Abstract
Papillomaviruses induce benign and malignant epithelial tumors in vertebrates through the action of virally encoded oncoproteins such as E6. Recent studies of human and animal E6 proteins determined the three-dimensional structure of E6 when bound to LXXLL peptides derived from E6-targeted cellular proteins. The interaction between diverse E6 proteins and their different cellular targets has revealed a commonality that is surprising and puzzling. E6 proteins that are divergent in evolution have conserved overall structures that bind to similar cellular peptides; these interactions target strikingly different cellular pathways to facilitate analogous viral replication life cycles.
Highlights
Papillomaviruses induce benign and malignant epithelial tumors in vertebrates through the action of virally encoded oncoproteins such as E6
Recent studies have elucidated much that was once unfocused about E6, but the above questions indicate we should look closer still, and put on some better glasses
Summary
Papillomaviruses induce benign and malignant epithelial tumors in vertebrates through the action of virally encoded oncoproteins such as E6. Recent studies of human and animal E6 proteins determined the three-dimensional structure of E6 when bound to LXXLL peptides derived from E6-targeted cellular proteins. The interaction between diverse E6 proteins and their different cellular targets has revealed a commonality that is surprising and puzzling. E6 proteins that are divergent in evolution have conserved overall structures that bind to similar cellular peptides; these interactions target strikingly different cellular pathways to facilitate analogous viral replication life cycles
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