Molecular mechanism of paramyxovirus infection in the epithelial cells

2017 Fiscal Year Final Research Report

• Project/Area Number: 16K19146
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Virology
• Research Institution: National Institute of Infectious Diseases
• Principal Investigator: Katoh Hiroshi 国立感染症研究所, ウイルス第三部, 主任研究官 (80711712)
• Project Period (FY): 2016-04-01 – 2018-03-31
• Keywords: パラミクソウイルス / ムンプスウイルス / 麻疹ウイルス / Heat shock protein 90 / Lタンパク質 / 複合体形成 / RNA合成

Outline of Final Research Achievements

In order to clarify the molecular mechanisms of paramyxovirus infection in the epithelial cells, we analyzed the roles of host chaperone protein, heat shock protein 90 (Hsp90), in the mumps virus and measles virus infections. The Hsp90 activity was required for the stability and activity of the L protein that is the catalytic subunit of viral polymerase, because an Hsp90-specific inhibitor, 17-AAG, destabilized the L protein and suppressed the viral RNA synthesis. The data in this study show that the Hsp90 chaperone machinery assists in the maturation of the paramyxovirus L protein, and thereby in the formation of a mature polymerase complex and efficient viral replication.

Free Research Field

ウイルス学