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Mutations in the E6AP binding site of E6 prevent both E6AP degradation and oncogenesis, but a selective mutation is not available. Moreover, the E6 AP binding site is mutated in the majority of cervical carcinomas. Our studies have shown that HPV16 E6 is an intrinsically unstable protein that is stabilized by E6AP, and that both full-length and truncated E6 proteins are functional for transformation. We have further shown that both full-length and truncated E6 proteins are expressed in cervical carcinomas and express a functional E6AP binding site. The majority of cervical carcinomas show low levels of E6AP, suggesting that E6AP is not necessary for E6 protein expression or function. Our hypothesis is that one mechanism of HPV persistence is that HPV encodes proteins that prevent E6AP-mediated ubiquitination and degradation of cellular proteins that are required for productive HPV infection. 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