Faculty Opinions recommendation of Targeting the latent cytomegalovirus reservoir with an antiviral fusion toxin protein.

2018 ◽  
Author(s):  
Ramon Arens
Keyword(s):  
Fusion Toxin ◽  
Toxin Protein

scholarly journals Fusion toxin protein inhibits CMV infection

2015 ◽  
Vol 14 (8) ◽  
pp. 528-528
Author(s):  
Sarah Crunkhorn
Keyword(s):  
Cmv Infection ◽  
Fusion Toxin ◽  
Toxin Protein

scholarly journals Advances in the treatment of cytomegalovirus

2019 ◽  
Vol 131 (1) ◽  
pp. 5-17 ◽  
Author(s):  
B A Krishna ◽  
M R Wills ◽  
J H Sinclair
Keyword(s):  
Immune Responses ◽  
Dna Polymerase ◽  
Hcmv Infection ◽  
Research Papers ◽  
Fusion Toxin ◽  
Latently Infected ◽  
Congenital Hcmv Infection ◽  
Infected Cells ◽  
Toxin Protein ◽  
Published Research

Abstract Background Human cytomegalovirus (HCMV) is a threat to immunologically weak patients. HCMV cannot yet be eliminated with a vaccine, despite recent advances. Sources of data Sources of data are recently published research papers and reviews about HCMV treatments. Areas of agreement Current antivirals target the UL54 DNA polymerase and are limited by nephrotoxicity and viral resistance. Promisingly, letermovir targets the HCMV terminase complex and has been recently approved by the FDA and EMA. Areas of controversy Should we screen newborns for HCMV, and use antivirals to treat sensorineural hearing loss after congenital HCMV infection? Growing points Growing points are developing drugs against latently infected cells. In addition to small molecule inhibitors, a chemokine-based fusion toxin protein, F49A-FTP, has shown promise in killing both lytically and latently infected cells. Areas timely for developing research We need to understand what immune responses are required to control HCMV, and how best to raise these immune responses with a vaccine.

Targeting Latent Human Cytomegalovirus (CMV) with a Novel Fusion Toxin Protein during Ex Vivo Lung Perfusion

2020 ◽  
Vol 39 (4) ◽  
pp. S83
Author(s):  
R. VP Ribeiro ◽  
T. Ku ◽  
V.H. Ferreira ◽  
M. Galasso ◽  
S. Moshkelgosha ◽  
...  
Keyword(s):  
Human Cytomegalovirus ◽  
Ex Vivo ◽  
Lung Perfusion ◽  
Ex Vivo Lung Perfusion ◽  
Fusion Toxin ◽  
Toxin Protein

scholarly journals Targeting the latent cytomegalovirus reservoir with an antiviral fusion toxin protein

2017 ◽  
Vol 8 (1) ◽  
Author(s):  
B. A. Krishna ◽  
K. Spiess ◽  
E. L. Poole ◽  
B. Lau ◽  
S. Voigt ◽  
...  
Keyword(s):  
Fusion Toxin ◽  
Toxin Protein

Fusion Toxin

2020 ◽  
Author(s):  
Keyword(s):  
Fusion Toxin

Mechanistic Insights into Pore Formation by an α-Pore Forming Toxin: Protein and Lipid Bilayer Interactions of Cytolysin A

2020 ◽  
Vol 54 (1) ◽  
pp. 120-131
Author(s):  
Pradeep Sathyanarayana ◽  
Sandhya S. Visweswariah ◽  
K. Ganapathy Ayappa
Keyword(s):  
Lipid Bilayer ◽  
Pore Formation ◽  
Toxin Protein

scholarly journals Entry of diphtheria toxin-protein A chimeras into cells.

1991 ◽  
Vol 266 (26) ◽  
pp. 17446-17453
Author(s):  
I.H. Madshus ◽  
H. Stenmark ◽  
K. Sandvig ◽  
S. Olsnes
Keyword(s):  
Diphtheria Toxin ◽  
Protein A ◽  
Toxin Protein

scholarly journals A YoeB toxin cleaves both RNA and DNA

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Julia McGillick ◽  
Jessica R. Ames ◽  
Tamiko Murphy ◽  
Christina R. Bourne
Keyword(s):  
Dna Cleavage ◽  
Divalent Cations ◽  
Nuclease Activity ◽  
Dose Dependence ◽  
Cleavage Activity ◽  
Double Stranded Dna ◽  
Dna Cleavage Activity ◽  
Evolutionarily Conserved ◽  
Toxin Protein ◽  
Rna And Dna

AbstractType II toxin-antitoxin systems contain a toxin protein, which mediates diverse interactions within the bacterial cell when it is not bound by its cognate antitoxin protein. These toxins provide a rich source of evolutionarily-conserved tertiary folds that mediate diverse catalytic reactions. These properties make toxins of interest in biotechnology applications, and studies of the catalytic mechanisms continue to provide surprises. In the current work, our studies on a YoeB family toxin from Agrobacterium tumefaciens have revealed a conserved ribosome-independent non-specific nuclease activity. We have quantified the RNA and DNA cleavage activity, revealing they have essentially equivalent dose-dependence while differing in requirements for divalent cations and pH sensitivity. The DNA cleavage activity is as a nickase for any topology of double-stranded DNA, as well as cleaving single-stranded DNA. AtYoeB is able to bind to double-stranded DNA with mid-micromolar affinity. Comparison of the ribosome-dependent and -independent reactions demonstrates an approximate tenfold efficiency imparted by the ribosome. This demonstrates YoeB toxins can act as non-specific nucleases, cleaving both RNA and DNA, in the absence of being bound within the ribosome.

Fusion Protein of Interleukin 4 and Diphtherial Toxin with High Cytotoxicity to Cancer Cells

2004 ◽  
Vol 36 (6) ◽  
pp. 437-442
Author(s):  
Yu-Jian Zhang ◽  
Xiao-Bo Hu ◽  
Su-Xia Li ◽  
Li-Ping Tian ◽  
Sheng-Li Yang ◽  
...  
Keyword(s):  
Fusion Gene ◽  
Cancer Cell Line ◽  
Interleukin 4 ◽  
Toxin Gene ◽  
Cytotoxic Action ◽  
Fusion Toxin ◽  
Good Target ◽  
Sequence Encoding ◽  
High Cytotoxicity ◽  
Mcf 7

Abstract Receptor of human interleukin 4 (hIL4R) has been found to be present on many types of cancer, so it may be a good target for cancer therapy. Here, fusion toxin gene DT4H has been constructed by fusing DNA sequence encoding the first 389 amino acids of diphtherial toxin (DT), which can not bind its own receptor, to human interleukin 4 (hIL4) gene. In order to improve the affinity of fusion toxin for hIL4R, a circularly permuted form of hIL4 (cpIL4) was used. The fusion gene was expressed in Escherichia coli where the fusion toxin DT4H was highly expressed. Purified DT4H was very cytotoxic to cancer cell line U251 cells, and moderate cytotoxic to HepG2 and MCF-7 cells. SGC-7901 cells were insensitive to it. The cytotoxic action of DT4H was specific because it was blocked by excess hIL4. These results suggest that DT4H may be a useful agent in the treatment of certain malignancies.

Killer toxin of Pichia membranifaciens and its possible use as a biocontrol agent against grey mould disease of grapevine

Microbiology ◽  
2004 ◽  
Vol 150 (8) ◽  
pp. 2527-2534 ◽  
Author(s):  
A. Santos ◽  
D. Marquina
Keyword(s):  
Killer Toxin ◽  
Grey Mould ◽  
Toxin Production ◽  
Killer Activity ◽  
Pichia Membranifaciens ◽  
Sds Page ◽  
Toxin Protein ◽  
Killing Action ◽  
Killer Protein ◽  
Potential Use

The use of Pichia membranifaciens CYC 1106 killer toxin against Botrytis cinerea was investigated. This strain exerted a broad-specificity killing action against other yeasts and fungi. At pH 4, optimal killer activity was observed at temperatures up to 20 °C. At 25 °C the toxic effect was reduced to 70 %. The killer activity was higher in acidic medium. Above about pH 4·5 activity decreased sharply and was barely noticeable at pH 6. The killer toxin protein from P. membranifaciens CYC 1106 was purified to electrophoretic homogeneity. SDS-PAGE of the purified killer protein indicated an apparent molecular mass of 18 kDa. Killer toxin production was stimulated in the presence of non-ionic detergents. The toxin concentrations present in the supernatant during optimal production conditions exerted a fungicidal effect on a strain of B. cinerea. The symptoms of infection and grey mould observed in Vitis vinifera plants treated with B. cinerea were prevented in the presence of purified P. membranifaciens killer toxin. The results obtained suggest that P. membranifaciens CYC 1106 killer toxin is of potential use in the biocontrol of B. cinerea.

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