Results 11 to 20 of about 1,567,080 (217)

Structural Insights into Clostridium perfringens Delta Toxin Pore Formation. [PDF]

PLoS ONE, 2013
Clostridium perfringens Delta toxin is one of the three hemolysin-like proteins produced by C. perfringens type C and possibly type B strains. One of the others, NetB, has been shown to be the major cause of Avian Nectrotic Enteritis, which following the
Jessica Huyet, Claire E Naylor, Christos G Savva, Maryse Gibert, Michel R Popoff, Ajit K Basak   +5 more
doaj   +2 more sources

Multifaceted Suppression of Staphylococcal Virulence Phenotypes: In Vitro Study of a Cellular Status With Reduced Agr Activity and Impaired Biofilm. [PDF]

Microbiologyopen
Finding of in vitro S. aureus status with reduced Agr activity and impaired biofilm. ABSTRACT Anti‐quorum sensing (QS) therapy has been focused on to reduce the virulence of pathogenic bacteria. However, there is a risk that suppression of the staphylococcal QS Agr system might promote biofilm formation.
Nguyen NB, Ushijima Y, Sekiya R, Morikawa K, Nguyen LTT.   +4 more
europepmc   +2 more sources

First Report of Antimicrobial Susceptibility and Virulence Gene Characterization Associated with Staphylococcus aureus Carriage in Healthy Camels from Tunisia

Animals, 2021
A total of 318 nasal and rectal swabs were collected from 159 apparently healthy camels (Camelus dromedarius) randomly selected from five regions in southern and central Tunisia and screened for Staphylococcus aureus carriage. Staphylococcus spp.
Faten Ben Chehida, Haythem Gharsa, Wafa Tombari, Rachid Selmi, Sana Khaldi, Monia Daaloul, Karim Ben Slama, Lilia Messadi   +7 more
doaj   +1 more source

Redirecting Pore Assembly of Staphylococcal α-Hemolysin by Protein Engineering [PDF]

ACS Central Science, 2019
α-Hemolysin (αHL), a β-barrel pore-forming toxin (βPFT), is secreted as a water-soluble monomer by Staphylococcus aureus. Upon binding to receptors on target cell membranes, αHL assembles to form heptameric membrane-spanning pores. We have previously engineered αHL to create a protease-activatable toxin that is activated by site-specific proteolysis ...
Sunwoo Koo, Stephen Cheley, Hagan Bayley
openaire   +3 more sources

Antibiotics shaping bacterial genome: deletion of an IS91 flanked virulence determinant upon exposure to subinhibitory antibiotic concentrations. [PDF]

PLoS ONE, 2011
The nucleoid-associated proteins Hha and YdgT repress the expression of the toxin α-hemolysin. An Escherichia coli mutant lacking these proteins overexpresses the toxin α-hemolysin encoded in the multicopy recombinant plasmid pANN202-312R.
Laura Pedró, Rosa C Baños, Sonia Aznar, Cristina Madrid, Carlos Balsalobre, Antonio Juárez   +5 more
doaj   +1 more source

Effect of an electrolyte cation on detecting DNA damage with the latch onstriction of α-hemolysin

, 2014
The effect of an electrolyte cation on the unzipping of furan-containing double-stranded DNA in an α-hemolysin (?HL) nanopore is described. The current through an open ?HL channel increases in proportion to the ion mobility.
Aaron M. Fleming (1314534), Cynthia J. Burrows (1314543), Henry S. White (1339506), Robert Johnson (17160901)   +3 more
core   +5 more sources

The fusion protein of peste des petits ruminants virus is a hemolysin [PDF]

Archives of Virology, 1999
The fusion glycoprotein (F protein) of paramyxoviruses plays a vital role in virus-induced cytopathology. To explore the role of the F protein in peste des petits ruminants virus (PPRV)-induced cytopathology, the F protein of PPRV was purified by immunoaffinity chromatography.
Devireddy, LR, Raghavan, R, Ramachandran, S, Shaila, MS   +3 more
openaire   +3 more sources

Base-excision repair activity of uracil-DNA glycosylase monitored using the latch zone of ?-hemolysin

, 2013
Nanopores have been investigated as a simple and label-free tool to characterize DNA nucleotides when a ssDNA strand translocates through the constriction of the pore.
Yun Ding (234322), Aaron M. Fleming (1314534), Cynthia J. Burrows (1314543), Henry S. White (1339506), Qian Jin (112422), Robert Johnson (17160901)   +5 more
core   +5 more sources

Insights into protein sequencing with an α-Hemolysin nanopore by atomistic simulations [PDF]

Scientific Reports, 2019
AbstractSingle molecule protein sequencing would represent a disruptive burst in proteomic research with important biomedical impacts. Due to their success in DNA sequencing, nanopore based devices have been recently proposed as possible tools for the sequencing of peptide chains.
Di Muccio, Giovanni, Rossini, Aldo Eugenio, Di Marino, Daniele, Zollo, Giuseppe, Chinappi, Mauro   +4 more
openaire   +4 more sources

Unfoldase-mediated protein translocation through an α-hemolysin nanopore [PDF]

Nature Biotechnology, 2013
Using nanopores to sequence biopolymers was proposed more than a decade ago. Recent advances in enzyme-based control of DNA translocation and in DNA nucleotide resolution using modified biological pores have satisfied two technical requirements of a functional nanopore DNA sequencing device. Nanopore sequencing of proteins was also envisioned. Although
Jeff, Nivala, Douglas B, Marks, Mark, Akeson   +2 more
openaire   +2 more sources