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OmpF porins of Enterobacteriaceae possess amyloidogenic properties
Author(s) -
Belousov Mikhail V.,
Kosolapova Anastasiia O.,
Sulatskaya Anna I.,
Sulatsky Maksim I.,
Antonets Kirill S.,
Nizhnikov Anton A.
Publication year - 2022
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2022.36.s1.l7850
Subject(s) - bacterial outer membrane , porin , proteases , escherichia coli , congo red , amyloid (mycology) , thioflavin , virulence , microbiology and biotechnology , biochemistry , chemistry , bacteria , biology , biophysics , enzyme , medicine , inorganic chemistry , genetics , disease , organic chemistry , adsorption , alzheimer's disease , pathology , gene
Outer membrane porins represent an important group of bacterial virulence associated proteins, whose amyloidogenic properties are actively investigated. Amyloids are protein fibrils with highly ordered beta‐sheet‐rich spatial structure and unique physicochemical properties including unusual resistance to treatment with different detergents and proteases. In prokaryotes, at least ten different functional groups of functional amyloids have been identified. Several outer membrane porins of gram‐negative bacteria were shown to adopt amyloid state. In this study, we analyzed amyloid properties of the OmpF porins of Escherichia coli and Salmonella enteritidis species which are known to be associated with the virulence and pathogenic properties of these bacteria in humans and animals. Our data show that recombinant OmpF proteins form fibrils with morphology typical for amyloids. The in vitro obtained aggregates of OmpF demonstrate resistance to treatment with cold ionic detergents and proteases. Moreover, these aggregates bind amyloid‐specific dye thioflavin T and exhibit apple‐green birefringence in polarized light upon staining with Congo Red dye. Overall, these data confirm the amyloidogenic properties of the OmpF porins of E. coli and S. enteritidis in vitro and suggest that these proteins could represent novel functional bacterial amyloids probably associated with pathogen‐host interactions.