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Papillomavirus polypeptides E6 and E7 are zinc-binding proteins

Barbosa, M S, Lowy, D R, Schiller, J T·1989·Journal of Virology
DOI 10.1128/jvi.63.3.1404-1407.1989
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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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Cited by

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
DOI
10.1128/jvi.63.3.1404-1407.1989
Cited by
184
References
0
Language
en
Licence
journals.asm.org/non-commercial-tdm-license (tdm)

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