Important note: Information in this article was accurate in 1986. The state of the art may have changed since the publication date.
EXPRESSION OF AN HTLV-I VIRAL GENE USING A BPV DERIVED EXPRESSION PLASMID
Diss Abstr Int (Sci); 46(5):1460B 1985. Unique Identifier : AIDSLINE ICDB/86624668 Eiden MV; The George Washington Univ.
Abstract:
Eukaryotic recombinant expression vector systems have facilitated the large scale synthesis of cloned gene products, as well as dramatically enhancing our understanding of gene regulation and polypeptide processing. The expression of cloned genes in eukaryotic cells has been demonstrated for a wide variety of viral replicon vectors. Simian virus 40, adenovirus, herpesvirus, vaccinia, retrovirus, and bovine papilloma viruses have all shown their utility as mammalian expression vectors. Bovine papilloma virus (BPV) is unique among the viral replicon vectors in that it represents the first non-lytic virus based shuttle expression system. The BPV vector replicates as a stable extrachromosomal episome in mouse C127 cells and as a plasmid in bacteria. Transformation of recipient mouse cells provides a selection criterion following gene transfer and the transformed cell lines are usually stable, containing 20-100 copies of BPV-hybrid DNA plasmids. The extrachromosomal recombinant genome is therefore maintained in a homogeneous DNA sequence environment and is easily recovered from low molecular weight DNA preparations. Human T cell leukemia/lymphoma virus, type I (HTLV-I) is a retrovirus etiologically linked with adult T cell leukemia/lymphomas. Only recently has progress been made in identifying the viral envelope proteins of HTLV-I due to difficulties in purifying intact envelope protein from viral particles or HTLV-I infected cells. The features, described above, of the BPV expression vector make this system well suited for expressing HTLV-I envelope gene products in a background devoid of other viral gene products and virally induced cell proteins. The mammalian expression vector, pMBE I, was constructed to facilitate the expression of the carboxyl portion of the small or transmembrane envelope protein in mouse cells and to make monoclonal antibodies against this HTLV-I protein. The pMBE I plasmid was introduced via conventional calcium precipitation-mediated gene transfer into mouse C127 cells. Transformed mouse cells which express the introduced HTLV-I viral gene, were injected into BALB/c mice. Hyperimmune antisera from these mice recognize a protein in the cytoplasm of the pMBE I plasmid-containing mouse cells that is not present in control mouse cells transformed with BPV-I alone, and a protein on the surface of HTLV-I infected human T cells that is not present in autologous uninfected B cells or uninfected T cells. A monoclonal antibody, made against disrupted pMBE I transformed cells, recognizes a 21 kilodalton protein present in HTLV-I virions, indicating that the pMBEI plasmid present in the mouse cells encodes the carboxyl terminal portion of the HTLV-I small envelope protein. (Author abstract)
Keywords: Animal *Gene Expression Regulation *Genes, Viral Human HTLV-BLV Viruses/*GENETICS Mice Mice, Inbred BALB C Papillomavirus, Bovine/*GENETICS *Plasmids Viral Envelope Proteins/GENETICS THESIS
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Important note: Information in this article was accurate in 1986. The state of the art may have changed since the publication date.
