Cloning, Expression and Kinetic Characterization of the Feline Immunodeficiency Virus Proteinase
Biological and biochemical characterizations of non-human AIDS model systems are essential for understanding the mechanism of retrovirus-induced immune deficiency diseases. Furthermore, animal-based AIDS model systems will be important for the complete testing and evaluation of drugs and vaccines directed against diseases with retroviral etiologies. The feline immunodeficiency virus (FIV) is a member of the lentivirus family, a group of retroviruses that also includes the human immunodeficiency viruses, HIV-1 and HIV-2. As with human lentiviruses, FIV exhibits a T-lymphocyte tropism and is associated with an immunodeficiency syndrome in infected domestic cats (Pederson et al., 1987, Yamamoto et al., 1988, Pederson et al., 1989). The merit of a feline-based system for evaluating AIDS chemotherapies will be partially dependent upon the structural and functional homology between feline and human viral proteins. A variety of HIV specific proteins have been identified as potential targets for anti-viral compounds, with much attention focused on the HIV-specific proteinase (HIV PR). At the primary structural level the human and feline viral proteinases share 29% amino acid identity and approximately 48 % amino acid similarity, with the highest degree of homology associated with residues involved in the formation of the active site cleft. In order to evaluate the degree of functional homology between the human and feline proteinases we have cloned and expressed the FTV PR gene in E. coli.
KeywordsFeline Immunodeficiency Virus Functional Homology Kinetic Characterization Active Site Cleft Feline Immunodeficiency Virus Infection
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- Phylip, L. H., Richards, A. D., Kay, J., Konvalinka, J., Strop, P., Blaha, I., Velek, J., Kostka, V., Ritchie, A. J., Broadhurst, A. V., Farmerie, W. G., Scarborough, P. E. & Dunn, B. M., 1990, Hydrolysis of synthetic chromogenic substrates by HIV-1 and HIV-2 proteinases, Biochem. Biophys. Res. Comm. 171: 439–444.PubMedCrossRefGoogle Scholar