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ProteomicsA conserved tryptophan in the acylated segment controls β2- integrin-independent cell penetration of RTX toxins
The post-translationally acylated Repeats in ToXins (RTX) leukotoxins, such as the adenylate cyclase (CyaA) or α-hemolysin (HlyA), bind β2-integrins of leukocytes, but also penetrate cells lacking these receptors. We show that the indole of conserved tryptophans within the acylated segments, e.g. W8...
ORGANISM(S): Bordetella pertussis 
2023-07-11 | PXD041207 | Pride
Hydrogen-deuterium exchange Tryptophan residue Adenylate cyclase toxin Α-hemolysin Trp-pro interaction Thermal stability Β2-integrins Rtx toxin Acylated segment Cytotoxicity 
ProteomicsA conserved tryptophan in the acylated segment controls β2- integrin-independent cell penetration of RTX toxins
The post-translationally acylated Repeats in ToXins (RTX) leukotoxins, such as the adenylate cyclase (CyaA) or α-hemolysin (HlyA), bind β2-integrins of leukocytes, but also penetrate cells lacking these receptors. We show that the indole of conserved tryptophans within the acylated segments, e.g. W8...
ORGANISM(S): Escherichia coli Bacteria Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251) 
2023-06-30 | PXD041280 | Pride
Hydrogen-deuterium exchange Tryptophan residue Adenylate cyclase toxin Α-hemolysin Trp-pro interaction Thermal stability Β2-integrins Rtx toxin Acylated segment Cytotoxicity 
ProteomicsNovel calcium-binding sites in the acylated segment control the folding and membrane penetration of RTX toxins
The Repeats in ToXin (RTX) domain of RTX cytolysins harbors numerous hexacoordinated Ca2+-binding sites that facilitate cooperative and vectorial folding of the RTX β-rolls. Recent study identified Ca2+-binding sites in the acylated N-terminal extension of the RTX domain of Bordetella pertussis aden...
ORGANISM(S): Bordetella pertussis 
2026-04-22 | PXD058094 | Pride
Membrane penetration H/d exchange Rtx toxin Folding Calcium binding site Acylated segment 
ProteomicsCalcium-loaded acylated segment controls the membrane penetration capacity of repeats-in-toxin cytolysins
Loading of calcium ions into the numerous carboxy-terminus-proximal binding sites in the Repeats in ToXin (RTX) domains drives the cooperative and vectorial folding of RTX β-roll structures involved in cell binding and membrane penetration of RTX cytolysins. Two additional binding sites for calcium ...
ORGANISM(S): Bordetella pertussis NBRC 107857 Escherichia coli Bacteria 
2026-04-28 | PXD065966 | Pride
Adenylate cyclase toxin Calcium binding sites Rtx toxin Folding 
ProteomicsRetargeting from CR3 to the LFA-1 receptor uncovers the adenylyl cyclase enzymetranslocating segment of Bordetella adenylate cyclase toxin
The Bordetella adenylate cyclase toxinhemolysin (CyaA) and the α-hemolysin (HlyA) of Escherichia coli both belong to the family of cytolytic pore-forming Repeats in ToXin (RTX) cytotoxins. HlyA preferentially binds the αLβ2 integrin LFA-1 (CD11a/CD18) of leukocytes and can promiscuously bind and per...
ORGANISM(S): Escherichia coli Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251) 
2020-05-11 | PXD018789 | Pride
Ac domain translocation Fatty acyl Rtx toxin Acylation Acyltransferase Integrin 
UnknownA conserved tryptophan in the acylated segment of RTX toxins controls their β2 integrin-independent cell penetration.
Not available
S-EPMC10392135 | biostudies-literature
ProteomicsResidues 1 to 563 of α-hemolysin alone form a fully functional pore and their proper membrane insertion depends on the acylation status of the molecule
The acylated pore-forming Repeats in ToXin (RTX) cytolysins α-hemolysin (HlyA) and adenylate cyclase toxin (CyaA) bind primarily to β2 integrins of leukocytes. HlyA binds the common CD18 subunit of the β2 integrins and CyaA selectively binds the CD11b subunit of complement receptor 3 (CR3). However,...
ORGANISM(S): Escherichia coli 
2024-03-25 | PXD046160 | Pride
Acylation Rtx toxin 
UnknownDifferent roles of conserved tyrosine residues of the acylated domains in folding and activity of RTX toxins.
Not available
S-EPMC8494930 | biostudies-literature
UnknownAcyl chains stabilize the acylated domain and determine the receptor-mediated interaction of the Bordetella adenylate cyclase toxin with cell membrane.
Not available
S-EPMC12332401 | biostudies-literature
UnknownHuman Sialidase Neu3 is S-Acylated and Behaves Like an Integral Membrane Protein.
Not available
S-EPMC5482835 | biostudies-literature
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