Expression of functional protease and subviral particles by vaccinia virus containing equine infectious anaemia virus gag and 5′ pol genes.
Abstract: Cells infected with vaccinia viruses expressing the equine infectious anaemia virus (EIAV) gag gene (VGag) or gag plus the 5' pol encoding protease (VGag/PR) were evaluated with monoclonal antibody to a p26 capsid protein linear epitope (QEISKFLTD). Both recombinant viruses expressed Gag precursor protein (55K) whereas only VGag/PR expressed a detectable Gag-Pol fusion protein (82K) with a functional protease, shown by subviral particles containing processed p26. Horses inoculated with VGag/PR produced antibodies reactive with EIAV Gag proteins.
Publication Date: 1994-04-01 PubMed ID: 8151302DOI: 10.1099/0022-1317-75-4-895Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
- Research Support
- U.S. Gov't
- P.H.S.
Summary
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This study evaluates the use of vaccinia viruses in the expression of Gag and Gag-Pol proteins related to Equine Infectious Anemia Virus (EIAV) and their subsequent reaction in horses in order to develop an effective immunization strategy against EIAV.
Context and Objective
- The researchers of this paper aim to evaluate and understand how vaccinia viruses expressing the equine infectious anaemia virus (EIAV) Gag gene or the Gag gene plus the 5′ pol encoding protease are processed and interpreted by the host cells.
Methodology
- The researchers infected cells with vaccinia viruses expressing the EIAV Gag gene (VGag) or proteins resulting from the Gag gene plus the 5′ portion of the Pol gene that encodes for protease (VGag/PR).
- These cells were then evaluated using a monoclonal antibody reactive to a p26 capsid protein, replicating a linear sequence (QEISKFLTD).
Results
- Both types of recombinant viruses (VGag and VGag/PR) were found to express a Gag precursor protein, albeit of different sizes: VGag expressed a 55K protein while VGag/PR expressed an 82K Gag-Pol fusion protein.
- Importantly, it was proven that only VGag/PR expressed a detectable Gag-Pol fusion protein (82K) with a functional protease, which was shown by the presence of subviral particles containing processed p26. This is indicative of the proper maturation of viral particles, a critical aspect for effective immunization strategies.
- Further, the researchers illustrate that horses inoculated with VGag/PR recombinant virus successfully produced antibodies reactive with EIAV Gag proteins, showing a positive immune response.
Significance
- The results of this study aid in the development of vaccinia viruses as effective carriers of Gag and Gag-Pol proteins related to EIAV. These carriers can then be used as part of a strategy for EIAV immunization in horses.
- The findings of this study are particularly relevant to the development of live-attenuated vaccines, which employ viruses capable of replication but bereft of disease-causing ability.
- Successful development of such viruses would help in the prevention and control of equine infectious anemia in equine populations globally.
Cite This Article
APA
McGuire TC, O'Rourke KI, Baszler TV, Leib SR, Brassfield AL, Davis WC.
(1994).
Expression of functional protease and subviral particles by vaccinia virus containing equine infectious anaemia virus gag and 5′ pol genes.
J Gen Virol, 75 ( Pt 4), 895-900.
https://doi.org/10.1099/0022-1317-75-4-895 Publication
Researcher Affiliations
- Department of Veterinary Microbiology and Pathology, College of Veterinary Medicine, Washington State University.
MeSH Terms
- Amino Acid Sequence
- Animals
- Antibodies, Monoclonal
- Antibodies, Viral / blood
- Cell Line
- Cloning, Molecular
- Endopeptidases / biosynthesis
- Endopeptidases / genetics
- Endopeptidases / immunology
- Fusion Proteins, gag-pol / biosynthesis
- Fusion Proteins, gag-pol / genetics
- Genes, gag / genetics
- Genes, pol / genetics
- Horses
- Infectious Anemia Virus, Equine / genetics
- Infectious Anemia Virus, Equine / isolation & purification
- Infectious Anemia Virus, Equine / ultrastructure
- Kidney / microbiology
- Molecular Sequence Data
- Molecular Weight
- Protein Processing, Post-Translational / genetics
- Proviruses
- RNA, Viral / isolation & purification
- Recombinant Proteins / genetics
- Sequence Analysis, DNA
- Vaccinia virus / genetics
Grant Funding
- AI24291 / NIAID NIH HHS
Citations
This article has been cited 8 times.- Zhou X, Si J, Corvera J, Gallick GE, Kuang J. Decoding the intrinsic mechanism that prohibits ALIX interaction with ESCRT and viral proteins. Biochem J 2010 Dec 15;432(3):525-34.
- Mealey RH, Leib SR, Littke MH, Wagner B, Horohov DW, McGuire TC. Viral load and clinical disease enhancement associated with a lentivirus cytotoxic T lymphocyte vaccine regimen. Vaccine 2009 Apr 21;27(18):2453-68.
- Mealey RH, Stone DM, Hines MT, Alperin DC, Littke MH, Leib SR, Leach SE, Hines SA. Experimental Rhodococcus equi and equine infectious anemia virus DNA vaccination in adult and neonatal horses: effect of IL-12, dose, and route. Vaccine 2007 Oct 23;25(43):7582-97.
- Fraser DG, Oaks JL, Brown WC, McGuire TC. Identification of broadly recognized, T helper 1 lymphocyte epitopes in an equine lentivirus. Immunology 2002 Mar;105(3):295-305.
- Lonning SM, Zhang W, McGuire TC. Gag protein epitopes recognized by CD4(+) T-helper lymphocytes from equine infectious anemia virus-infected carrier horses. J Virol 1999 May;73(5):4257-65.
- Lonning SM, Zhang W, Leib SR, McGuire TC. Detection and induction of equine infectious anemia virus-specific cytotoxic T-lymphocyte responses by use of recombinant retroviral vectors. J Virol 1999 Apr;73(4):2762-9.
- Zhang W, Lonning SM, McGuire TC. Gag protein epitopes recognized by ELA-A-restricted cytotoxic T lymphocytes from horses with long-term equine infectious anemia virus infection. J Virol 1998 Dec;72(12):9612-20.
- Oaks JL, McGuire TC, Ulibarri C, Crawford TB. Equine infectious anemia virus is found in tissue macrophages during subclinical infection. J Virol 1998 Sep;72(9):7263-9.
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