FUNCTIONAL OLIGOMERIZATION OF PURIFIED HUMAN PAPILLOMAVIRUS TYPE-16 AND TYPE-6B E7 PROTEINS EXPRESSED IN ESCHERICHIA-COLI

Authors
CHINAMI M SASAKI S HACHIYA N YUGE K OHSUGI T MAEDA H SHINGU M
Citation
M. Chinami et al., FUNCTIONAL OLIGOMERIZATION OF PURIFIED HUMAN PAPILLOMAVIRUS TYPE-16 AND TYPE-6B E7 PROTEINS EXPRESSED IN ESCHERICHIA-COLI, Journal of General Virology, 75, 1994, pp. 277-281
Citations number
26
Categorie Soggetti
Virology
Journal title
Journal of General Virology → ACNP
ISSN journal
00221317
Volume
75
Year of publication
1994
Part
2
Pages
277 - 281
Database
ISI
SICI code
0022-1317(1994)75:<277:FOOPHP>2.0.ZU;2-M
Abstract
Purified non-fused soluble human papillomavirus type 16 and 6b E7 prot eins expressed in Escherichia coli were found to form oligomers. For b oth proteins, several degrees of oligomerization were demonstrated by gel filtration, dynamic laser light scattering and scanning electron m icroscopy. Oligomerization was dependent on the concentration of E7 pr otein. Oligomerized E7 proteins were able to bind the retinoblastoma g ene product pRB and stimulated DNA synthesis when introduced into cell s.