Abstract
The new protein carrier was developed on the basis of recombinant RNA phage Qβ capsid. C-terminal UGA extension of the short form of Qβ coat, so-called A1 extension, served as a target for presentation of foreign peptides on the outer surface of mosaic Qβ particles. In conditions of enhanced UGA suppression, the proportion of A1-extended to short coats in mosaic particles dropped from 48% to 14%, with an increase of the length of A1 extension. A model insertion, short preS1 epitope 31=DPAFR-35 of hepatitis B surface antigen, demonstrated superficial location on the mosaic Qβ particles and ensured specific antigenicity and immunogenicity.
| Original language | English |
|---|---|
| Pages (from-to) | 7-11 |
| Number of pages | 5 |
| Journal | FEBS Letters |
| Volume | 431 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 10 Jul 1998 |
UN SDGs
This output contributes to the following UN Sustainable Development Goals (SDGs)
-
SDG 3 Good Health and Well-being
Keywords
- A1 extension
- Capsid assembly
- Coat protein UGA suppression
- Hepatitis B virus preS1
- Immunogenicity
- Phage Qβ
Fingerprint
Dive into the research topics of 'Mosaic Qβ coats as a new presentation model'. Together they form a unique fingerprint.Cite this
- APA
- Author
- BIBTEX
- Harvard
- Standard
- RIS
- Vancouver