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Characterization of humam respiratory syncytial virus nucleoprotein and methylosome interaction.

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Juliana Kaori Ogawa
Total Authors: 1
Document type: Master's Dissertation
Press: São Paulo.
Institution: Universidade de São Paulo (USP). Instituto de Ciências Biomédicas (ICB/SDI)
Defense date:
Examining board members:
Armando Morais Ventura; Viviane Fongaro Botosso; Bryan Eric Strauss
Advisor: Armando Morais Ventura

In this project we had as objective to characterize the interaction observed previously in the laboratory of viral nucleoprotein (N) with PRMT5 and WDR77 proteins that constitute the cell metilosome. We confirmed that this interaction occurs through co-imunoprecipitation in human cells and in vitro interaction of these purified proteins. We also demonstrated the co-localization of these proteins in inclusion bodies, by immunofluorescence and confocal microscopy. Inhibiting or enhancing PRMT5 expression we didnt see effect on viral replication. Our results show that methylation occurs in both arginine and lysine residues, through reactivity with antibodies specific to these modifications, and analysis by mass spectrometry. We tested the effect of arginine and lysine methylation and de-methylation inhibitors in viral replication. We obtained significant inhibitory effect on HRSV replication with a lysine methylation inhibitor, UNC0646, indicating that N-metilossome interaction has the potential to be exploited as a therapeutic target in developing antiviral drugs. (AU)

FAPESP's process: 14/03944-2 - Characterization of the interaction between the methylosome and the human respiratory syncytial virus nucleocapsid
Grantee:Juliana Kaori Ogawa
Support Opportunities: Scholarships in Brazil - Master