Abstract
The leader proteinase (Lpro) of the foot-and-mouth disease virus inhibits the host innate immune response by at least three different mechanisms. The most well-characterised of these is the prevention of the synthesis of cytokines such as interferons immediately after infection, brought about by specific proteolytic cleavage of the eukaryotic initiation factor 4G. This prevents the recruitment of capped cellular mRNA; however, the viral RNA can be translated under these conditions. The two other mechanisms are the induction of NF-κB cleavage and the deubiquitination of immune signalling molecules. This review focuses on the structure-function relationships in Lpro responsible for these widely divergent activities.
Acknowledgments
This work was supported by grants P20889 and P24038 from the Austrian Science Foundation to T.S.
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©2014 by De Gruyter
Artikel in diesem Heft
- Frontmatter
- Guest Editorial
- Highlight: The protease web
- Angiotensin-I converting enzyme (ACE): structure, biological roles, and molecular basis for chloride ion dependence
- Non-B HIV-1 subtypes in sub-Saharan Africa: impact of subtype on protease inhibitor efficacy
- Inflammatory outcomes of apoptosis, necrosis and necroptosis
- Angiotensin-converting enzyme overexpression in myelocytes enhances the immune response
- The leader proteinase of foot-and-mouth disease virus: structure-function relationships in a proteolytic virulence factor
- Immune-modulating effects of alpha-1 antitrypsin
- Mammalian gamete fusion depends on the inhibition of ovastacin by fetuin-B
- The activity and localization patterns of cathepsins B and X in cells of the mouse gastrointestinal tract differ along its length
- Membrane-type I matrix metalloproteinase-dependent ectodomain shedding of mucin16/ CA-125 on ovarian cancer cells modulates adhesion and invasion of peritoneal mesothelium
- Homology model of human prothrombinase based on the crystal structure of Pseutarin C
- Specific targeting of human caspases using designed ankyrin repeat proteins
- Analysis of the evolution of granule associated serine proteases of immune defence (GASPIDs) suggests a revised nomenclature
Artikel in diesem Heft
- Frontmatter
- Guest Editorial
- Highlight: The protease web
- Angiotensin-I converting enzyme (ACE): structure, biological roles, and molecular basis for chloride ion dependence
- Non-B HIV-1 subtypes in sub-Saharan Africa: impact of subtype on protease inhibitor efficacy
- Inflammatory outcomes of apoptosis, necrosis and necroptosis
- Angiotensin-converting enzyme overexpression in myelocytes enhances the immune response
- The leader proteinase of foot-and-mouth disease virus: structure-function relationships in a proteolytic virulence factor
- Immune-modulating effects of alpha-1 antitrypsin
- Mammalian gamete fusion depends on the inhibition of ovastacin by fetuin-B
- The activity and localization patterns of cathepsins B and X in cells of the mouse gastrointestinal tract differ along its length
- Membrane-type I matrix metalloproteinase-dependent ectodomain shedding of mucin16/ CA-125 on ovarian cancer cells modulates adhesion and invasion of peritoneal mesothelium
- Homology model of human prothrombinase based on the crystal structure of Pseutarin C
- Specific targeting of human caspases using designed ankyrin repeat proteins
- Analysis of the evolution of granule associated serine proteases of immune defence (GASPIDs) suggests a revised nomenclature