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Volume 159, Issue Pt_12

Role of porin proteins in acquisition of transferrin iron by enteropathogens Free

Abstract

Acquisition of iron from key innate immune defence proteins such as transferrin (Tf) and lactoferrin is an important mechanism by which pathogenic bacteria obtain essential iron for growth within their host. Bacterial species that do not produce siderophores often use specific Tf-binding proteins, the best characterized being the -type Tf-binding proteins TbpA and TbpB. Previous work from our laboratory has shown that siderophore-producing enteric species such as also readily bind Tf, although no genomic evidence exists for Tbp-like Tf-binding proteins. Application of proteomic analyses and molecular mutagenesis strategies to an enteropathogenic identified the OmpA and OmpC porins as Tf-binding proteins. Mutagenesis of the or genes affected Tf binding and, furthermore, compromised the ability of the mutant to respond to growth promotion by certain catecholamine stress hormones. Evidence was also found to implicate the OmpA porin as an entry point for catecholamine stress hormones. Further proteomic analyses in other bacterial pathogens revealed wide-scale involvement of porins in Tf binding: (OmpC), and , and (OmpC and/or OmpA). This study shows that in addition to their existing housekeeping functions, the Gram-negative porin family of proteins can also act as Tf-capture proteins for those bacteria that lack the classical -type Tf-binding proteins.

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/content/journal/micro/10.1099/mic.0.071928-0
2013-12-01
2024-04-16
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Role of porin proteins in acquisition of transferrin iron by enteropathogens
Microbiology 159, 2639 (2013); https://doi.org/10.1099/mic.0.071928-0
/content/journal/micro/10.1099/mic.0.071928-0
/content/journal/micro/10.1099/mic.0.071928-0
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