PicU, a second serine protease autotransporter of uropathogenic Escherichia coli

Parham, Nick J.; Srinivasan, Usha; Desvaux, Mickaël; Foxman, Betsy; Marrs, Carl F.; Henderson, Ian R.

doi:10.1016/s0378-1097(03)00862-0

Cited by 88 publications

(107 citation statements)

References 43 publications

(86 reference statements)

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“…These data indicate that pic gene detected in the three pathogens (2,22,37) is active and that, based on their secretion features, the protein is autosecreted to the extracellular medium and thereby to the intestinal lumen during bacterial infection.…”

Section: Discussionmentioning

confidence: 78%

“…Other authors have shown that Pic does not produce cytotoxic effects on HEp-2 cells during 5 h of incubation and is unable to degrade ovine spectrin or pepsin but that is able to degrade human coagulation factor V (12). In contrast, PicU (from UPEC) degraded human spectrin as well as pepsin, coagulation factor V, and bovine submaxillary gland mucus (37). Due to these contradictory results and to the fact that pic is found in three important pathogens (EAEC, S. flexneri, and UPEC), our group sought to identify intestinal substrates for Pic.…”

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confidence: 96%

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Pic, an Autotransporter Protein Secreted by Different Pathogens in the Enterobacteriaceae Family, Is a Potent Mucus Secretagogue

et al. 2010

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A hallmark of enteroaggregative Escherichia coli (EAEC) infection is a formation of biofilm, which comprises a mucus layer with immersed bacteria in the intestines of patients. While studying the mucinolytic activity of Pic in an in vivo system, rat ileal loops, we surprisingly found that EAEC induced hypersecretion of mucus, which was accompanied by an increase in the number of mucus-containing goblet cells. Interestingly, an isogenic pic mutant (EAEC ⌬pic) was unable to cause this mucus hypersecretion. Furthermore, purified Pic was also able to induce intestinal mucus hypersecretion, and this effect was abolished when Pic was heat denatured. Site-directed mutagenesis of the serine protease catalytic residue of Pic showed that, unlike the mucinolytic activity, secretagogue activity did not depend on this catalytic serine protease motif. Other pathogens harboring the pic gene, such as Shigella flexneri and uropathogenic E. coli (UPEC), also showed results similar to those for EAEC, and construction of isogenic pic mutants of S. flexneri and UPEC confirmed this secretagogue activity. Thus, Pic mucinase is responsible for one of the pathophysiologic features of the diarrhea mediated by EAEC and the mucoid diarrhea induced by S. flexneri.

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Section: Discussionmentioning

confidence: 78%

mentioning

confidence: 96%

Pic, an Autotransporter Protein Secreted by Different Pathogens in the Enterobacteriaceae Family, Is a Potent Mucus Secretagogue

et al. 2010

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“…Phenotypes identified for Pic suggest that it is involved in the early stages of pathogenesis and most probably promotes intestinal colonization (196). Recently, a homologue, PicU (96% identity at the amino acid level), with similar functions has been characterized in uropathogenic E. coli (381). Subsequent investigations by Heimer et al (194) revealed that picU was expressed during experimental infection in the mouse model of urinary tract infection.…”

Section: Serine Protease Autotransporters Of the Enterobacteriaceaementioning

confidence: 99%

Type V Protein Secretion Pathway: the Autotransporter Story

Henderson

Navarro-Garcı́a

Desvaux

et al. 2004

Microbiol Mol Biol Rev

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795

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Gram-negative bacteria possess an outer membrane layer which constrains uptake and secretion of solutes and polypeptides. To overcome this barrier, bacteria have developed several systems for protein secretion. The type V secretion pathway encompasses the autotransporter proteins, the two-partner secretion system, and the recently described type Vc or AT-2 family of proteins. Since its discovery in the late 1980s, this family of secreted proteins has expanded continuously, due largely to the advent of the genomic age, to become the largest group of secreted proteins in gram-negative bacteria. Several of these proteins play essential roles in the pathogenesis of bacterial infections and have been characterized in detail, demonstrating a diverse array of function including the ability to condense host cell actin and to modulate apoptosis. However, most of the autotransporter proteins remain to be characterized. In light of new discoveries and controversies in this research field, this review considers the autotransporter secretion process in the context of the more general field of bacterial protein translocation and exoprotein function

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“…which, like the immunoglobulin A1 (IgA1) proteases and Hap autotransporters of Neisseria and Haemophilus spp., possess a consensus serine protease motif (19). Since the description of the first SPATE (30), a number of investigators have described SPATE proteins in the different pathotypes of E. coli and in Shigella (2,9,12,16,27). SPATE proteins possess several common features: (i) all possess an unusual extended signal sequence, (ii) the serine protease active site is reminiscent of a chymotrypsin clan protease, (iii) unlike the IgA1 proteases, none of the SPATE family has been shown to cleave IgA1, (iv) the serine protease motif of SPATE proteins does not have a role in cleavage of the passenger domain from the ␤-domain, (v) the point of cleavage of passenger domains from the ␤-domains is identical, (vi) each SPATE member is among the predominant secreted proteins of their respective pathogens, and (vii) SPATEs are associated with pathogenic strains (18).…”

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confidence: 99%

Distribution of the Serine Protease Autotransporters of the Enterobacteriaceae among Extraintestinal Clinical Isolates of Escherichia coli

et al. 2005

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Urinary tract infections continue to be among the most common extraintestinal diseases. Cystitis in women is by far the most common urinary tract infection; pyelonephritis in both sexes and prostatitis in men are more severe but less frequent complaints. Escherichia coli is by far the most common cause of urinary tract infection. It is believed that uropathogenic E. coli is adept at colonizing the urinary tract via the production of specific virulence factors. Recently, a novel virulence determinant, Vat, was described for the prototypical uropathogenic E. coli strain CFT073. Vat is a member of the SPATE (serine protease autotransporters of the Enterobacteriaceae) subfamily of the autotransporters. Previously, SPATEs have been described for all pathovars of E. coli, but until recently their presence had been noticeably absent in nonpathogenic E. coli. In this report we describe the prevalence and phylogenetic distribution of the SPATEs among uropathogenic E. coli and the ECOR collection, demonstrating an association between the presence of the SPATEs, including Vat, and uropathogenic E. coli phylogroups. In addition, we describe the distribution of SPATEs among nonpathogenic E. coli.Escherichia coli is the predominant cause of urinary tract infections (UTIs), accounting for 50% of all nosocomial urinary tract infections and 90% of infections among ambulatory patients (6). Among UTIs, cystitis in women is by far the most common, with the more severe complaints pyelonephritis and prostatitis being less frequent (34). The production of specific virulence factors is thought to be necessary for uropathogenic E. coli (UPEC) to colonize the urinary tract (6, 8). These factors include adhesins, capsule, aerobactin, toxins, and proteases, which may aid attachment to host mucosal tissues, allow evasion of immune defenses, and promote invasion of the normally sterile urinary tract and tissues (1,8,24,32). UPEC strains have a greater prevalence of virulence factors than commensal E. coli, with virulence determinants being more prevalent among strains causing invasive rather than noninvasive disease (13,22,32). However, half of all UPEC isolates possess none, or only one, of the virulence factors characterized thus far, and hence other as yet uncharacterized bacterial factors may be important in the pathogenesis of UTI (22).The genome sequence of the UPEC strain CFT073 has been completed, and this has propagated the identification of further potential virulence genes (35). Autotransporters are one category of secreted proteins implicated in the virulence of UPEC (17,18). Members of the serine protease autotransporters of the Enterobacteriaceae (SPATE) family are proteins from E. coli and Shigella spp. which, like the immunoglobulin A1 (IgA1) proteases and Hap autotransporters of Neisseria and Haemophilus spp

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PicU, a second serine protease autotransporter of uropathogenic Escherichia coli

Cited by 88 publications

References 43 publications

Pic, an Autotransporter Protein Secreted by Different Pathogens in the Enterobacteriaceae Family, Is a Potent Mucus Secretagogue

Pic, an Autotransporter Protein Secreted by Different Pathogens in the Enterobacteriaceae Family, Is a Potent Mucus Secretagogue

Type V Protein Secretion Pathway: the Autotransporter Story

Distribution of the Serine Protease Autotransporters of the Enterobacteriaceae among Extraintestinal Clinical Isolates of Escherichia coli

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