TY - JOUR
T1 - Determination of the functional difference between human papillomavirus type 6 and 16 E7 proteins by their 30 N-terminal amino acid residues
AU - Takami, Yasunari
AU - Sasagawa, Toshiyuki
AU - Sudiro, Tjahjani Mirawati
AU - Yutsudo, Masuo
AU - Hakura, Akira
N1 - Funding Information:
We thank Dr. H. zur Hausen for providing cloned HPV 16 DNA, and Dr. R. C. Mulligan for permitting use of the pZipNeoSV(X)i vector. This work was supported in part by grants-in-aid for Special Project Research Cancer-Bioscience from the Ministry of Education, Science and Culture and for cancer research (2-1) from the Ministry of Health and Welfare of Japan.
PY - 1992/2
Y1 - 1992/2
N2 - Human papillomavirus type 16 (HPV 16) is often found in cervical carcinomas, while HPV 6 is frequently associated with benign genital lesions. We have compared the abilities of the E7 transforming proteins of HPV 6 and 16 to transform various established and primary rodent cells by using the same heterologous promoter system. HPV 16 E7 efficiently induced anchorage-independent growth of all the rodent cell lines tested and immortalized or cooperated with ras in transforming primary rat cells. On the other hand, the transforming activity of HPV 6 E7 was lower and was restricted. By construction of chimeras of HPV 6 and 16 E7, we found that the difference in transforming activity between the two E7 proteins was mainly determined by the difference in their 30 N-terminal amino acid residues, although some activities seem to be slightly affected by differences in their residual C-terminal portions.
AB - Human papillomavirus type 16 (HPV 16) is often found in cervical carcinomas, while HPV 6 is frequently associated with benign genital lesions. We have compared the abilities of the E7 transforming proteins of HPV 6 and 16 to transform various established and primary rodent cells by using the same heterologous promoter system. HPV 16 E7 efficiently induced anchorage-independent growth of all the rodent cell lines tested and immortalized or cooperated with ras in transforming primary rat cells. On the other hand, the transforming activity of HPV 6 E7 was lower and was restricted. By construction of chimeras of HPV 6 and 16 E7, we found that the difference in transforming activity between the two E7 proteins was mainly determined by the difference in their 30 N-terminal amino acid residues, although some activities seem to be slightly affected by differences in their residual C-terminal portions.
UR - http://www.scopus.com/inward/record.url?scp=0026513553&partnerID=8YFLogxK
U2 - 10.1016/0042-6822(92)90014-G
DO - 10.1016/0042-6822(92)90014-G
M3 - Article
C2 - 1310180
AN - SCOPUS:0026513553
SN - 0042-6822
VL - 186
SP - 489
EP - 495
JO - Virology
JF - Virology
IS - 2
ER -