Structure of the GspK–GspI–GspJ complex from the enterotoxigenic Escherichia coli type 2 secretion system

2008 ◽  
Vol 15 (5) ◽  
pp. 462-468 ◽  
Author(s):  
Konstantin V Korotkov ◽  
Wim G J Hol
Keyword(s):  
Escherichia Coli ◽  
Secretion System ◽  
Enterotoxigenic Escherichia Coli ◽  
Type 2 Secretion

scholarly journals Structure and Membrane Topography of the Vibrio-Type Secretin Complex from the Type 2 Secretion System of EnteropathogenicEscherichia coli

2017 ◽  
Vol 200 (5) ◽  
Author(s):  
Iain D. Hay ◽  
Matthew J. Belousoff ◽  
Rhys A. Dunstan ◽  
Rebecca S. Bamert ◽  
Trevor Lithgow
Keyword(s):  
Escherichia Coli ◽  
Membrane Proteins ◽  
Outer Membrane ◽  
Secretion System ◽  
Complex Activity ◽  
Content Type ◽  
Intestinal Mucus ◽  
Bam Complex ◽  
Type 2 Secretion

ABSTRACTThe β-barrel assembly machinery (BAM) complex is the core machinery for the assembly of β-barrel membrane proteins, and inhibition of BAM complex activity is lethal to bacteria. Discovery of integral membrane proteins that are key to pathogenesis and yet do not require assistance from the BAM complex raises the question of how these proteins assemble into bacterial outer membranes. Here, we address this question through a structural analysis of the type 2 secretion system (T2SS) secretin from enteropathogenicEscherichia coliO127:H6 strain E2348/69. Long β-strands assemble into a barrel extending 17 Å through and beyond the outer membrane, adding insight to how these extensive β-strands are assembled into theE. coliouter membrane. The substrate docking chamber of this secretin is shown to be sufficient to accommodate the substrate mucinase SteC.IMPORTANCEIn order to cause disease, bacterial pathogens inhibit immune responses and induce pathology that will favor their replication and dissemination. In Gram-negative bacteria, these key attributes of pathogenesis depend on structures assembled into or onto the outer membrane. One of these is the T2SS. TheVibrio-type T2SS mediates cholera toxin secretion inVibrio cholerae, and inEscherichia coliO127:H6 strain E2348/69, the same machinery mediates secretion of the mucinases that enable the pathogen to penetrate intestinal mucus and thereby establish deadly infections.

1H, 15N and 13C resonance assignments and secondary structure of PulG, the major pseudopilin from Klebsiella oxytoca type 2 secretion system

2017 ◽  
Vol 11 (2) ◽  
pp. 155-158 ◽  
Author(s):  
Aracelys López-Castilla ◽  
Bruno Vitorge ◽  
Léa Khoury ◽  
Nelly Morellet ◽  
Olivera Francetic ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Klebsiella Oxytoca ◽  
Resonance Assignments ◽  
Secretion System ◽  
Type 2 Secretion

Structural and Functional Studies of EpsC, a Crucial Component of the Type 2 Secretion System from Vibrio cholerae

2006 ◽  
Vol 363 (2) ◽  
pp. 311-321 ◽  
Author(s):  
Konstantin V. Korotkov ◽  
Brian Krumm ◽  
Michael Bagdasarian ◽  
Wim G.J. Hol
Keyword(s):  
Vibrio Cholerae ◽  
Secretion System ◽  
Functional Studies ◽  
Crucial Component ◽  
Type 2 Secretion

scholarly journals The trans-envelope architecture and function of the type 2 secretion system: new insights raising new questions

2017 ◽  
Vol 105 (2) ◽  
pp. 211-226 ◽  
Author(s):  
Jenny-Lee Thomassin ◽  
Javier Santos Moreno ◽  
Ingrid Guilvout ◽  
Guy Tran Van Nhieu ◽  
Olivera Francetic
Keyword(s):  
Secretion System ◽  
And Function ◽  
Type 2 Secretion

scholarly journals Pseudopilin residue E5 is essential for recruitment by the type 2 secretion system assembly platform

2016 ◽  
Vol 101 (6) ◽  
pp. 924-941 ◽  
Author(s):  
Mangayarkarasi Nivaskumar ◽  
Javier Santos-Moreno ◽  
Christian Malosse ◽  
Nathalie Nadeau ◽  
Julia Chamot-Rooke ◽  
...  
Keyword(s):  
Secretion System ◽  
Type 2 Secretion

scholarly journals Type 2 Secretion Promotes Enterohemorrhagic Escherichia coli Adherence and Intestinal Colonization

2008 ◽  
Vol 76 (5) ◽  
pp. 1858-1865 ◽  
Author(s):  
Theresa D. Ho ◽  
Brigid M. Davis ◽  
Jennifer M. Ritchie ◽  
Matthew K. Waldor
Keyword(s):  
Escherichia Coli ◽  
Rabbit Model ◽  
Enterohemorrhagic Escherichia Coli ◽  
Growth Defect ◽  
Intestinal Colonization ◽  
Colonization Factor ◽  
Enterocyte Effacement ◽  
Type 2 Secretion

ABSTRACT Enterohemorrhagic Escherichia coli (EHEC) is a noninvasive food-borne pathogen that colonizes the distal ileum and colon. Proteins encoded in the EHEC locus of enterocyte effacement (LEE) pathogenicity island are known to contribute to this pathogen's adherence to epithelial cells and intestinal colonization. The role of non-LEE-encoded proteins in these processes is not as clear. We found that the Z2053 gene (designated adfO here), a gene located in a cryptic EHEC prophage, exhibits similarity to adherence and/or colonization factor genes found in several other enteric pathogens. An EHEC adfO mutant exhibited marked reductions in adherence to HeLa cells and in the secretion of several proteins into the supernatant. YodA, one of these secreted proteins, was found to be a substrate of the EHEC pO157-encoded type 2 secretion system (T2SS). Both the T2SS and YodA proved to be essential for EHEC adherence to cultured HeLa cell monolayers. Using an infant rabbit model of infection, we found that the adfO mutation did not affect colonization but that the colonization of an etpC (T2SS) mutant was reduced ∼5-fold. A strain deficient in YodA had a more severe colonization defect; however, this strain also exhibited a growth defect in vitro. Overall, our findings indicate that the pO157-encoded T2SS contributes to EHEC adherence and intestinal colonization and thus show that EHEC pathogenicity depends on type 2 secretion as well as type 3 secretion.

scholarly journals The Crystal Structure of a Binary Complex of two Pseudopilins: EpsI and EpsJ from the Type 2 Secretion System of Vibrio vulnificus

2008 ◽  
Vol 375 (2) ◽  
pp. 471-486 ◽  
Author(s):  
Marissa E. Yanez ◽  
Konstantin V. Korotkov ◽  
Jan Abendroth ◽  
Wim G.J. Hol
Keyword(s):  
Crystal Structure ◽  
Vibrio Vulnificus ◽  
Secretion System ◽  
Binary Complex ◽  
Type 2 Secretion

scholarly journals The three-dimensional structure of the cytoplasmic domains of EpsF from the type 2 secretion system of Vibrio cholerae

2009 ◽  
Vol 166 (3) ◽  
pp. 303-315 ◽  
Author(s):  
Jan Abendroth ◽  
Daniel D. Mitchell ◽  
Konstantin V. Korotkov ◽  
Tanya L. Johnson ◽  
Allison Kreger ◽  
...  
Keyword(s):  
Vibrio Cholerae ◽  
Three Dimensional ◽  
Secretion System ◽  
Dimensional Structure ◽  
Cytoplasmic Domains ◽  
Three Dimensional Structure ◽  
Type 2 Secretion
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