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Papillomavirus polypeptides E6 and E7 are zinc-binding proteins
Abstract
Papillomavirus proteins E6 and E7 have Cys-X-X-Cys repeats which have been suggested to mediate zinc binding. We have developed a modification of an assay that detects zinc binding to proteins immobilized on filters. Using well-characterized metalloproteins, we show that, under reducing conditions, this assay distinguishes proteins that coordinate zinc through cysteine residues from those that bind the metal through other amino acids. Under these conditions, E6 and E7 polypeptides of human papillomavirus type 18 and bovine papillomavirus type 1 exhibited high-affinity zinc binding. Our results suggest that E6 and E7 are metalloproteins and may coordinate the metal ions through cysteine residues.
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“The HPV E6 proteins are approximately 150 amino acids in length and are zinc-binding proteins with four CXXC motifs [31,32]”
From The Not-So-Good, the Bad and the Ugly: HPV E5, E6 and E7 Oncoproteins in the Orchestration of Carcinogenesis (2021) · cites this paper as [31]
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“in the C-terminus, the CR3 region contains two CXXC zinc-binding motifs separated by 29 amino acids [31,62]”
From The Not-So-Good, the Bad and the Ugly: HPV E5, E6 and E7 Oncoproteins in the Orchestration of Carcinogenesis (2021) · cites this paper as [31]
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Cited by
Basukala, O., & Banks, L. (2021) · Viruses · doi:10.3390/v13101892 · Cited by 137
Metadata
- Authors
- Barbosa, M. S., Lowy, D. R., & Schiller, J. T.
- Affiliations
- Laboratory of Cellular Oncology, National Cancer Institute, Bethesda, Maryland 20892.
- Venue
- Journal of Virology
- Publisher
- American Society for Microbiology
- Published
- 1989-03
- Volume
- 63
- Issue
- 3
- Pages
- 1404-1407
- ISSN
- 0022-538X
- 1098-5514
- Cited by
- 184
- References
- 0
- Language
- en
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- Barbosa, M. S., Lowy, D. R., & Schiller, J. T. (1989). Papillomavirus polypeptides E6 and E7 are zinc-binding proteins. Journal of Virology. https://doi.org/10.1128/jvi.63.3.1404-1407.1989