Intercellular trafficking and enhanced in vivo antitumour activity of a non-virally delivered P27-VP22 fusion protein

Gene Therapy

Volumn 10, Issue 4, 2003, Pages 314-325

  Zavaglia, D ^a   Favrot, M C ^a   Eymin, B ^a   Tenaud, C ^a   Coll, J L ^a  

^a INSTITUT ALBERT BONNIOT   (France)

Author keywords

Intercellular trafficking; Protein delivery; VP22

Indexed keywords

CYCLIN DEPENDENT KINASE 2; CYCLINE; GENE PRODUCT; HYBRID PROTEIN; NAKED DNA; PROTEIN P27; STRUCTURAL PROTEIN;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ANTINEOPLASTIC ACTIVITY; CANCER THERAPY; CELL GROWTH; CELL PROLIFERATION; CELL TRANSPORT; CLONOGENESIS; CONTROLLED STUDY; ENZYME INHIBITION; FEMALE; GENE TARGETING; GENE THERAPY; GENETIC TRANSFECTION; GROWTH INHIBITION; HERPES SIMPLEX VIRUS 1; HUMAN; HUMAN CELL; IN VIVO STUDY; NONHUMAN; NONVIRAL GENE THERAPY; NUDE MOUSE; PLASMID; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN TRANSPORT; REVIEW;

ANIMALS; ANTIGENS, CD11B; CASPASE 3; CASPASES; CELL CYCLE PROTEINS; COS CELLS; CYCLIN-DEPENDENT KINASE INHIBITOR P27; FEMALE; GENE THERAPY; HELA CELLS; HUMANS; IMMEDIATE-EARLY PROTEINS; MICE; MICE, NUDE; NEOPLASMS, EXPERIMENTAL; RECOMBINANT FUSION PROTEINS; TRANSFECTION; TUMOR SUPPRESSOR PROTEINS; VIRAL PROTEINS;

ANIMALIA; HUMAN HERPESVIRUS 1; MUS MUSCULUS; SIMPLEXVIRUS;

EID: 0037295437     PISSN: 09697128     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.gt.3301904     Document Type: Review

References (29)

1. Elliott G, Mouzakitis G, O'Hare P. VP16 interacts via its activation domain with VP22, a tegument proten of herpes simplex virus, and is relocated to a novel macromolecular assembly in coexpressing cells. J Virol 1995; 69: 7932-7941.
2. Sciortino MT et al. Of the three tegument proteins that package mRNA in herpes simplex virions, one (VP22) transports the mRNA to uninfected cells for expression prior to viral infection. Proc Natl Acad Sci USA 2002; 99: 8318-8323.
3. Elliott G, O'Hare P. Intercellular trafficking and protein delivery by a herpesvirus structural protein. Cell 1997; 88: 223-233.
4. Aints A, Dilber MS, Smith CI. Intercellular spread of GFP-VP22. J Gene Med 1999; 1: 275-279.
5. Brewis N et al. Evaluation of VP22 spread in tissue culture. J Virol 2000; 74: 1051-1056.
6. Elliott G, O'Hare P. Intercellular trafficking of VP22-GFP fusion proteins. Gene Ther 1999; 6: 149-151.
7. Wybranietz WA et al. Quantification of VP22-GFP spread by direct fluorescence in 15 commonly used cell lines. J Gene Med 1999; 1: 265-274.
8. Phelan A, Elliott G, O'Hare P. Intercellular delivery of functional p53 by the herpesvirus protein VP22. Nat Biotechnol 1998; 16: 440-443.
9. Wills KN et al. Intratumoural spread and increased efficacy of a p53-VP22 fusion protein expressed by a recombinant adenovirus. J Virol 2001; 75: 8733-8741.
10. Dilber MS et al. Intercellular delivery of thymidine kinase prodrug activating enzyme by the herpes simplex virus protein, VP22. Gene Ther 1999; 6: 12-21.
11. Liu CS et al. VP22 enhanced intercellular trafficking of HSV thymidine kinase reduced the level of ganciclovir needed to cause suicide cell death. J Gene Med 2001; 3: 145-152.
12. Wybranietz WA et al. Enhanced suicide gene effect by adenoviral transduction of a VP22-cytosine deaminase (CD) fusion gene. Gene Ther 2001; 8: 1654-1664.
13. Bennett RP, Dalby B. Protein delivery using VP22. Nat Biotechnol 2002; 20: 20.
14. Derer W, Easwaran HP, Leonhardt H, Cardoso MC. A novel approach to induce cell cycle reentry in terminally differentiated muscle cells. FASEB J 2002; 16: 132-133.
15. Oliveira SC, Harms JS, Afonso RR, Splitter GA. A genetic immunization adjuvant system based on BVP22-antigen fusion. Hum Gene Ther 2001; 12: 1353-1359.
16. Hung CF et al. Improving vaccine potency through intercellular spreading and enhanced MHC class I presentation of antigen. J Immunol 2001; 166: 5733-5740.
17. Fang B, Xu B, Koch P, Roth JA. Intercellular trafficking of VP22-GFP fusion proteins is not observed in cultured mammalian cells. Gene Ther 1998; 5: 1420-1424.
18. Lundberg M, Johansson M. Is VP22 nuclear homing an artifact?. Nat Biotechnol 2001; 19: 713-714.
19. Sgambato A, Cittadini A, Faraglia B, Weinstein IB. Multiple functions of p27(Kip1) and its alterations in tumour cells: a review. J Cell Physiol 2000; 183: 18-27.
20. Philipp-Staheli J, Payne SR, Kemp CJ. p27(Kip1): regulation and function of a haploinsufficient tumour suppressor and its misregulation in cancer. Exp Cell Res 2001; 264: 148-168.
21. Porter PL et al. Expression of cell-cycle regulators p27Kip1 and cyclin E, alone and in combination, correlate with survival in young breast cancer patients. Nat Med 1997; 3: 222-225.
22. Chen J, Willingham T, Shuford M, Nisen PD. Tumour suppression and inhibition of aneuploid cell accumulation in human brain tumour cells by ectopic overexpression of the cyclin-dependent kinase inhibitor p27KIP1. J Clin Invest 1996; 97: 1983-1988.
23. Craig C et al. A recombinant adenovirus expressing p27Kip1 induces cell cycle arrest and loss of cyclin-Cdk activity in human breast cancer cells. Oncogene 1997; 14: 2283-2289.
24. Naruse I et al. Over-expression of p27kip1 induces growth arrest and apoptosis mediated by changes of pRb expression in lung cancer cell lines. Int J Cancer 2000; 88: 377-383.
25. Pomeranz LE, Blaho JA. Modified VP22 localizes to the cell nucleus during synchronized herpes simplex virus type 1 infection. J Virol 1999; 73: 6769-6781.
26. Harms JS, Ren X, Oliveira SC, Splitter GA. Distinctions between bovine herpesvirus 1 and herpes simplex virus type 1 VP22 tegument protein subcellular associations. J Virol 2000; 74: 3301-3312.
27. Aints A et al. Mapping of herpes simplex virus-1 VP22 functional domains for inter- and subcellular protein targeting. Gene Ther 2001; 8: 1051-1056.
28. Koelle DM, Frank JM, Johnson ML, Kwok WW. Recognition of herpes simplex virus type 2 tegument proteins by CD4 T cells infiltrating human genital herpes lesions. J Virol 1998; 72: 7476-7483.
29. Koelle DM et al. CD4 T-cell responses to herpes simplex virus type 2 major capsid protein VP5: comparison with responses to tegument and envelope glycoproteins. J Virol 2000; 74: 11422-11425.