2019
DOI: 10.3390/biom9110694
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Two Novel Amyloid Proteins, RopA and RopB, from the Root Nodule Bacterium Rhizobium leguminosarum

Abstract: Amyloids represent protein fibrils with a highly ordered spatial structure, which not only cause dozens of incurable human and animal diseases but also play vital biological roles in Archaea, Bacteria, and Eukarya. Despite the fact that association of bacterial amyloids with microbial pathogenesis and infectious diseases is well known, there is a lack of information concerning the amyloids of symbiotic bacteria. In this study, using the previously developed proteomic method for screening and identification of … Show more

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Cited by 29 publications
(47 citation statements)
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References 95 publications
(128 reference statements)
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“…The best results have been obtained by the usage of 1,1,1,3,3,3-Hexafluoro-2-propanol (HFIP) solvent at 37˚C for the proteins dissolution with its subsequent removal from the sample and incubation of dissolved proteins in the distilled water ( Fig 1B, row 4). Similar conditions have been used previously in other works to obtain amyloid fibrils of human amyloid-beta peptide (Aβ) [33] and RopA and RopB proteins of the bacterium Rhizobium leguminosarum [34].…”
Section: Recombinant Vicilin and Its Domains Cupin-11 And Cupin-12mentioning
confidence: 96%
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“…The best results have been obtained by the usage of 1,1,1,3,3,3-Hexafluoro-2-propanol (HFIP) solvent at 37˚C for the proteins dissolution with its subsequent removal from the sample and incubation of dissolved proteins in the distilled water ( Fig 1B, row 4). Similar conditions have been used previously in other works to obtain amyloid fibrils of human amyloid-beta peptide (Aβ) [33] and RopA and RopB proteins of the bacterium Rhizobium leguminosarum [34].…”
Section: Recombinant Vicilin and Its Domains Cupin-11 And Cupin-12mentioning
confidence: 96%
“…Notably, being structurally similar to Cupins, β-barrel domain-containing proteins that belong to the outer membrane proteins (Omps) of Gram-negative bacteria also form amyloids [34,70,71] whereas human Aβ (1-42 aa) vice versa forms β-barrel pores in specific conditions [72]. In addition, recently, formation of β-barrel oligomer intermediates has been proposed as a common step in general mechanism of amyloid formation [73].…”
Section: Plos Biologymentioning
confidence: 99%
“…In vitro, RopA and RopB form fibrillar aggregates exhibiting typical physicochemical properties of amyloids including green birefringence in polarized light upon CR staining, binding of ThT, resistance to proteases and ionic detergents treatment. In vivo, RopA and RopB form extracellular amyloid fibrils after the prolonged incubation of R. leguminosarum cells on the cultural media [ 40 ]. Moreover, the amount and size of the aggregates formed by RopA protein after induction of the nodulation process in free-living culture is increased after flavonoid treatment [ 40 ].…”
Section: Amyloids Of the Outer Membrane Proteins And Their Probablmentioning
confidence: 99%
“…In vivo, RopA and RopB form extracellular amyloid fibrils after the prolonged incubation of R. leguminosarum cells on the cultural media [ 40 ]. Moreover, the amount and size of the aggregates formed by RopA protein after induction of the nodulation process in free-living culture is increased after flavonoid treatment [ 40 ]. Based on these observations, RopA and RopB hypothetically act as adhesins and represent a part of the EPS of biofilms formed by R. leguminosarum on different surfaces including the plant roots, thus participating in colonization of plant by bacteria cells.…”
Section: Amyloids Of the Outer Membrane Proteins And Their Probablmentioning
confidence: 99%
See 1 more Smart Citation