Morin B., Coutard B., Lelke M., Ferron F., Kerber R., Jamal S., Frangeul A., Baronti Cécile, Charrel R., de Lamballerie Xavier, Vonrhein C., Lescar J., Bricogne G., Gunther S., Canard B. (2010). The N-terminal domain of the Arenavirus L protein is an RNA endonuclease essential in mRNA transcription. Plos Pathogens, 6 (9), p. e1001038. ISSN 1553-7366.
Titre du document
The N-terminal domain of the Arenavirus L protein is an RNA endonuclease essential in mRNA transcription
Année de publication
2010
Auteurs
Morin B., Coutard B., Lelke M., Ferron F., Kerber R., Jamal S., Frangeul A., Baronti Cécile, Charrel R., de Lamballerie Xavier, Vonrhein C., Lescar J., Bricogne G., Gunther S., Canard B.
Source
Plos Pathogens, 2010,
6 (9), p. e1001038 ISSN 1553-7366
Arenaviridae synthesize viral mRNAs using short capped primers presumably acquired from cellular transcripts by a 'cap-snatching' mechanism. Here, we report the crystal structure and functional characterization of the N-terminal 196 residues (NL1) of the L protein from the prototypic arenavirus: lymphocytic choriomeningitis virus. The NL1 domain is able to bind and cleave RNA. The 2.13 angstrom resolution crystal structure of NL1 reveals a type II endonuclease alpha/beta architecture similar to the N-terminal end of the influenza virus PA protein. Superimposition of both structures, mutagenesis and reverse genetics studies reveal a unique spatial arrangement of key active site residues related to the PD...(D/E) XK type II endonuclease signature sequence. We show that this endonuclease domain is conserved and active across the virus families Arenaviridae, Bunyaviridae and Orthomyxoviridae and propose that the arenavirus NL1 domain is the Arenaviridae cap-snatching endonuclease.
Plan de classement
Entomologie médicale / Parasitologie / Virologie [052]
Localisation
Fonds IRD [F B010052850]
Identifiant IRD
fdi:010052850
