Abstract:
:Diverse members of the Paramyxovirus family of negative-strand RNA viruses effectively suppress host innate immune responses through the actions of their V proteins. The V protein mediates interference with the interferon regulatory RNA helicase MDA5 to avoid cellular antiviral responses. Analysis of the interaction interface revealed the MDA5 helicase C domain as necessary and sufficient for association with V proteins from human parainfluenza virus type 2, parainfluenza virus type 5, measles virus, mumps virus, Hendra virus, and Nipah virus. The identified approximately 130-residue region is highly homologous between MDA5 and the related antiviral helicase LGP2, but not RIG-I. Results indicate that the paramyxovirus V proteins can also associate with LGP2. The V protein interaction was found to disrupt ATP hydrolysis mediated by both MDA5 and LGP2. These findings provide a potential mechanistic basis for V protein-mediated helicase interference and identify LGP2 as a second cellular RNA helicase targeted by paramyxovirus V proteins.
journal_name
J Viroljournal_title
Journal of virologyauthors
Parisien JP,Bamming D,Komuro A,Ramachandran A,Rodriguez JJ,Barber G,Wojahn RD,Horvath CMdoi
10.1128/JVI.00153-09subject
Has Abstractpub_date
2009-07-01 00:00:00pages
7252-60issue
14eissn
0022-538Xissn
1098-5514pii
JVI.00153-09journal_volume
83pub_type
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