Cleavage of human immunodeficiency virus type 1 proteinase from the N- terminally adjacent p6* protein is essential for efficient Gag polyprotein processing and vital infectivity

Journal of Virology

Volumn 72, Issue 4, 1998, Pages 3459-3463

  Tessmer, Uwe ^a   Kräusslich, Hans Georg ^a  

^a LEIBNIZ INSTITUTE FOR EXPERIMENTAL VIROLOGY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN; PROTEIN PRECURSOR; PROTEINASE;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CERCOPITHECIDAE; HUMAN; HUMAN CELL; HUMAN IMMUNODEFICIENCY VIRUS 1; IMMUNOFLUORESCENCE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; SYNCYTIUM; VIRION; VIRUS INFECTIVITY; VIRUS REPLICATION;

EID: 2642680072     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.72.4.3459-3463.1998     Document Type: Article

References (30)

1. Adachi, A., H. E. Gendelman, S. Koenig, T. Folks, R. Willey, A. Rabson, and M. A. Martin. 1986. Production of acquired immunodeficiency syndrome-associated retrovirus in human and nonhuman cells transfected with an infectious molecular clone. J. Virol. 59:284-291.
2. pol-protease fusion protein is present in mature particles of human immunodeficiency virus type 1. J. Virol. 70:7228-7232.
3. 1H-NMR spectra and structural characterization in solution of the HIV-1 transframe protein p6*. Eur. J. Biochem. 237:383-392.
4. Chen, C., and H. Okayama. 1987. High-efficiency transformation of mammalian cells by plasmid DNA. Mol. Cell. Biol. 7:2745-2752.
5. Co, E., G. Koelsch, Y. Lin, E. Ido, J. A. Hartsuck, and J. Tang. 1994. Proteolytic processing mechanisms of a miniprecursor of the aspartic proteinase of human immunodeficiency virus type 1. Biochemistry 33:1248-1254.
6. Davies, D. R. 1990. The structure and function of the aspartic proteinases. Annu. Rev. Biochem. Biophys. Chem. 19:189-215.
7. Harada, S., Y. Koyagani, and N. Yamamoto. 1985. Infection of HTLV-III/ LAV in HTLV-I carrying cells MT-2 and MT-4 and application in a plaque assay. Science 229:563-566.
8. Konvalinka, J., A. M. Heuser, O. Hruskova-Heidingsfeldova, V. M. Vogt, J. Sedlacek, P. Strop, and H.-G. Kräusslich. 1995. Proteolytic processing of particle associated retroviral proteins by homologous and heterologous viral proteinases. Eur. J. Biochem. 228:191-198.
9. Konvalinka, J., M. A. Litterst, R. Welker, H. Kottler, F. Rippmann, A.-M. Heuser, and H.-G. Kräusslich. 1995. HIV-1 proteinase (PR) active-site mutation causes reduced PR activity and PR-mediated cytotoxicity without apparent effect on virus maturation and infectivity. J. Virol. 69:7180-7186.
10. Kotler, M., G. Arad, and S. H. Hughes. 1992. Human immunodeficiency virus type 1 gag-protease fusion proteins are enzymatically active. J. Virol. 66:6781-6783.
11. Kräusslich, H.-G., H. Schneider, G. Zybarth, C. A. Carter, and E. Wimmer. 1988. Processing of in vitro-synthesized gag precursor proteins of human immunodeficiency virus (HIV) type 1 by HIV proteinase generated in Escherichia coli. J. Virol. 62:4393-4397.
12. Kunkel, T. A. 1985. Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA 82:488-492.
13. Leis, J., D. Baltimore, J. M. Bishop, J. Coffin, E. Fleissner, S. P. Goff, S. Oroszlan, H. Robinson, A. M. Skalka, H. M. Temin, and V. M. Vogt. 1988. Standardized and simplified nomenclature for proteins common for all retroviruses. J. Virol. 62:1808-1809.
14. Levy, J. A., A. D. Hoffman, S. M. Kramer, J. A. Landis, J. M. Shimabukuro, and L. S. Oshiro. 1984. Isolation of lymphocytopathic retroviruses from San Francisco patients with AIDS. Science 225:840-842.
15. Louis, J. M., N. T. Nashed, K. D. Parris, A. R. Kimmel, and D. M. Jerina. 1994. Kinetics and mechanism of autoprocessing of human immunodeficiency virus tvpe 1 protease from an analog of the Gag-Pol polyprotein. Proc. Natl. Acad Sci. USA 91:7970-7974.
16. Mergener, K., M. Fäcke, R. Welker, V. Brinkmann, H. R. Gelderblom, and H.-G. Kräusslich. 1992. Analysis of HIV particle formation using transient expression of subviral constructs in mammalian cells. Virology 186:25-39.
17. Nermut, M. V., and D. J. Hockley. 1996. Comparative morphology and structural classification of retroviruses. Curr. Top. Microbiol. Immunol. 214: 1-24.
18. Partin, K., G. Zybarth, L. Ehrlich, M. DeCrombrugghe, E. Wimmer, and C. Carter. 1991. Deletion of sequences upstream of the proteinase improves the proteolytic processing of human immunodeficiency vius type 1. Proc. Natl. Acad. Sci. USA 88:4776-4780.
19. Pettit, S. C., J. Simsic, D. D. Loeb, L. Everitt, C. A. Hutchison III, and R. Swanstrom. 1991. Analysis of retroviral protease cleavage sites reveals two types of cleavage sites and the structural requirements of the P1 amino acid. J. Biol. Chem. 266:14539-14547.
20. Phylip, L. H., J. S. Mills, B. F. Parten, B. M. Dunn, and J. Kay. 1992. Intrinsic activity of precursor forms of HIV-1 proteinase. FEBS Lett. 314: 449-454.
21. Poorman, R. A., A. G. Tomasselli, R. L. Heinrikson, and F. J. Kézky. 1991. A cumulative specificity model for proteases from human immunodeficiency virus types 1 and 2, inferred from statistical analysis of extended substrate database. J. Biol. Chem. 266:14554-14561.
22. Popovic, M., M. G. Sarngadharan, E. Read, and R. C. Gallo. 1984. Detection, isolation, and continuous production of cytopathic retroviruses (HTLV-III) from patients with AIDS and pre-AIDS. Science 224:497-500.
23. Ratner, L., A. Fisher, L. L. Jagodzinski, H. Mitsuya, R.-S. Liou, R. C. Gallo, and F. Wong-Staal. 1987. Complete nucleotide sequence of functional clones of the AIDS virus. AIDS Res. Hum. Retroviruses 3:57-69.
24. Salahuddin, S. Z., P. D. Markhan, F. Wong-Staal, G. Franchini, V. S. Kalyanaraman, and R. C. Gallo. 1983. Restricted expression of human T-cell leukemia-lymphoma virus (HTLV) in transformed human umbilical cord blood lymphocytes. Virology 129:51-64.
25. Schäger, H., and G. von Jagow. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:368-379.
26. Schechter, I., and A. Berger. 1967. On the size of the active sites in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27:157-162.
27. Schulz, T. F., D. Whitby, J. G. Hoad, T. Corrah, H. Whittle, and R. A. Weiss. 1990. Biological and molecular variability of human immunodeficiency virus type 2 isolates from The Gambia. J. Virol. 64:5177-5182.
28. Vogt, V. M. 1996. Proteolytic processing and particle maturation. Curr. Top. Microbiol. Immunol. 214:95-132.
29. Wlodawer, A., M. Miller, M. Jaskolski, B. K. Sathyanarayna, E. Baldwin, I. T. Weber, L. Selk, L. Clawson, J. Schneider, and S. B. H. Kent. 1989. Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 proteinase. Science 245:616-621.
30. Zybarth, G., H.-G. Kräusslich, K. Partin, and C. Carter. 1994. Proteolytic activity of novel human immunodeficiency virus type 1 proteinase proteins from a precursor with a blocking mutation at the N terminus of the PR domain. J. Virol. 68:240-250.