Results 141 to 150 of about 1,147 (168)

Growth and Translation Inhibition Through Sequence-Specific RNA Binding by Mycobacterium tuberculosis VapC Toxin [PDF]

Journal of Biological Chemistry, 2012
The Mycobacterium tuberculosis genome harbors an unusually large number of toxin-antitoxin (TA) modules. Curiously, over half of these are VapBC (virulence-associated protein) family members. Nonetheless, the cellular target, precise mode of action, and physiological role of the VapC toxins in this important pathogen remain unclear.
Robert N Husson, Nancy A Woychik, Masayori Inouye   +2 more
exaly   +3 more sources

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Resonance assignments of a VapC family toxin from Clostridium thermocellum

Biomolecular NMR Assignments, 2016
Toxin-antitoxin (TA) systems widely exist in bacterial plasmids, phages, and chromosomes and play important roles in growth persistence and host-pathogen interaction. Virulence associated protein BC (VapBC) family TAs are the most abundant TAs in bacteria and many pathogens contain a large number of vapBC loci in the genome which have been extensively ...
Chen Wang, Jinsong Xuan, Qiu Cui, Yingang Feng   +3 more
openaire   +2 more sources

VapC toxin inhibition as a method for prevention of the formation of resting forms of mycobacteria

Applied Biochemistry and Microbiology, 2016
It has been shown that inactivation of the VapC toxin from the VapВС toxin-antitoxin system prevents mycobacterial cells from transitioning to an ovoid state that meets the criteria of dormancy. The results indicate a potential target for medicines that prevent the development of latent tuberculosis infection and provide a basis to obtain bacterial ...
O I, Demidenok, M S, Shumkov, A V, Goncharenko   +2 more
openaire   +2 more sources

Are All VapC Toxins of Mycobacterium tuberculosis Endowed With Enigmatic RNase Activity?

Journal of Biosciences
Mycobacterium tuberculosis (M. tb) employs an extensive network of more than 90 toxin-antitoxin systems, and among them, VapC toxins are the most abundant. While most VapCs function as classical RNases with toxic effects, a significant number of them do not exhibit toxicity.
Seyed E. Hasnain, Nasreen Z Ehtesham, Sheeba Zarin   +2 more
exaly   +3 more sources

Structure-Based De Novo Design of Mycobacterium Tuberculosis VapC-Activating Stapled Peptides

ACS Chemical Biology, 2020
Toxin-antitoxin (TA) systems have been considered essential factors for bacterial survival. During our drug development program aimed against tuberculosis (TB), we discovered certain peptides that mimic the binding of the VapBC30 complex, leading to the arrest of bacterial cell growth and eventually cell death.
Sung-Min Kang, Heejo Moon, Sang-Woo Han, Do-Hee Kim, Byeong Moon Kim, Bong-Jin Lee   +5 more
openaire   +2 more sources

Structural analysis of the active site architecture of the VapC toxin from Shigella flexneri

Proteins: Structure, Function, and Bioinformatics, 2016
ABSTRACTThe VapC toxin from the Shigella flexneri 2a virulence plasmid pMYSH6000 belongs to the PIN domain protein family, which is characterized by a conserved fold with low amino acid sequence conservation. The toxin is a bona fide Mg2+‐dependent ribonuclease and has been shown to target initiator tRNAfMet in vivo. Here, we present crystal structures
Xu, Kehan, Dedic, Emil; id_orcid 0000-0003-1372-4932, Brodersen, Ditlev Egeskov; id_orcid 0000-0002-5413-4667   +2 more
openaire   +3 more sources

Treatment of feline intermediate to high‐grade alimentary lymphoma: A retrospective evaluation of 55 cats treated with the VAPC combination chemotherapy protocol (2017–2021)

Veterinary and Comparative Oncology, 2023
AbstractThe most commonly utilized protocols to treat lymphoma in cats employ vincristine, cyclophosphamide and prednisone; with additional drugs sometimes used including L‐asparaginase and doxorubicin. Medical records were reviewed for 55 cats with alimentary lymphoma treated with a novel multiagent protocol using prednisolone, L‐asparaginase ...
Antony Stewart Moore, Angela Erica Frimberger   +1 more
openaire   +2 more sources

Structural and Functional Study of the Klebsiella pneumoniae VapBC Toxin–Antitoxin System, Including the Development of an Inhibitor That Activates VapC

Journal of Medicinal Chemistry, 2020
Klebsiella pneumoniae is one of the most critical opportunistic pathogens. TA systems are promising drug targets because they are related to the survival of bacterial pathogens. However, structural information on TA systems in K. pneumoniae remains lacking; therefore, it is necessary to explore this information for the development of antibacterial ...
Sung-Min Kang, Chenglong Jin, Do-Hee Kim, Yuno Lee, Bong-Jin Lee   +4 more
openaire   +2 more sources

Ectopic production of VapCs from Enterobacteria inhibits translation and trans‐activates YoeB mRNA interferase

Molecular Microbiology, 2009
SummaryToxin–antitoxin loci have been identified in almost all free‐living prokaryotes, often in high copy numbers. The biological function and molecular targets of the abundant vapBC loci are not yet known. Here we analyse the vapBC loci of Salmonella LT2 and Shigella plasmid pMYSH6000.
Winther KS, Gerdes K
openaire   +3 more sources

Co‐expression and purification of a toxin‐antitoxin VapC–VapB complex from the E. coli O145:H28 strain RM12581 associated with a Romain lettuce outbreak.

The FASEB Journal, 2020
VapC and VapB are the toxin and anti‐toxin proteins, respectively, of the VapCB toxin–antitoxin system found in bacteria and associated with stunting cell growth during stressful conditions. VapC homologs typically are tRNA endonucleases, and VapB homologs are known to bind to double‐stranded DNA, as well as VapC to inihibit its ...
Seth Patrick Jones, Christian Goossen, Sean Lewis, Annie Delaney, Michael Gleghorn   +4 more
openaire   +1 more source