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The human papillomavirus type 6 and 16 E5 proteins are membrane-associated proteins which associate with the 16-kilodalton pore-forming protein

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Conrad, M, Bubb, V J, Schlegel, R·1993·Journal of Virology

Abstract

The human papillomavirus (HPV) E5 proteins are predicted from DNA sequence analysis to be small hydrophobic molecules, and the HPV type 6 (HPV-6) and HPV-11 E5 proteins share several structural similarities with the bovine papillomavirus type 1 (BPV-1) E5 protein. Also similar to the BPV-1 E5 protein, the HPV-6 and HPV-16 E5 proteins exhibit transforming activity when assayed on NIH 3T3 and C127 cells. In this study, we expressed epitope-tagged E5 proteins from both the "low-risk" HPV-6 and the "high-risk" HPV-16 in order to permit their immunologic identification and biochemical characterization. While the HPV-6 and HPV-16 E5 proteins fail to form disulfide-linked dimers and oligomers, they did resemble the BPV-1 E5 protein in their intracellular localization to the Golgi apparatus, endoplasmic reticulum, and nuclear membranes. In addition, the HPV E5 proteins also bound to the 16-kDa pore-forming protein component of the vacuolar ATPase, a known characteristic of the BPV-1 E5 protein. These studies reveal a common intramembrane localization and potential cellular protein target for both the BPV and HPV E5 proteins.

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Metadata

Authors
Conrad, M., Bubb, V. J., & Schlegel, R.
Venue
Journal of Virology
Published
1993-10
Volume
67
Issue
10
Pages
6170-6178
ISSN
  • 0022-538X (ISSN-L)
  • 1098-5514
OpenAlex
W1581360649
Cited by
248
References
0
FWCI
8.14
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: The human papillomavirus type 6 and 16 E5 proteins are membrane-associated proteins which associate with the 16-kilodalton pore-forming protein. https://app.cochat.ai/papers/10.1128/jvi.67.10.6170-6178.1993
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Conrad, M., Bubb, V. J., & Schlegel, R. (1993). The human papillomavirus type 6 and 16 E5 proteins are membrane-associated proteins which associate with the 16-kilodalton pore-forming protein. Journal of Virology. https://doi.org/10.1128/jvi.67.10.6170-6178.1993

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