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Human papillomavirus type 16 E7 protein expressed in Escherichia coli and monkey COS-1 Cells: Immunofluorescence detection of the nuclear E7 protein

Sato, Hironori, Watanabe, Sumie, Furuno, Akemi, Yoshiike, Kunito·1989·Virology
DOI 10.1016/0042-6822(89)90386-3
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Abstract

Human papillomavirus type 16 E7 protein, expressed in Escherichia coli as fusion protein lac alpha peptide-E7 (lac-E7), was purified by electrophoresis and used to immunize rabbits to raise antisera. The anti-lac-E7 sera recognized another bacterially expressed fusion protein trpE-E7 by the Western blot method. The antisera were used to identify E7 protein transiently expressed in monkey COS-1 cells from an SV40-derived expression plasmid containing E7 gene. Like the E7 protein from CaSki cells, the majority of 19K E7 protein in the transfected COS-1 cells was found by immunoprecipitation in the soluble cytoplasmic fraction. By immunofluorescence staining, however, the E7 protein was detectable in the nuclei of the transfected COS-1 cells. The results suggest that the E7 protein expressed in monkey cells is nuclear, although it is readily released from nuclei when the cell structure is broken.

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Cited by

Metadata

Authors
Sato, H., Watanabe, S., Furuno, A., & Yoshiike, K.
Venue
Virology
Publisher
Elsevier BV
Published
1989-05
Volume
170
Issue
1
Pages
311-315
ISSN
0042-6822
DOI
10.1016/0042-6822(89)90386-3
Cited by
50
References
0
Language
en
Licence
Funders
  • Ministry of Health, Labour and Welfare
  • Japan Health Sciences Foundation
  • Ministry of Education, Culture, Sports, Science and Technology

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