VapC proteins from Mycobacterium tuberculosis share ribonuclease sequence specificity but differ in regulation and toxicity. [PDF]
PLoS ONE, 2018 The chromosome of Mycobacterium tuberculosis (Mtb) contains a large number of Type II toxin-antitoxin (TA) systems. The majority of these belong to the VapBC TA family, characterised by the VapC protein consisting of a PIN domain with four conserved ...
Abigail Sharrock +4 more
doaj +4 more sources
Characterization of the Deep-Sea Streptomyces sp. SCSIO 02999 Derived VapC/VapB Toxin-Antitoxin System in Escherichia coli [PDF]
Toxins, 2016 Toxin-antitoxin (TA) systems are small genetic elements that are ubiquitous in prokaryotes. Most studies on TA systems have focused on commensal and pathogenic bacteria; yet very few studies have focused on TAs in marine bacteria, especially those ...
Yunxue Guo +4 more
doaj +3 more sources
In Silico Analysis of Genetic VapC Profiles from the Toxin-Antitoxin Type II VapBC Modules among Pathogenic, Intermediate, and Non-Pathogenic Leptospira [PDF]
Microorganisms, 2019 Pathogenic Leptospira spp. is the etiological agent of leptospirosis. The high diversity among Leptospira species provides an array to look for important mediators involved in pathogenesis.
Alexandre P. Y. Lopes +5 more
doaj +3 more sources
Toxins VapC and PasB from Prokaryotic TA Modules Remain Active in Mammalian Cancer Cells [PDF]
Toxins, 2014 Among the great number of addictive modules which have been discovered, only a few have been characterized. However, research concerning the adoption of toxins from these systems shows their great potential as a tool for molecular biology and medicine.
Łukasz Wieteska +3 more
doaj +3 more sources
The vapB-vapC operon of Acidovorax citrulli functions as a bona-fide toxin-antitoxin module [PDF]
Frontiers in Microbiology, 2016 Toxin–antitoxin systems are commonly found on plasmids and chromosomes of bacteria and archaea. These systems appear as biscystronic genes encoding a stable toxin and a labile antitoxin, which protects the cells from the toxin’s activity. Under specific,
Reut eShavit +4 more
doaj +3 more sources
VAPC, an human endogenous inhibitor for hepatitis C virus (HCV) infection, is intrinsically unstructured but forms a "fuzzy complex" with HCV NS5B. [PDF]
PLoS ONE, 2012 Nearly 200 million people are infected by hepatitis C virus (HCV) worldwide. For replicating the HCV genome, the membrane-associated machinery needs to be formed by both HCV non-structural proteins (including NS5B) and human host factors such as VAPB ...
Shaveta Goyal +6 more
doaj +4 more sources
VapC toxins from Mycobacterium tuberculosis are ribonucleases that differentially inhibit growth and are neutralized by cognate VapB antitoxins. [PDF]
PLoS ONE, 2011 The chromosome of Mycobacterium tuberculosis (Mtb) encodes forty seven toxin-antitoxin modules belonging to the VapBC family. The role of these modules in the physiology of Mtb and the function(s) served by their expansion are unknown.
Bintou Ahmadou Ahidjo +7 more
doaj +4 more sources
PLoS ONE, 2014 The prokaryotic ubiquitous Toxin-Antitoxin (TA) operons encode a stable toxin and an unstable antitoxin. The most accepted hypothesis of the physiological function of the TA system is the reversible cessation of cellular growth under stress conditions ...
Alexandre P Y Lopes +8 more
doaj +4 more sources
Effect of rickettsial toxin VapC on its eukaryotic host.
PLoS ONE, 2011 Rickettsia are intracellular bacteria typically associated with arthropods that can be transmitted to humans by infected vectors. Rickettsia spp. can cause mild to severe human disease with a possible protection effect of corticosteroids when antibiotic ...
Gilles Audoly +9 more
doaj +4 more sources
Phosphorylation of VapB antitoxins affects intermolecular interactions to regulate VapC toxin activity in <i>Mycobacterium tuberculosis</i>. [PDF]
J BacteriolToxin–antitoxin modules are present in many bacterial pathogens. The VapBC family is particularly abundant in members of the Mycobacterium tuberculosis complex, with 50 modules present in the M. tuberculosis genome.
Malakar B +4 more
europepmc +3 more sources