Results 181 to 190 of about 8,609 (220)
Some of the next articles are maybe not open access.

Anaerobiosis, growth phase and Actinobacillus pleuropneumoniae RTX toxin production

Microbial Pathogenesis, 2004
Actinobacillus pleuropneumoniae is the causative agent of an economically significant form of porcine pleuropneumonia. This bacterium produces four distinct RTX toxins (ApxI-ApxIV) that play a key role in its pathogenesis, but further characterization of these hemolytic toxins is needed to identify the environmental signals and genes that affect their ...
Erika, Jarma   +2 more
openaire   +2 more sources

Resveratrol modulates RTX toxin-induced cytotoxicity through interference in adhesion and toxin production

European Journal of Pharmacology, 2010
Host-parasite contact is a prerequisite for the acute cytotoxicity of Vibrio vulnificus, which is mediated primarily by RtxA1, a repeat in toxin (RTX) toxin. We found that resveratrol (at 10 or 30 microM), a natural polyphenol, protected HeLa cells from V. vulnificus cytotoxicity.
Jong Ro, Kim   +5 more
openaire   +2 more sources

RTX toxin genotypes and phenotypes in Actinobacillus pleuropneumoniae field strains

Journal of Clinical Microbiology, 1994
Actinobacillus pleuropneumoniae serotype reference strains and 204 A. pleuropneumoniae field strains representing all 12 serotypes and both biovars 1 and 2, obtained from laboratories from various countries worldwide, were analyzed for the presence of the toxin genes apxIC, apxIA, apxIB, apxID, apxIIC, apxIIA, apxIIIC, apxIIIA, apxIIIB, and apxIIID by ...
M, Beck   +6 more
openaire   +2 more sources

Membrane-Damaging Toxins: Family of RTX Toxins

2014
The major cellular effect of RTX toxins has been ascribed to their pore-forming capacity, resulting in plasma membrane lesions and osmotic lysis. One group of RTX toxins consists of hemolysins, such as Escherichia coli α-hemolysin (HlyA) and Actinobacillus pleuropneumoniae (ApxIA), that are toxic for a wide range of cell types from various species ...
Camilla Oxhamre, Agneta Richter-Dahlfors
openaire   +1 more source

Structure and function of RTX toxins

2015
Repeat-in-ToXin (RTX) toxins are pathogenic factors produced by a wide variety of Gram-negative bacteria. These toxins are commonly known as hemolysins or leukotoxins, as they are able to form pores in the membrane of their eukaryotic target cells.
Chenal, Alexandre   +2 more
openaire   +2 more sources

Biological effects of RTX toxins: the possible role of lipopolysaccharide

Trends in Microbiology, 1995
RTX toxins are a family of related exotoxins with hemolytic, leukotoxi c and leukocyte-stimulating activities that are produced by a diverse array of Gram-negative bacteria. Lipopolysaccharide might be required for the maximal production of some RTX toxins and might be a cofactor in some of the biological effects of RTX toxins.
C J, Czuprynski, R A, Welch
openaire   +2 more sources

Virulence in Actinobacillus pleuropneumoniae and RTX toxins

Trends in Microbiology, 1995
RTX toxins are pore-forming, cytolytic protein toxins that occur widely among pathogenic Gram-negative bacteria. RTX toxins appear to play a direct role in the virulence of Actinobacillus pleuropneumoniae, the etiological agent of porcine pleuropneumonia.
openaire   +2 more sources

AvxA, a composite serine-protease-RTX toxin of Avibacterium paragallinarum

Veterinary Microbiology, 2013
Avibacterium paragallinarum, the etiological agent of infectious coryza in chicken, was found to encode a bivalent serine-protease - RTX-porin toxin named AvxA. This toxin is encoded on a classical RTX operon structure with the activator gene avxC, the structural serin-protease-RTX toxin gene avxA, and the genes for a proper type I secretion system ...
Eliane, Küng, Joachim, Frey
openaire   +2 more sources

New Sea Anemone Toxin RTX-VI Selectively Modulates Voltage-Gated Sodium Channels

Doklady Biochemistry and Biophysics, 2020
A new neurotoxin RTX-VI that modulates the voltage-gated sodium channels (NaV) was isolated from the ethanolic extract of the sea anemone Heteractis crispa. Its amino acid sequence was determined using the combination of Edman degradation and tandem mass spectrometry.
R S, Kalina   +8 more
openaire   +2 more sources

Molecular Analysis of theActinobacillus pleuropneumoniaeRTX Toxin-III Gene Cluster

DNA and Cell Biology, 1993
Actinobacillus pleuropneumonia strains that secrete three different exotoxins (ApxI, ApxII, and ApxIII) have been implicated in the etiology of porcine pleuropneumonia. To understand the role of these toxins in the pathogenesis of this disease, we have previously reported the cloning of the hemolysin gene (apxII) (Chang et al., 1989a), which encodes a ...
Y F, Chang   +4 more
openaire   +2 more sources

Home - About - Disclaimer - Privacy