Interaction of FkpA, a peptidyl-prolyl<i>cis</i>/<i>trans</i>isomerase with EspP autotransporter protein

Ruı́z-Pérez, Fernando; Henderson, Ian R.; Nataro, James P.

doi:10.4161/gmic.1.5.13436

Cited by 48 publications

(36 citation statements)

References 39 publications

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“…One somewhat unique feature shared by LptD and FhuA is the presence of a large, periplasmic, N-terminal domain, which is the first to emerge into the periplasm during translocation. Skp has been shown to play a role in the folding and assembly of the N-terminal, soluble passenger domain of the autotransporter IcsA in S. flexneri (27), and both Skp and FkpA have been shown to interact with the N-terminal passenger domain of EspP in E. coli (24,25,35). It is possible that Skp and FkpA play a role in assembling proteins with these soluble N-terminal domains.…”

Section: Discussionmentioning

confidence: 99%

“…It has been shown that FkpA is necessary for colicin M toxicity in vivo (32,33) and that its PPIase activity is required for this function (34). It has also been shown that FkpA interacts with high affinity with the passenger domain of the autotransporter EspP (35), and, along with DsbC, FkpA has been implicated in the folding of the nonnative passenger domain of a hybrid autotransporter protein (36).…”

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Role for Skp in LptD Assembly in Escherichia coli

et al. 2013

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The periplasmic chaperone Skp has long been implicated in the assembly of outer membrane proteins (OMPs) in Escherichia coli. It has been shown to interact with unfolded OMPs, and the simultaneous loss of Skp and the main periplasmic chaperone in E. coli, SurA, results in synthetic lethality. However, a ⌬skp mutant displays only minor OMP assembly defects, and no OMPs have been shown to require Skp for their assembly. Here, we report a role for Skp in the assembly of the essential OMP LptD. This role may be compensated for by other OMP assembly proteins; in the absence of both Skp and FkpA or Skp and BamB, LptD assembly is impaired. Overexpression of SurA does not restore LptD levels in a ⌬skp ⌬fkpA double mutant, nor does the overexpression of Skp or FkpA restore LptD levels in the ⌬surA mutant, suggesting that Skp acts in concert with SurA to efficiently assemble LptD in E. coli. Other OMPs, including LamB, are less affected in the ⌬skp ⌬fkpA and ⌬skp bamB::kan double mutants, suggesting that Skp is specifically necessary for the assembly of certain OMPs. Analysis of an OMP with a domain structure similar to that of LptD, FhuA, suggests that common structural features may determine which OMPs require Skp for their assembly.

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Section: Discussionmentioning

confidence: 99%

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Role for Skp in LptD Assembly in Escherichia coli

et al. 2013

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“…Periplasmic chaperones such as SurA also participate in the folding and insertion stages for autotransporters, as does the translocation and assembly module that spans the outer and inner membrane 14,[16][17][18] . At least some of these factors might facilitate or retard aspects of protein folding, to assist an overall coordination of the process.…”

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A mortise–tenon joint in the transmembrane domain modulates autotransporter assembly into bacterial outer membranes

et al. 2014

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Bacterial autotransporters comprise a 12-stranded membrane-embedded b-barrel domain, which must be folded in a process that entraps segments of an N-terminal passenger domain. This first stage of autotransporter folding determines whether subsequent translocation can deliver the N-terminal domain to its functional form on the bacterial cell surface. Here, paired glycine-aromatic 'mortise and tenon' motifs are shown to join neighbouring b-strands in the C-terminal barrel domain, and mutations within these motifs slow the rate and extent of passenger domain translocation to the surface of bacterial cells. In line with this, biophysical studies of the autotransporter Pet show that the conserved residues significantly quicken completion of the folding reaction and promote stability of the autotransporter barrel domain. Comparative genomics demonstrate conservation of glycine-aromatic residue pairings through evolution as a previously unrecognized feature of all autotransporter proteins.

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“…AT proteins were originally thought to possess structural properties that facilitate their independent transport across the bacterial membrane system and final routing to the cell surface (28). However, this classical view has recently been called into question, as accessory factors, such as the Bam complex (also known as the YaeT or Omp85 complex), as well as periplasmic chaperones, such as SurA, Skp, and DegP, are required for the secretion of some AT proteins (30,51,56,57,59,74). In general, AT proteins differ substantially in their passenger domain sequence, which determines the unique functional characteristics of the protein and is often associated with virulence (28).…”

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Molecular Characterization of UpaB and UpaC, Two New Autotransporter Proteins of Uropathogenic Escherichia coli CFT073

et al. 2012

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Uropathogenic Escherichia coli (UPEC) is the primary cause of urinary tract infection (UTI) in the developed world. The major factors associated with virulence of UPEC are fimbrial adhesins, which mediate specific attachment to host receptors and trigger innate host responses. Another group of adhesins is represented by the autotransporter (AT) subgroup of proteins. The genomesequenced prototype UPEC strain CFT073 contains 11 putative AT-encoding genes. In this study, we have performed a detailed molecular characterization of two closely related AT adhesins from CFT073: UpaB (c0426) and UpaC (c0478). PCR screening revealed that the upaB and upaC AT-encoding genes are common in E. coli. The upaB and upaC genes were cloned and characterized in a recombinant E. coli K-12 strain background. This revealed that they encode proteins located at the cell surface but possess different functional properties: UpaB mediates adherence to several ECM proteins, while UpaC expression is associated with increased biofilm formation. In CFT073, upaB is expressed while upaC is transcriptionally repressed by the global regulator H-NS. In competitive colonization experiments employing the mouse UTI model, CFT073 significantly outcompeted its upaB (but not upaC) isogenic mutant strain in the bladder. This attenuated phenotype was also observed in single-challenge experiments, where deletion of the upaB gene in CFT073 significantly reduced early colonization of the bladder. U rinary tract infections (UTIs) are among the most frequent human bacterial infections, with an estimated 40 to 50% of women experiencing at least one cystitis episode in their lifetime (19,34). UTI usually starts as a bladder infection (cystitis) but can develop to acute kidney infection (pyelonephritis), ultimately resulting in scaring and renal failure. UTI is also a major cause of sepsis, which has a mortality rate of 25% and results in more than 36,000 deaths per year in the United States (66). Almost all patients with an indwelling urinary catheter for 30 days or longer develop catheter-associated UTI, which accounts for approximately 40% of all hospital-acquired infections (19).Uropathogenic Escherichia coli (UPEC) is the most common etiological agent responsible for UTI, resulting in more than 80% of infections. UPEC strains possess an array of virulence factors, with no factor solely responsible for the ability to cause UTI (49). However, the ability of UPEC to colonize the urinary tract and cause disease involves the expression of adhesins (e.g., type 1 and P fimbriae), toxins (e.g., hemolysin), and iron acquisition systems that utilize siderophores (e.g., enterobactin, salmochelin, aerobactin) (36, 78). Adherence to the urinary tract epithelium enables bacteria to resist the hydrodynamic forces of urine flow, to trigger host and bacterial cell signaling pathways, and to establish infection. Among adhesins, P and type 1 fimbriae correlate strongly with uropathogenesis and mediate binding to specific receptors within the urinary tract (11,46,53,67,79,80). B...

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Interaction of FkpA, a peptidyl-prolylcis/transisomerase with EspP autotransporter protein

Cited by 48 publications

References 39 publications

Role for Skp in LptD Assembly in Escherichia coli

Role for Skp in LptD Assembly in Escherichia coli

A mortise–tenon joint in the transmembrane domain modulates autotransporter assembly into bacterial outer membranes

Molecular Characterization of UpaB and UpaC, Two New Autotransporter Proteins of Uropathogenic Escherichia coli CFT073

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