Article

Expression of the potyvirus coat protein mediated by recombinant vaccinia virus and assembly of potyvirus-like particles in mammalian cells.

CSIRO, Australian Animal Health Laboratory, Geelong, Victoria, Australia.
Archives of Virology (impact factor: 2.11). 02/1998; 143(7):1433-9. pp.1433-9
Source: PubMed

ABSTRACT The coat protein of the potyvirus, Johnsongrass mosaic virus (JGMV), was expressed using a recombinant vaccinia virus (VV) system. Ultra-thin section electron microscopy demonstrated that the coat protein assembled into potyvirus-like particles (PVLPs) in recombinant VV infected cells. Infection of cells with two additional VV recombinants expressing coat protein plus N-terminal and N- and C-terminal extensions also resulted in the formation of PVLPs. These results suggest that the ability of VV to express the potyvirus coat protein at sufficient levels to allow PVLP formation in vitro, could make VV a suitable vector for the delivery of PVLPs displaying vaccine antigens in vivo without the need for particle purification and/or inclusion of adjuvant. Use of such a vaccine strategy would also benefit from the proven advantages of poxviruses as vaccines such as stability in a freeze dried form, resistance to environmental factors and the potential for oral administration.

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    Article: DNA vaccines based on chimeric potyvirus-like particles carrying HPV16 E7 peptide (aa 44-60).
    Dana Pokorna, Noemi Cerovska, Michal Smahel, Tomas Moravec, Viera Ludvikova, Jana Mackova, Helena Synkova, Martina Duskova, Pavel Hozak, Jiri Veleminsky
    [show abstract] [hide abstract]
    ABSTRACT: Vaccine strategies for the treatment of human papillomavirus-induced cervical cancer are based mainly on the human papillomavirus 16 E7 (HPV16 E7) oncoprotein. The immunogenicity of the E7 gene has been enhanced by its fusion to many different genes. Here, we linked a short sequence coding for the E7 peptide (aa 44-60) containing immunodominant epitopes for B and T cells to the 3' end of the gene coding for the whole coat protein (CP) of the poty-virus, potato virus A (PVA), and its deleted form (CPdel) with a short C-terminal deletion of 5 amino acids (LGVKG). CP-E7 and CPdel-E7 fusion proteins, just like CP alone, spontaneously assembled into virus-like particles in both procaryotic and eucaryotic cells. The CP-E7 and CPdel-E7 fusion genes induced slightly stronger E7-specific cytotoxic T-lymphocyte responses than the whole E7 gene, although they were still lower than those elicited by the previously constructed fusion gene, Sig/E7GGG/LAMP-1. The E7- and CP-specific antibody responses were not detected in mice vaccinated with CP-E7 and CPdel-E7 fusion genes. The CP-E7 and CPdel-E7 fusion genes protected mice against the development of tumors induced by TC-1 cells producing the E7 antigen and were also effective in the therapeutic setting, i.e. when the vaccination was performed after tumor cell administration. Their antitumor effect was comparable to those of the whole E7 gene and Sig/E7GGG/LAMP-1 fusion gene. There was no relevant difference between immune responses elicited by CP-E7 and CPdel-E7 DNA vaccination.
    Oncology Reports 11/2005; 14(4):1045-53. · 1.84 Impact Factor
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Keywords

additional VV recombinants
 
C-terminal extensions
 
coat protein
 
Johnsongrass mosaic virus
 
N-terminal
 
oral administration
 
particle purification
 
potyvirus
 
potyvirus coat protein
 
potyvirus-like particles
 
poxviruses
 
proven advantages
 
PVLP formation
 
recombinant vaccinia virus
 
recombinant VV
 
sufficient levels
 
Ultra-thin section electron microscopy
 
vaccine antigens
 
vaccine strategy
 
vaccines
 

J M Hammond