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Microbiologyopen. 2019 Sep 8:e915. doi: 10.1002/mbo3.915. [Epub ahead of print]

Identification and characterization of OmpT-like proteases in uropathogenic Escherichia coli clinical isolates.

Author information

1
Department of Microbiology and Immunology, McGill University, Montreal, QC, Canada.
2
Division of Nephrology, Nationwide Children's Hospital, Columbus, Ohio.
3
Microbiome and Disease Tolerance Centre, McGill University, Montreal, QC, Canada.
4
Department of Human Genetics, McGill University, Montreal, QC, Canada.
5
School of Population and Public Health, University of British Columbia, Vancouver, BC, Canada.
6
Faculty of Dentistry, McGill University, Montreal, QC, Canada.

Abstract

Bacterial colonization of the urogenital tract is limited by innate defenses, including the production of antimicrobial peptides (AMPs). Uropathogenic Escherichia coli (UPEC) resist AMP-killing to cause a range of urinary tract infections (UTIs) including asymptomatic bacteriuria, cystitis, pyelonephritis, and sepsis. UPEC strains have high genomic diversity and encode numerous virulence factors that differentiate them from non-UTI-causing strains, including ompT. As OmpT homologs cleave and inactivate AMPs, we hypothesized that UPEC strains from patients with symptomatic UTIs have high OmpT protease activity. Therefore, we measured OmpT activity in 58 clinical E. coli isolates. While heterogeneous OmpT activities were observed, OmpT activity was significantly greater in UPEC strains isolated from patients with symptomatic infections. Unexpectedly, UPEC strains exhibiting the greatest protease activities harbored an additional ompT-like gene called arlC (ompTp). The presence of two OmpT-like proteases in some UPEC isolates led us to compare the substrate specificities of OmpT-like proteases found in E. coli. While all three cleaved AMPs, cleavage efficiency varied on the basis of AMP size and secondary structure. Our findings suggest the presence of ArlC and OmpT in the same UPEC isolate may confer a fitness advantage by expanding the range of target substrates.

KEYWORDS:

ArlC; LL-37; OmpP; OmpT; RNase 7; UPEC; antimicrobial peptides

PMID:
31496120
DOI:
10.1002/mbo3.915
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