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© Michel Huerre
Coupe histologique de foie de patient atteint d'une hépatite C chronique active avec infiltrat (opacité) folliculaire (lymphocytes) (Grossissement X 400). L'hépatite C chronique peut être à l'origine de cirrhose et cancer du foie
Publication : Angewandte Chemie (International ed. in English)

Targeting the Two Oncogenic Functional Sites of the HPV E6 Oncoprotein with a High-Affinity Bivalent Ligand

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Angewandte Chemie (International ed. in English) - 27 May 2015

Ramirez J, Poirson J, Foltz C, Chebaro Y, Schrapp M, Meyer A, Bonetta A, Forster A, Jacob Y, Masson M, Deryckère F, Travé G

Link to Pubmed [PMID] – 26014966

Angew. Chem. Int. Ed. Engl. 2015 Jun;54(27):7958-62

Capture d’écran 2015-09-03 à 12.33.39The E6 oncoproteins of high-risk mucosal (hrm) human papillomaviruses (HPVs) contain a pocket that captures LxxLL motifs and a C-terminal motif that recruits PDZ domains, with both functions being crucial for HPV-induced oncogenesis. A chimeric protein was built by fusing a PDZ domain and an LxxLL motif, both known to bind E6. NMR spectroscopy, calorimetry and a mammalian protein complementation assay converged to show that the resulting PDZ-LxxLL chimera is a bivalent nanomolar ligand of E6, while its separated PDZ and LxxLL components are only micromolar binders. The chimera binds to all of the hrm-HPV E6 proteins tested but not to low-risk mucosal or cutaneous HPV E6. Adenovirus-mediated expression of the chimera specifically induces the death of HPV-positive cells, concomitant with increased levels of the tumour suppressor P53, its transcriptional target p21, and the apoptosis marker cleaved caspase 3. The bifunctional PDZ-LxxLL chimera opens new perspectives for the diagnosis and treatment of HPV-induced cancers.

http://www.ncbi.nlm.nih.gov/pubmed/26014966