EISSN:
-
1096-0341
- ISSN:
-
0042-6822
- URN:
-
uuid:88b8023a-a6b7-4de3-b1e1-b54b48c4fd4e
- Source identifiers:
-
99943
- Local pid:
- pubs:99943
- Copyright holder:
- Academic Press
- Copyright date:
- 2000
- Notes:
- The full text of this article is available open access on the publisher's website at http://dx.doi.org/10.1006/viro.2000.0407
Journal article
Hepatitis C virus glycoprotein E2 binding to CD81: the role of E1E2 cleavage and protein glycosylation in bioactivity.
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