Site-specific chemoenzymatic labeling of aerolysin enables the identification of new aerolysin receptors. [PDF]
Aerolysin is a secreted bacterial toxin that perforates the plasma membrane of a target cell with lethal consequences. Previously explored native and epitope-tagged forms of the toxin do not allow site-specific modification of the mature toxin with a ...
Irene Wuethrich +7 more
doaj +8 more sources
Aerolysin Nanopores for Single-Molecule Analysis [PDF]
Biological nanopores have become powerful tools for single-molecule analysis in many fields, including metal ion detection, single-molecule chemistry, polymer size discrimination, nucleic acid sequencing, and protein/peptide/glycan analysis.
Yun Zhang, Chan Cao
doaj +4 more sources
Eliminating the Interference of Neighboring Nucleobases in Aerolysin for Nanopore Sequencing [PDF]
Biological nanopores have revolutionized DNA sequencing with their incredible advantages of long reads, high throughput, portability, and low material requirement. Despite numerous improvements, base calling remains challenging due to the influence of neighboring nucleobases at the reading site.
Chan Cao, Verena Rukes
exaly +5 more sources
Driven Translocation of Polynucleotides Through an Aerolysin Nanopore [PDF]
Aerolysin has been used as a biological nanopore for studying peptides, proteins, and oligosaccharides in the past two decades. Here, we report that wild-type aerolysin could be utilized for polynucleotide analysis. Driven a short polynucleotide of four nucleotides length through aerolysin occludes nearly 50% amplitude of the open pore current ...
Chan, Cao +4 more
openaire +3 more sources
Cryo-EM structure of aerolysin variants reveals a novel protein fold and the pore-formation process [PDF]
Aerolysin is a secreted bacterial pore forming toxin that inserts into the host plasma membrane, potentially leading to cell death. Here the authors present Cryo-EM structures of aerolysin arrested at different stages of the pore formation process that ...
Ioan Iacovache +5 more
doaj +5 more sources
Dissecting the Membrane Association Mechanism of Aerolysin Pores at Femtomolar Concentrations Using Water as a Probe [PDF]
Aerolysin is a bacterial toxin that forms transmembrane pores at the host plasma membrane and has a narrow internal diameter and great stability. These assets make it a highly promising nanopore for detecting biopolymers such as nucleic acids and ...
Juan Francisco Bada Juarez +2 more
exaly +3 more sources
Aerolysin from Aeromonas hydrophila and Related Toxins
Aeromonads are ubiquitous gram-negative bacteria found in aqueous environments. Some members of the genus are pathogenic for fish, reptiles and cows. In humans, Aeromonas infection is mainly associated with grastrointestinal diseases, but in immuno-compromised individuals infection can lead to septicemia and meningitis (Austin et al. 1996).
Fivaz, M. +3 more
openaire +4 more sources
Increased Stability upon Heptamerization of the Pore-forming Toxin Aerolysin [PDF]
Aerolysin is a bacterial pore-forming toxin that is secreted as an inactive precursor, which is then processed at its COOH terminus and finally forms a circular heptameric ring which inserts into membranes to form a pore. We have analyzed the stability of the precursor proaerolysin and the heptameric complex.
Lesieur, C. +5 more
core +6 more sources
The purpose of this study was to evaluate the pathogene of Aeromonas hydrophila genes (Aerolysin) as the cause of Lepidochelys olivacea death and to perform the antibiotic sensitivity test for antibiotic that often used in order to provide the best ...
Rima Ratnanggana Prasetya +2 more
doaj +2 more sources
Homology between the seed cytolysin enterolobin and bacterial aerolysins
Enterolobin, a 55-kDa cytolytic, inflammatory, and insecticidal protein isolated from seeds of the Brazilian tree Enterolobium contortisiliquum (Leguminosae-Mimosoideae) has been further purified and partially sequenced by using both manual and automated methods. A computational search of enterolobin partial amino acid sequence against the PIR database
M V, Sousa +3 more
openaire +3 more sources

