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L protease from foot and mouth disease virus confers eIF2‐independent translation for mRNAs bearing picornavirus IRES
Author(s) -
Moral-López Pablo,
Alvarez Enrique,
Redondo Natalia,
Skern Tim,
Carrasco Luis
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.09.030
Subject(s) - internal ribosome entry site , foot and mouth disease virus , picornavirus , eif4g , translation (biology) , protein biosynthesis , biology , initiation factor , aphthovirus , microbiology and biotechnology , virology , protease , virus , chemistry , rna , biochemistry , messenger rna , enzyme , gene
The leader protease (L pro ) from foot‐and‐mouth disease virus (FMDV) has the ability to cleave eIF4G, leading to a blockade of cellular protein synthesis. In contrast to previous reports, our present findings demonstrate that FMDV L pro is able to increase translation driven by FMDV IRES. Additionally, inactivation of eIF2 subsequent to phosphorylation induced by arsenite or thapsigargin in BHK cells blocks protein synthesis directed by FMDV IRES, whereas in the presence of L pro , significant translation is found under these conditions. This phenomenon was also observed in cell‐free systems after induction of eIF2 phosphorylation by addition of poly(I:C).