Open AccessDifferential IFN‐α/β production suppressing capacities of the leader proteins of mengovirus and foot‐and‐mouth disease virus
Author(s) -
Hato Stanleyson V.,
Sorgeloos Frédéric,
Ricour Celine,
Zoll January,
Melchers Willem J. G.,
Michiels Thomas,
Van Kuppeveld Frank J. M.
Publication year - 2010
Publication title -
cellular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.542
H-Index - 138
eISSN - 1462-5822
pISSN - 1462-5814
DOI - 10.1111/j.1462-5822.2009.01395.x
Subject(s) - biology , virus , virology , interferon , foot and mouth disease virus , rna , chemokine , messenger rna , protein biosynthesis , viral replication , protease , picornavirus , aphthovirus , transcription (linguistics) , immune system , gene , microbiology and biotechnology , immunology , enzyme , genetics , biochemistry , linguistics , philosophy
Summary Picornaviruses encompass a large family of RNA viruses. Some picornaviruses possess a leader (L) protein at the N‐terminus of their polyprotein. The L proteins of encephalomyocarditis virus, a cardiovirus, and foot‐and‐mouth disease virus (FMDV), an aphthovirus, are both dispensable for replication and their major function seems to be the suppression of antiviral host cell responses. Previously, we showed that the L protein of mengovirus, a strain of encephalomyocarditis virus, inhibits antiviral responses by inhibiting type I interferon (IFN‐α/β) gene transcription. The L protein of the FMDV is a protease (L pro ) that cleaves cellular factors to reduce cytokine and chemokine mRNA production and to inhibit cap‐dependent cellular host mRNA translation, thereby limiting the production of proteins with antiviral activity. In this study, we constructed a viable chimeric mengovirus that expresses FMDV L pro in place of the authentic L protein in order to compare the efficiency of the immune evasion mechanisms mediated by L and L pro respectively. We show that in this mengovirus background the L protein is more potent than FMDV L pro in suppressing IFN‐α/β responses. Yet, FMDV L pro is important to antagonize infection‐limiting responses both in vitro and in vivo .