scholarly journals Post‐translational acylation controls the folding and functions of the CyaA RTX toxin

2019 ◽  
Vol 33 (9) ◽  
pp. 10065-10076 ◽  
Author(s):  
Darragh P. O'Brien ◽  
Sara E. Cannella ◽  
Alexis Voegele ◽  
Dorothée Raoux‐Barbot ◽  
Marilyne Davi ◽  
...  
Keyword(s):  
Rtx Toxin

scholarly journals Fatal Pulmonary Hemorrhage Associated with RTX Toxin-Producing Actinobacillus Equuli Subspecies Haemolyticus Infection in an Adult Horse

2008 ◽  
Vol 20 (1) ◽  
pp. 118-121 ◽  
Author(s):  
Nicola Pusterla ◽  
Megan E. B. Jones ◽  
F. Charles Mohr ◽  
Jamie K. Higgins ◽  
Samantha Mapes ◽  
...  
Keyword(s):  
Pulmonary Hemorrhage ◽  
Rtx Toxin

scholarly journals Detection of RTX toxin genes in gram-negative bacteria with a set of specific probes.

1997 ◽  
Vol 63 (6) ◽  
pp. 2258-2265 ◽  
Author(s):  
P Kuhnert ◽  
B Heyberger-Meyer ◽  
A P Burnens ◽  
J Nicolet ◽  
J Frey
Keyword(s):  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Toxin Genes ◽  
Rtx Toxin

scholarly journals Structural analysis of the Actinobacillus pleuropneumoniae-RTX-toxin I (ApxI) operon.

1993 ◽  
Vol 61 (9) ◽  
pp. 3688-3695 ◽  
Author(s):  
R Jansen ◽  
J Briaire ◽  
E M Kamp ◽  
A L Gielkens ◽  
M A Smits
Keyword(s):  
Structural Analysis ◽  
Actinobacillus Pleuropneumoniae ◽  
Rtx Toxin

scholarly journals Growth Phase Regulation of Vibrio cholerae RTX Toxin Export

2006 ◽  
Vol 189 (5) ◽  
pp. 1827-1835 ◽  
Author(s):  
Bethany Kay Boardman ◽  
Brian M. Meehan ◽  
Karla J. Fullner Satchell
Keyword(s):  
Stationary Phase ◽  
Vibrio Cholerae ◽  
Growth Phase ◽  
Diarrheal Disease ◽  
Outer Membrane Vesicles ◽  
Transcriptional Level ◽  
Type I ◽  
Bacterial Membranes ◽  
Rtx Toxin ◽  
Phase Regulation

ABSTRACT Vibrio cholerae, the causative agent of the severe diarrheal disease cholera, secretes several “accessory” toxins, including RTX toxin, which causes the cross-linking of the actin cytoskeleton. RTX toxin is exported to the extracellular milieu by an atypical type I secretion system (T1SS), and we previously noted that RTX-associated activity is detectable only in supernatant fluids from log phase cultures. Here, we investigate the mechanisms for regulating RTX toxin activity in supernatant fluids. We find that exported proteases are capable of destroying RTX activity and may therefore play a role in the growth phase regulation of toxin activity. We determined that the absence of RTX toxin in stationary-phase culture supernatant fluids is also due to a lack of toxin secretion and not attributable to solely proteolytic degradation. We ascertained that the T1SS apparatus is regulated at the transcriptional level by growth phase control that is independent of quorum sensing, unlike other virulence factors of V. cholerae. Additionally, in stationary-phase cultures, all RTX toxin activity is associated with bacterial membranes or outer membrane vesicles.

scholarly journals Autoprocessing of the Vibrio cholerae RTX toxin by the cysteine protease domain

2007 ◽  
Vol 26 (10) ◽  
pp. 2552-2561 ◽  
Author(s):  
Kerri-Lynn Sheahan ◽  
Christina L Cordero ◽  
Karla J Fullner Satchell
Keyword(s):  
Vibrio Cholerae ◽  
Cysteine Protease ◽  
Protease Domain ◽  
Rtx Toxin ◽  
Cysteine Protease Domain

scholarly journals Vibrio cholerae Strains with Mutations in an Atypical Type I Secretion System Accumulate RTX Toxin Intracellularly

2004 ◽  
Vol 186 (23) ◽  
pp. 8137-8143 ◽  
Author(s):  
Bethany Kay Boardman ◽  
Karla J. Fullner Satchell
Keyword(s):  
Binding Site ◽  
Vibrio Cholerae ◽  
Secretion System ◽  
Atp Binding ◽  
Type I ◽  
Atp Binding Site ◽  
Rtx Toxin ◽  
Component Type ◽  
Transport Atpases

ABSTRACT This study shows that the Vibrio cholerae RTX toxin is secreted by a four-component type I secretion system (TISS) encoded by rtxB, rtxD, rtxE, and tolC. ATP-binding site mutations in both RtxB and RtxE blocked secretion, demonstrating that this atypical TISS requires two transport ATPases that may function as a heterodimer.

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