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Ebola Virus VP35 Interacts Non-Covalently with Ubiquitin Chains to Promote Viral Replication Creating New Therapeutic Opportunities.

Carlos Andrés Rodriguez-SalazarSarah van TolOlivier MailhotGabriel GaldinoNatália TeruelLihong ZhangAbbey N WarrenMaría González-OrozcoAlexander N FreibergRafael J NajmanovichMaria I Giraldo GiraldoRicardo Rajsbaum
Published in: bioRxiv : the preprint server for biology (2023)
Ebola virus infection can result in high mortality rates with extreme risk of person-to-person transmission. Sporadic outbreaks in Africa have resulted in thousands of fatal cases, highlighting that there is still insufficient knowledge to develop effective antiviral therapies. Like other viruses, Ebola utilizes the host machinery to replicate. Understanding how viral and host proteins interact can help identifying targets for the rational design of antiviral drugs. Here, we identified interactions between the cellular ubiquitin machinery and the Ebola virus polymerase cofactor protein VP35, which are important for efficient virus replication. We developed an approach to identify and block these virus-host interactions using small chemical compounds, which provides a useful tool to study functional molecular mechanisms and at the same time a potential approach to antiviral therapies.
Keyphrases
  • disease virus
  • sars cov
  • healthcare
  • small molecule
  • binding protein
  • late onset
  • cardiovascular disease
  • risk factors
  • amino acid