Research Article Open Access
Volume 1 | Issue 1 | DOI: https://doi.org/10.33696/immunology.1.005

Design of a Peptide Against the Interaction Between Immune Response Protein TRAF5 and the Oncoprotein E6 from HPV

  • 1Biological Sciences Institute, Federal University of Goiás, UFG, GO, Brazil
  • 2Replicon, Pontifical Catholic University of Goiás, PUC-GO, Brazil
  • 3Department of Biochemistry, University of Brasilia, UnB, DF, Brazil
  • 4Department of Medicine, University Center of Anápolis, Unievangélica - GO, Brazil
  • 5Department of Pharmacy, United College of Campinas, FacUnicamps - GO, Brazil
+ Affiliations - Affiliations

Corresponding Author

Silva KSF, smallbinho@hotmail.com

Received Date: April 10, 2019

Accepted Date: June 17, 2019


HPV is the most common sexual transmitted disease worldwide. There is no specific treatment for the disease and the impact of HPV on public health and the necessity for more prominent diagnosis and treatment are reflected by the genital infection and cervical cancer statistics. The disease has a high rate of deaths due to its relation to cancer, principally cervix cancer. Cancerous warts also affect the vulva, vagina, anus, penis, mouth and throat. There are more than 80 HPV types and more than 40 infect the genital tract. Several HPV genes and proteins are potential candidates as genetic markers for the development of cancer and they are target for vaccines and HPV treatment. E6 exerts pleiotropic functions, including signaling, cell cycle regulation, cell line transformation, immortalization of primary cell line and genome stability regulation. The E6 protein interacts with several host-proteins, including TRAF5, which is related to cytokines signaling. E6 induces the destruction of host regulatory proteins through the proteasome system, being an important target for the development of new therapies against HPV. Here, we hypothesize that interaction between TRAF5 and E6 could be modulated in order to inhibit the activity of E6. We have shown an in silico approach of interaction between TRAF5 and HPV E6 through the identification of hot spots within the interface of interaction of the complex. We propose a new peptide that interacts and inhibits HPV E6. For a future perspective, the peptide designed will be tested in vitro and other regions of the interface of interaction will also be screened so that other peptides could also be designed and tested.


HPV; TRAF5; hot spots screening; design of peptide

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