Presentation of a foreign peptide on the surface of tomato bushy stunt virus
T Joelson, L Akerblom, P Oxelfelt, B Strandberg, K Tomenius and TJ Morris Department of Molecular Biology, Uppsala University, Sweden. thorleif.joelson@bmc.uu.se A 13-amino-acid peptide derived from the V3 loop of human immunodeficiency virus (HIV-1) glycoprotein 120 (gp120) was attached as a C-term...
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Veröffentlicht in: | Journal of general virology 1997-06, Vol.78 (6), p.1213-1217 |
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Sprache: | eng |
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Zusammenfassung: | T Joelson, L Akerblom, P Oxelfelt, B Strandberg, K Tomenius and TJ Morris
Department of Molecular Biology, Uppsala University, Sweden. thorleif.joelson@bmc.uu.se
A 13-amino-acid peptide derived from the V3 loop of human immunodeficiency
virus (HIV-1) glycoprotein 120 (gp120) was attached as a C-terminal gene
fusion to the coat protein of tomato bushy stunt virus (TBSV). The
architecture of this plant virus permitted external display of the foreign
sequence 180 times on the surface of the chimaeric virus particle. The
chimaera replicated to a level similar to wild-type TBSV and the foreign
sequence was retained through six sequential passages in plants. The HIV
epitope was detected on the surface of the virus capsid by a V3-specific
monoclonal antibody and by human sera from HIV-1-positive patients,
demonstrating the potential of using plant-derived chimaeric particles for
diagnostic purposes. Chimaeric virus also induced a specific immune
response to the foreign HIV epitope when injected into NMRI mice. |
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ISSN: | 0022-1317 1465-2099 |
DOI: | 10.1099/0022-1317-78-6-1213 |