12:00 Noon, Monday, 7th December
Room 208, 2nd Floor
720 Cumberland St
University of Otago, Microbiology & Immunology
'Protein modifications during influenza A virus infection'
The ever-evolving nature of influenza virus has restricted the development of universal vaccine and efficacy of seasonal vaccines. Furthermore, the emergence of drug-resistant influenza variants has made the available drugs almost ineffective. Therefore, exploring new approaches such as identifying protein modifications and understanding their roles in influenza virus-host interactions might facilitate the development of novel antiviral strategies.
We employed mass spectrometry approach to identify global protein modifications occurring in response to influenza A virus (IAV) infection. A range of viral and host proteins was found to be modified by multiple modifications including methylation, acetylation, and allysine. The majority of modified amino acids in viral proteins were highly conserved and exhibited sequence homology across influenza viruses, indicating their fundamental importance in influenza virus biology. Further, the modified host proteins were assigned to multiple host pathways, some of which were already known to be involved in influenza virus infection. The analysis of acetylation-catalysing enzymes, histone acetyltransferases showed a proviral role of N-alpha-acetyltransferase 60 (Naa60) during IAV infection. Mechanistically, Naa60 was found to be an important component of IAV-induced host innate antiviral response. Together, these data point to the critical role of protein modifications in influenza virus infection.