scholarly journals A novel BK virus-based episomal vector for expression of foreign genes in mammalian cells

1991 ◽  
Vol 19 (8) ◽  
pp. 1925-1931 ◽  
Author(s):  
Arrigo De Benedetti ◽  
Robert E. Rhoads
1991 ◽  
Vol 19 (16) ◽  
pp. 4485-4490 ◽  
Author(s):  
Randal J. Kaufman ◽  
Monique V. Davies ◽  
Louise C. Wasley ◽  
Donna Michnick

2003 ◽  
pp. 461-474
Author(s):  
Simon J. Forster ◽  
Francis J. Carr ◽  
William J. Harris ◽  
Anita A. Hamilton

2019 ◽  
Vol 30 (22) ◽  
pp. 2761-2770
Author(s):  
Xiao-Yin Wang ◽  
Xi Zhang ◽  
Tian-Yun Wang ◽  
Yan-Long Jia ◽  
Dan-Hua Xu ◽  
...  

Matrix attachment regions (MARs) can mediate the replication of vector episomes in mammalian cells; however, the molecular mode of action remains unclear. Here, we assessed the characteristics of MARs and the mechanism that mediates episomal vector replication in mammalian cells. Five shortened subfragments of β-interferon MAR fragments were cloned and transferred into CHO cells, and transgene expression levels, presence of the gene, and the episomal maintenance mechanism were determined. Three shortened MAR derivatives (position 781–1320, 1201–1740, and 1621–2201) retained full MAR activity and mediated episomal vector replication. Moreover, the three shortened MARs showed higher transgene expression levels, greater efficiency in colony formation, and more persistent transgene expression compared with those of the original pEPI-1 plasmid, and three functional truncated MARs can bind to SAF-A MAR-binding protein. These results suggest that shortened MARs are sufficient for replication and maintenance of episomes in CHO cells.


1994 ◽  
Vol 1 (3) ◽  
pp. 251-263
Author(s):  
Simon J. Forster ◽  
Francis J. Carr ◽  
William J. Harris ◽  
Anita A. Hamilton

Gene ◽  
1988 ◽  
Vol 71 (1) ◽  
pp. 19-27 ◽  
Author(s):  
Ikeda Hitoshi ◽  
Trowsdale John ◽  
Saito Izumu

1999 ◽  
Vol 46 (2) ◽  
pp. 325-339 ◽  
Author(s):  
K Bieńkowska-Szewczyk ◽  
B Szewczyk

The outermost layers of animal viruses are usually composed of glycoproteins. They are responsible not only for the entrance of viruses into, and release from host cells but also for the initial interaction of a viral particle with immunological defense of the host. It is therefore not surprising that many laboratories devote a lot of effort to study viral glycoproteins at the molecular level. Very often such studies are possible only after the introduction of a glycoprotein gene into a heterologous system. Expression of glycoprotein genes is usually obtained in mammalian or insect cells. Expression in mammalian cells yields viral glycoproteins with glycan chains indistinguishable from the original counterparts in virion particles but the level of synthesis of glycoproteins is very low. Vaccinia virus is the most common vector for expression in mammalian cells. It is easy to grow, the introduction of foreign genes is relatively simple and, due to the size of the vaccinia genome, it can accept large pieces of foreign DNA. Glycosylation in insect cells is not as complex as in mammalian cells and usually glycoproteins produced in insect cells are of slightly lower molecular mass than those produced in mammalian cells. The most common vector for expression of glycoproteins in insect cells is a baculovirus, Autographa californica nuclear polyhedrosis virus (AcNPV). The great advantage of this system is a very high level of expression of foreign genes.


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