Intercellular trafficking of VP22-GFP fusion proteins is not observed in cultured mammalian cells

Gene Therapy

Volumn 5, Issue 10, 1998, Pages 1420-1424

  Fang, B ^a   Xu, B ^a   Koch, P ^a   Roth, J A ^a  

^a UNIVERSITY OF TEXAS MD ANDERSON CANCER CENTER   (United States)

Author keywords

GFP fusion proteins; HSV; Protein trafficking; VP22

Indexed keywords

GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; VIRUS PROTEIN;

ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL COMMUNICATION; CELL CULTURE; CELL NUCLEUS; CONTROLLED STUDY; HERPES SIMPLEX VIRUS 1; HUMAN; HUMAN CELL; MAMMAL CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN LOCALIZATION;

EID: 0031786954     PISSN: 09697128     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.gt.3300741     Document Type: Article

References (21)

1. Elliott CD, Meredith DM. The herpes simplex virus type 1 tegument protein VP22 is encoded by gene UL49. J Gen Virol 1992; 73: 723-726.
2. Gibson W, Roizman B. Proteins specified by herpes simplex virus. Staining and radiolabeling properties of B capsid and virion proteins in polyacrylamide gels. J Virol 1974; 13: 155-165.
3. Knopf KW, Kaerner HC. Virus-specific basic phosphoproteins associated with herpes simplex virus type a (HSV-1) particles and the chromatin of HSV-1-infected cells. J Gen Virol 1980; 46: 405-414.
4. Pinard MF, Simard R, Bibor-Hardy V. DNA-binding proteins of herpes simplex virus type 1-infected BHK cell nuclear matrices. J Gen Virol 1987; 68: 727-735.
5. Leslie J, Rixon FJ, Mclauchlan J. Overexpression of the herpes simplex virus type 1 tegument protein VP22 increases its incorporation into virus particles. Virology 1996; 220: 60-68.
6. Elliott G, O'Hare P. Intercellular trafficking and protein delivery by a herpesvirus structural protein. Cell 1997; 88: 223-233.
7. Chalfie M et al. Green fluorescent protein as a marker for gene expression. Science 1994; 263: 802-805.
8. Sly WS, Fischer HD. The phosphomannosyl recognition system for intracellular and intercellular transport of lysosomal enzymes (review). J Cell Biochem 1982; 18: 67-85.
9. Mignatti P, Morimoto T, Rifkin DB. Basic fibroblast growth factor released by single, isolated cells stimulates their migration in an autocrine manner. Proc Natl Acad Sci USA 1991, 88: 11007-11011.
10. Rubartelli A, Cozzolino F, Talio M, Sitia R. A novel secretory pathway for interleukin-1 β, a protein lacking a signal sequence. EMBO J 1990; 9: 1503-1510.
11. Meyer DI, Krause E, Dobberstein B. Secretory protein translocation across membranes - the role of the 'docking protein'. Nature 1982; 297: 647-650.
12. Tajima S, Lauffer L, Rath VL, Walter P. The signal recognition particle receptor is a complex that contains two distinct polypeptide chains. J Cell Biol 1986; 103: 1167-1178.
13. Jungnickel B, Rapoport TA, Hartmann E. Protein translocation: common themes from bacteria to man (review). FEES Lett 1994; 346: 73-77.
14. Nichols BJ et al. Homotypic vacuolar fusion mediated by t- and v-SNAREs. Nature 1997; 387: 199-202.
15. Wacker I et al. Microtubule-dependent transport of secretory vesicles visualized in real time with a GFP-tagged secretory protein. J Cell Sci 1997; 110: 1453-1463.
16. Stenmark H et al. Peptides fused to the amino-terminal end of diphtheria toxin are translocated to the cytosol. J Cell Biol 1991; 113: 1025-1032.
17. Perez F et al. Antennapedia homeobox as a signal for the cellular internalization and nuclear addressing of a small exogenous peptide. J Cell Sci 1992; 102: 717-722.
18. Dingwall C, Laskey RA. Nuclear targeting sequences - a consensus? Trends Biochem Sci 1991; 16: 478-481.
19. Graham FL, Van Der Eb AJ. A new technique for the assay of infectivity of human adenovirus 5 DNA. Virology 1973; 52: 456-467.
20. MacGregor GR, Mogg AE, Burke JF, Caskey CT. Histochemical staining of clonal mammalian cell lines expressing E. coli β-galactosidase indicates heterogeneous expression of the bacterial gene. Somat Cell Mol Genet 1987; 13: 253-265.
21. Ropp JD et al. Aequorea green fluorescent protein analysis by flow cytometry. Cytometry 1995; 21: 309-317.