HIV-1 proprotein processing as a target for gene therapy

Gene Therapy

Volumn 10, Issue 6, 2003, Pages 467-477

  Cordelier, P ^a   Zern, M A ^b   Strayer, D S ^a  

^a THOMAS JEFFERSON UNIVERSITY   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

; Antitrypsin; gp160; p55Gag; SV40

Indexed keywords

ALPHA 1 ANTITRYPSIN; ANTIGEN P24; ASPARTIC PROTEINASE; ASPARTIC PROTEINASE INHIBITOR; GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 160; PROTEIN P55; PROTEINASE; SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR; VIRUS PROTEIN;

ANIMAL CELL; CELL LINE; CONTROLLED STUDY; CYTOPATHOGENIC EFFECT; DOSE RESPONSE; DRUG DESIGN; GENETIC TRANSDUCTION; HUMAN; HUMAN CELL; HUMAN IMMUNODEFICIENCY VIRUS 1; HUMAN IMMUNODEFICIENCY VIRUS INFECTION; IMMUNOHISTOCHEMISTRY; IMMUNOPRECIPITATION; NONHUMAN; NORTHERN BLOTTING; PERIPHERAL LYMPHOCYTE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN PROCESSING; PROVOCATION TEST; REVIEW; SIMIAN VIRUS 40; VIRAL GENE DELIVERY SYSTEM; VIRAL GENE THERAPY; VIRION; VIRUS PARTICLE; VIRUS RECOMBINANT; VIRUS REPLICATION; WESTERN BLOTTING;

ALPHA 1-ANTITRYPSIN; ANIMALS; CELLS, CULTURED; COS CELLS; GENE PRODUCTS, GAG; GENE THERAPY; GENETIC VECTORS; HIV ENVELOPE PROTEIN GP160; HIV INFECTIONS; HUMANS; LYMPHOCYTES; PROTEIN PRECURSORS; SERINE PROTEINASE INHIBITORS; SIMIAN VIRUS 40; TRANSDUCTION, GENETIC; VIRUS REPLICATION;

ANIMALIA; HUMAN IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS 1; RNA VIRUSES; SIMIAE; SIMIAN VIRUS; SIMIAN VIRUS 40;

EID: 0344642957     PISSN: 09697128     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.gt.3301891     Document Type: Review

References (49)

1. Trono D, Feinberg MB, Baltimore D. HIV-1 Gag mutants can dominantly interfere with the replication of the wild-type virus. Cell 1989; 59: 113-120.
2. Aguilar-Cordova E et al. Inhibition of HIV-1 by a double transdominant fusion gene. Gene Ther 1995; 2: 181-186.
3. Malim MH, Cullen BR. HIV-1 structural gene expression requires the binding of multiple Rev monomers to the viral RRE: implications for HIV-1 latency. Cell 1991;65: 241-248.
4. Pearson L et al. A transdominant tat mutant that inhibits tat-induced gene expression from the human immunodeficiency virus long terminal repeat. Proc Natl Acad Sci USA 1991; 87: 5079-5083.
5. Babe LM, Rose J, Craik CS. Trans-dominant inhibitory human immunodeficiency virus type 1 protease monomers prevent protease activation and virion maturation. Proc Natl Acad Sci USA 1990; 92: 10 069-10 073.
6. Lee TC et al. Overexpression of RRE-derived sequences inhibits HIV-1 replication in CEM cells. New Biol 1992; 4: 66-74.
7. Sullenger BA et al. Overexpression of TAR sequences renders cells resistant to human immunodeficiency virus replication. Cell 1990; 63: 601-608.
8. Sczakiel G, Pawlita M. Inhibition of human immunodeficiency virus type 1 replication in human T cells stably expressing antisense RNA. J Virol 1991; 65: 468-472.
9. Duan L et al. Potent inhibition of human immunodeficiency virus type 1 replication by an intracellular anti-Rev single-chain antibody. Proc Natl Acad Sci USA 1994; 91: 5075-5079.
10. Marasco WA, Haseltine WA, Chen SY. Design, intracellular expression, and activity of a human anti-human immunodeficiency virus type 1 gp120 single-chain antibody. Proc Natl Acad Sci USA 1993; 90: 7889-7893.
11. Mhashilkar AM et al. Inhibition of human immunodeficiency virus type 1 replication in vitro in acutely and persistently infected human CD4+ mononuclear cells expressing murine and humanized anti-human immunodeficiency virus type 1 Tat single-chain variable fragment intrabodies. Hum Gene Ther 1999; 10: 1453-1467.
12. Sarver N et al. Ribozymes as potential anti-HIV-1 therapeutic agents. Science 1990; 247: 1222-1225.
13. Ojwang JO et al. Inhibition of human immunodeficiency virus type 1 expression by a hairpin ribozyme. Proc Natl Acad Sci USA 1992; 89: 10 802-10 806.
14. San Jose E, Munoz-Fernandez MA, Alarcon B. Retroviral vector-mediated expression in primary human T cells of an endoplasmic reticulum-retained CD4 chimera inhibits human immunodeficiency virus type-1 replication. Hum Gene Ther 1998; 9: 1345-1357.
15. Allan JS et al. Major glycoprotein antigens that induce antibodies in AIDS patients are encoded by HTLV-III. Science 1985; 228: 1091-1094.
16. McCune JM et al. Endoproteolytic cleavage of gp160 is required for the activation of human immunodeficiency virus. Cell 1988; 53: 55-67.
17. Kowalski M et al. Functional regions of the envelope glycoprotein of human immunodeficiency virus type 1. Science 1987; 237: 1351-1355.
18. Hallenberger S et al. The role of eukaryotic subtilisin-like endoproteases for the activation of human immunodeficiency virus glycoproteins in natural host cells. J Virol 1997; 71: 1036-1045.
19. Hallenberger S et al. Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160. Nature 1992; 360: 358-361.
20. Moulard M, Decroly E. Maturation of HIV envelope glycoprotein precursors by cellular endoproteases. Biochim Biophys Acta 2000; 1469: 121-132.
21. Kohl NE et al. Active human immunodeficiency virus protease is required for viral infectivity. Proc Natl Acad Sci USA 1988; 85: 4686-4690.
22. Gottlinger HG, Sodroski JG, Haseltine WA. Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1. Proc Natl Acad Sci USA 1989; 86: 5781-5785.
23. Travis J, Salvesen GS. Human plasma proteinase inhibitors. Annu Rev Biochem 1983; 52: 655-709.
24. Strayer DS. SV40 as an effective gene transfer vector in vivo. J Biol Chem 1996; 271: 24 741-24 746.
25. Strayer DS et al. Use of SV40-based vectors to transduce foreign genes to normal human peripheral blood mononuclear cells. Gene Ther 1997; 4: 219-225.
26. Strayer DS, Milano J. SV40 mediates stable gene transfer in vivo. Gene Ther 1996; 3: 581-587.
27. Strayer DS. Gene therapy using SV40-derived vectors: what does the future hold? J Cell Physiol 1999; 181: 375-384.
28. BouHamdan M et al. Inhibition of HIV-1 by an anti-integrase single-chain variable fragment (SFv): delivery by SV40 provides durable protection against HIV-1 and does not require selection. Gene Ther 1999; 6: 660-666.
29. Beatty K, Bieth J, Travis J. Kinetics of association of serine proteinases with native and oxidized alpha-1-proteinase inhibitor and alpha-1-antichymotrypsin. J Biol Chem 1980; 255: 3931-3934.
30. Matheson NR, van Halbeek H, Travis J. Evidence for a tetrahedral intermediate complex during serpin- proteinase interactions. J Biol Chem 1991; 266: 13 489-13 491.
31. Dalgleish AG et al. The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus. Nature 1984; 312: 763-767.
32. Franzusoff A et al. Biochemical and genetic definition of the cellular protease required for HIV-1 gp160 processing. J Biol Chem 1995; 270: 3154-3159.
33. Anderson ED et al. Inhibition of HIV-1 gp160-dependent membrane fusion by a furin-directed alpha 1-antitrypsin variant. J Biol Chem 1993; 268: 24 887-24 891.
34. Jean F et al. alpha1-antitrypsin Portland, a bioengineered serpin highly selective for furin: application as an antipathogenic agent. Proc Natl Acad Sci USA 1998; 95: 7293-7298.
35. Bahbouhi B et al. Effect of alpha-1 antitrypsin portland variant (alpha1-PDX) on HIV-1 replication. Biochem J 2000; 352: 91-98.
36. Shapiro L, Pott GB, Ralston AH. Alpha-1-antitrypsirin inhibits human immunodeficiency virus type 1. FASEB J 2001; 15: 115-122.
37. Guo HG et al. Characterization of an HIV-1 point mutant blocked in envelope glycoprotein cleavage. Virology 1990; 174: 217-224.
38. Moulard M et al. Processing and routage of HIV glycoproteins by furin to the cell surface. Virus Res 1999; 60: 55-65.
39. Decroly E et al. The convertases furin and PC1 can both cleave the human immunodeficiency virus (HIV)-1 envelope glycoprotein gp160 into gp120 (HIV-1 SU) and gp41 (HIV-I TM). J Biol Chem 1994; 269: 12240-12247.
40. Ho DD et al. Rapid turnover of plasma virions and CD4 lymphocytes in HIV-1 infection. Nature 1995; 373: 123-126.
41. Gulnik SV et al. Kinetic characterization and cross-resistance patterns of HIV-1 protease mutants selected under drug pressure. Biochemistry 1995; 34: 9282-9287.
42. Condra JH et al. In vivo emergence of HIV-1 variants resistant to multiple protease inhibitors. Nature 1995; 374: 569-571.
43. Scharpe S et al. alpha-1-Anti-trypsin, an inhibitor of renin. Biochem J 1976; 153: 505-507.
44. Jayan GC et al. SV40-derived vectors provide effective transgene expression and inhibition of HIV-1 using, constitutive, conditional and pol III promoters. Gene Ther 2001; 8: 1033-1042.
45. Zern MA et al. A novel SV40-based vector successfully transduces and expresses an alpha 1-antitrypsin ribozyme in a human hepatoma-derived cell line. Gene Ther 1999; 6: 114-120.
46. Kondo R, Feitelson MA, Strayer DS. Use of SV40 to immunize against hepatitis B surface antigen: implications for the use of SV40 for gene transduction and its use as an immunizing agent. Gene Ther 1998; 5: 575-582.
47. Sauter BV et al. A replication-deficient rSV40 mediates liver-directed gene transfer and a long-term amelioration of jaundice in gunn rats. Gastroenterology 2000; 119: 1348-1357.
48. Strayer DS et al. Titering replication-defective virus for use in gene transfer. Biotechniques 1997; 22: 447-450.
49. Johnson V, Byington R. Quantitative Assays for Virus Infectivity. Basic Virologic Tech 1988; 71-76.