Literature DB >> 19036636

Serine protease espP subtype alpha, but not beta or gamma, of Shiga toxin-producing Escherichia coli is associated with highly pathogenic serogroups.

Abdul Basit Khan1, Asma Naim, Dorothea Orth, Katharina Grif, Mashkoor Mohsin, Rita Prager, Manfred P Dierich, Reinhard Würzner.   

Abstract

Besides Shiga toxins (Stx), Stx-producing Escherichia coli (STEC) harbour several other putative virulence factors, including the serine protease EspP. We have investigated 214 STEC strains from Austria belonging to 61 different serotypes from humans, animals, and food for the presence of this serine protease gene and have determined the espP subtypes and their association with clinical outcome. espP was detected in 121 (57%) out of 214 strains. Sixty-five of 68 strains (96%) of non-sorbitol-fermenting (NSF) O157:H7/NM (NM, non-motile) were positive for espP, while none of 8 SF E. coli O157:NM isolates contained this gene. All 9 strains of serotype O145:NM and 17 of 21 strains (81%) of serotype O26:H11/NM were positive for espP. Nineteen STEC serogroups including O103 and O111 serogroups--considered to be highly pathogenic--were completely negative for espP. Only 5 of 12 strains isolated from patients suffering from haemolytic uraemic syndrome (HUS) were espP-positive (all serogroup NSF O157) as well as 28 of 39 strains from patients with bloody diarrhoea, 40 of 63 strains from patients with non-bloody diarrhoea, and 15 of 19 strains from asymptomatic patients. In O157:H7/NM, O26:H11/NM, and O145:NM only espP subtype alpha was found, whereas in most of the other non-O157 serogroups, subtypes beta and gamma were found. Subtype delta was not detected in our strain collection. Regarding the espP subtypes, only subtype alpha, but not beta and gamma, were found in HUS patients. Moreover, we could demonstrate that espP, and in particular subtype alpha, is associated with highly pathogenic serogroups.

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Year:  2008        PMID: 19036636     DOI: 10.1016/j.ijmm.2008.08.006

Source DB:  PubMed          Journal:  Int J Med Microbiol        ISSN: 1438-4221            Impact factor:   3.473


  13 in total

1.  EspP, a serine protease of enterohemorrhagic Escherichia coli, impairs complement activation by cleaving complement factors C3/C3b and C5.

Authors:  Dorothea Orth; Silvia Ehrlenbach; Jens Brockmeyer; Abdul Basit Khan; Georg Huber; Helge Karch; Bettina Sarg; Herbert Lindner; Reinhard Würzner
Journal:  Infect Immun       Date:  2010-07-19       Impact factor: 3.441

Review 2.  Infection strategies of enteric pathogenic Escherichia coli.

Authors:  Abigail Clements; Joanna C Young; Nicholas Constantinou; Gad Frankel
Journal:  Gut Microbes       Date:  2012-03-01

3.  Structure and function relationship of the autotransport and proteolytic activity of EspP from Shiga toxin-producing Escherichia coli.

Authors:  Jens Brockmeyer; Sabrina Spelten; Thorsten Kuczius; Martina Bielaszewska; Helge Karch
Journal:  PLoS One       Date:  2009-07-01       Impact factor: 3.240

4.  Isolation of a putative virulence agent, cytotoxic serine-elastase, from a newly isolated Pseudomonas aeruginosa ZuhP13.

Authors:  Essam Kotb; Yehia A El-Zawahry; Ghadeer E Saleh
Journal:  J Biosci       Date:  2019-03       Impact factor: 1.826

Review 5.  Bacterial serine proteases secreted by the autotransporter pathway: classification, specificity, and role in virulence.

Authors:  Fernando Ruiz-Perez; James P Nataro
Journal:  Cell Mol Life Sci       Date:  2013-05-21       Impact factor: 9.261

6.  Enterohaemorrhagic Escherichia coli haemolysin is cleaved and inactivated by serine protease EspPα.

Authors:  Jens Brockmeyer; Thomas Aldick; Jens Soltwisch; Wenlan Zhang; Philip I Tarr; André Weiss; Klaus Dreisewerd; Johannes Müthing; Martina Bielaszewska; Helge Karch
Journal:  Environ Microbiol       Date:  2011-02-23       Impact factor: 5.491

Review 7.  Prevalence, biogenesis, and functionality of the serine protease autotransporter EspP.

Authors:  André Weiss; Jens Brockmeyer
Journal:  Toxins (Basel)       Date:  2012-12-28       Impact factor: 4.546

8.  Structural and functional characterization of cleavage and inactivation of human serine protease inhibitors by the bacterial SPATE protease EspPα from enterohemorrhagic E. coli.

Authors:  André Weiss; Hanna Joerss; Jens Brockmeyer
Journal:  PLoS One       Date:  2014-10-27       Impact factor: 3.240

9.  Biochemical characterization of the SPATE members EspPα and EspI.

Authors:  André Weiss; David Kortemeier; Jens Brockmeyer
Journal:  Toxins (Basel)       Date:  2014-09-16       Impact factor: 4.546

10.  EspP, an Extracellular Serine Protease from Enterohemorrhagic E. coli, Reduces Coagulation Factor Activities, Reduces Clot Strength, and Promotes Clot Lysis.

Authors:  Kevin H M Kuo; Shekeb Khan; Margaret L Rand; Hira S Mian; Elena Brnjac; Linda E Sandercock; Indira Akula; Jean-Philippe Julien; Emil F Pai; Alden E Chesney
Journal:  PLoS One       Date:  2016-03-02       Impact factor: 3.240

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