Non-specific porins of Gram-negative bacteria as proteins containing intrinsically disordered regions with amyloidogenic potential

Novikova, O. D.; Uversky, Vladimir N.; Zelepuga, Elena

doi:10.1016/bs.pmbts.2021.06.012

Cited by 5 publications

(2 citation statements)

References 46 publications

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“…The E. coli OmpA porin, which is one of the most abundant proteins in cells of Gram-negative bacteria [2], forms aggregates in vitro, demonstrating several traits of amyloids, including fibrillar morphology and binding ThT [23]. The Yersinia pseudotuberculosis OmpF porin is bioinformatically predicted to be moderately disordered and potentially amyloidogenic [56], and being overproduced at low temperatures in E. coli is present at inclusion bodies with high β-sheet content [57]. The OmpC common porin of E. coli was demonstrated to form fibrils in vitro, possessing a set of amyloid properties, including protease resistance, and birefringence, in polarized light, though the authors did not analyze whether these fibrils possess a cross-β structure specific for amyloids [24].…”

Section: Discussionmentioning

confidence: 99%

OmpC and OmpF Outer Membrane Proteins of Escherichia coli and Salmonella enterica Form Bona Fide Amyloids

Belousov,

Kosolapova,

Fayoud

et al. 2023

IJMS

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Outer membrane proteins (Omps) of Gram-negative bacteria represent porins involved in a wide range of virulence- and pathogenesis-related cellular processes, including transport, adhesion, penetration, and the colonization of host tissues. Most outer membrane porins share a specific spatial structure called the β-barrel that provides their structural integrity within the membrane lipid bilayer. Recent data suggest that outer membrane proteins from several bacterial species are able to adopt the amyloid state alternative to their β-barrel structure. Amyloids are protein fibrils with a specific spatial structure called the cross-β that gives them an unusual resistance to different physicochemical influences. Various bacterial amyloids are known to be involved in host-pathogen and host-symbiont interactions and contribute to colonization of host tissues. Such an ability of outer membrane porins to adopt amyloid state might represent an important mechanism of bacterial virulence. In this work, we investigated the amyloid properties of the OmpC and OmpF porins from two species belonging to Enterobacteriaceae family, Escherichia coli, and Salmonella enterica. We demonstrated that OmpC and OmpF of E. coli and S. enterica form toxic fibrillar aggregates in vitro. These aggregates exhibit birefringence upon binding Congo Red dye and show characteristic reflections under X-ray diffraction. Thus, we confirmed amyloid properties for OmpC of E. coli and demonstrated bona fide amyloid properties for three novel proteins: OmpC of S. enterica and OmpF of E. coli and S. enterica in vitro. All four studied porins were shown to form amyloid fibrils at the surface of E. coli cells in the curli-dependent amyloid generator system. Moreover, we found that overexpression of recombinant OmpC and OmpF in the E. coli BL21 strain leads to the formation of detergent- and protease-resistant amyloid-like aggregates and enhances the birefringence of bacterial cultures stained with Congo Red. We also detected detergent- and protease-resistant aggregates comprising OmpC and OmpF in S. enterica culture. These data are important in the context of understanding the structural dualism of Omps and its relation to pathogenesis.

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Section: Discussionmentioning

confidence: 99%

OmpC and OmpF Outer Membrane Proteins of Escherichia coli and Salmonella enterica Form Bona Fide Amyloids

Belousov,

Kosolapova,

Fayoud

et al. 2023

IJMS

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“…С помощью биоинформатических web ресурсов, таких как D 2 P 2 (http://d2p2.pro/) [2] и ODiNPred (https://stprotein.chem.au.dk/odinpred) [3] был проведен анализ первичной структуры YpOmpF и YpOmpC поринов. Проанализировано количественное содержание амилоидогенных участков в аминокислотной последовательности рассматриваемых белков и с помощью их теоретических моделей определена локализация IDPRs [4]. Обнаружено, что значительное количество IDPRs находится в области наружных петель обоих поринов, напротив, β-тяжи, образующие β-баррель, таких участков не содержат, но существенно различаются по степени своей конформационной гибкости.…”

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Study on the Amyloidoigenic Potential of Non-Specific Yersinia Pseudotuberculosis Porins

Rybinskaya

Portnyagina

Zelepuga

et al. 2022

Russian Journal of Biological Physics and Chemisrty

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The paper considers the process of formation and properties of amyloid-like aggregates of outer membrane non-specific porins (OmpC and OmpF) of the gram-negative bacterium Yersinia pseudotuberculos in an acidic medium (pH 4.5) at elevated temperature. The dynamics of the formation of amyloid-like aggregates of porins was monitored after two and four weeks of incubation (at 42 °C) and after 3-5 hours (at 90 °C) by staining the samples with amyloid-specific dye thioflavin T, analyzing the spectra of circular dichroism in the far UV region, IR -spectroscopy and confocal microscopy. It was found that in the case of porin OmpC, incubation under mild conditions (42°C) leads to a reversible accumulation of α-helical regions in the protein polypeptide chain. No significant changes are observed in the spatial structure of OmpF porin under these conditions, however, under harsh conditions (95 ºC) amyloid-like aggregates are formed, which are characterized by an increased content of the β-sheet structure. Using IR spectroscopy, it was shown that the conformational rearrangement in the molecule of OmpF porin is associated with a change in the quantity and quality of elements of the β-structure. According to confocal microscopy, the aggregates of the studied non-specific porins can be considered as intermediate products of the amyloidogenic pathway - oligomers. According to the literature data, these oligomers, which precede the formation of mature fibrils, have membranolytic and cytotoxic properties. For heated samples of the studied porins during reconstitution into bilayer lipid membranes, neither pore-forming nor membranolytic activity was detected. With respect to Neuro-2a CCL-131™ mouse neuroblastoma cells, the aggregates of OmpF and OmpC porins obtained after incubation had a higher toxicity compared to the initial protein samples.

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New insights into xenobiotic tolerance of Antarctic bacteria: transcriptomic analysis of Pseudomonas sp. TNT3 during 2,4,6-trinitrotoluene biotransformation

Cabrera,

Márquez,

Pérez-Donoso

2024

Environ Sci Pollut Res

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Non-specific porins of Gram-negative bacteria as proteins containing intrinsically disordered regions with amyloidogenic potential

Cited by 5 publications

References 46 publications

OmpC and OmpF Outer Membrane Proteins of Escherichia coli and Salmonella enterica Form Bona Fide Amyloids

OmpC and OmpF Outer Membrane Proteins of Escherichia coli and Salmonella enterica Form Bona Fide Amyloids

Study on the Amyloidoigenic Potential of Non-Specific Yersinia Pseudotuberculosis Porins

New insights into xenobiotic tolerance of Antarctic bacteria: transcriptomic analysis of Pseudomonas sp. TNT3 during 2,4,6-trinitrotoluene biotransformation

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