Two Novel Amyloid Proteins, RopA and RopB, from the Root Nodule Bacterium Rhizobium leguminosarum

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Two Novel Amyloid Proteins, RopA and RopB, from the Root Nodule Bacterium Rhizobium leguminosarum. / Kosolapova, Anastasiia O.; Belousov, Mikhail V.; Sulatskaya, Anna I.; Belousova, Maria E.; Sulatsky, Maksim I.; Antonets, Kirill S.; Volkov, Kirill V.; Lykholay, Anna N.; Shtark, Oksana Y.; Vasileva, Ekaterina N.; Zhukov, Vladimir A.; Ivanova, Alexandra N.; Zykin, Pavel A.; Kuznetsova, Irina M.; Turoverov, Konstantin K.; Tikhonovich, Igor A.; Nizhnikov, Anton A.

в: Biomolecules, Том 9, № 11, 694, 04.11.2019.

Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование

Author

Kosolapova, Anastasiia O. ; Belousov, Mikhail V. ; Sulatskaya, Anna I. ; Belousova, Maria E. ; Sulatsky, Maksim I. ; Antonets, Kirill S. ; Volkov, Kirill V. ; Lykholay, Anna N. ; Shtark, Oksana Y. ; Vasileva, Ekaterina N. ; Zhukov, Vladimir A. ; Ivanova, Alexandra N. ; Zykin, Pavel A. ; Kuznetsova, Irina M. ; Turoverov, Konstantin K. ; Tikhonovich, Igor A. ; Nizhnikov, Anton A. / Two Novel Amyloid Proteins, RopA and RopB, from the Root Nodule Bacterium Rhizobium leguminosarum. в: Biomolecules. 2019 ; Том 9, № 11.

BibTeX

@article{dbf9a6a9fc8b4e3aa22e6ee298a19892,

title = "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 amyloids (PSIA), we identified amyloidogenic proteins in the proteome of the root nodule bacterium Rhizobium leguminosarum. Among 54 proteins identified, we selected two proteins, RopA and RopB, which are predicted to have β-barrel structure and are likely to be involved in the control of plant-microbial symbiosis. We demonstrated that the full-length RopA and RopB form bona fide amyloid fibrils in vitro. In particular, these fibrils are β-sheet-rich, bind Thioflavin T (ThT), exhibit green birefringence upon staining with Congo Red (CR), and resist treatment with ionic detergents and proteases. The heterologously expressed RopA and RopB intracellularly aggregate in yeast and assemble into amyloid fibrils at the surface of Escherichia coli. The capsules of the R. leguminosarum cells bind CR, exhibit green birefringence, and contain fibrils of RopA and RopB in vivo.",

keywords = "Amyloid, Bacteria, Fibril, Microbial interaction, Outer membrane protein, Plant, Porin, Rhizobium leguminosarum, Root nodule, RopA, RopB, bacteria, ALZHEIMERS-DISEASE, ESCHERICHIA-COLI, FUNCTIONAL PRION, BIOFILM, outer membrane protein, FIBRILS, THIOFLAVIN-T, plant-microbial interaction, root nodule, porin, FORMS, fibril, amyloid, GENE, AGGREGATION, YEAST PRION",

author = "Kosolapova, {Anastasiia O.} and Belousov, {Mikhail V.} and Sulatskaya, {Anna I.} and Belousova, {Maria E.} and Sulatsky, {Maksim I.} and Antonets, {Kirill S.} and Volkov, {Kirill V.} and Lykholay, {Anna N.} and Shtark, {Oksana Y.} and Vasileva, {Ekaterina N.} and Zhukov, {Vladimir A.} and Ivanova, {Alexandra N.} and Zykin, {Pavel A.} and Kuznetsova, {Irina M.} and Turoverov, {Konstantin K.} and Tikhonovich, {Igor A.} and Nizhnikov, {Anton A.}",

year = "2019",

month = nov,

day = "4",

doi = "10.3390/biom9110694",

language = "English",

volume = "9",

journal = "Biomolecules",

issn = "2218-273X",

publisher = "MDPI AG",

number = "11",

}

RIS

TY - JOUR

T1 - Two Novel Amyloid Proteins, RopA and RopB, from the Root Nodule Bacterium Rhizobium leguminosarum

AU - Kosolapova, Anastasiia O.

AU - Belousov, Mikhail V.

AU - Sulatskaya, Anna I.

AU - Belousova, Maria E.

AU - Sulatsky, Maksim I.

AU - Antonets, Kirill S.

AU - Volkov, Kirill V.

AU - Lykholay, Anna N.

AU - Shtark, Oksana Y.

AU - Vasileva, Ekaterina N.

AU - Zhukov, Vladimir A.

AU - Ivanova, Alexandra N.

AU - Zykin, Pavel A.

AU - Kuznetsova, Irina M.

AU - Turoverov, Konstantin K.

AU - Tikhonovich, Igor A.

AU - Nizhnikov, Anton A.

PY - 2019/11/4

Y1 - 2019/11/4

N2 - 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 amyloids (PSIA), we identified amyloidogenic proteins in the proteome of the root nodule bacterium Rhizobium leguminosarum. Among 54 proteins identified, we selected two proteins, RopA and RopB, which are predicted to have β-barrel structure and are likely to be involved in the control of plant-microbial symbiosis. We demonstrated that the full-length RopA and RopB form bona fide amyloid fibrils in vitro. In particular, these fibrils are β-sheet-rich, bind Thioflavin T (ThT), exhibit green birefringence upon staining with Congo Red (CR), and resist treatment with ionic detergents and proteases. The heterologously expressed RopA and RopB intracellularly aggregate in yeast and assemble into amyloid fibrils at the surface of Escherichia coli. The capsules of the R. leguminosarum cells bind CR, exhibit green birefringence, and contain fibrils of RopA and RopB in vivo.

AB - 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 amyloids (PSIA), we identified amyloidogenic proteins in the proteome of the root nodule bacterium Rhizobium leguminosarum. Among 54 proteins identified, we selected two proteins, RopA and RopB, which are predicted to have β-barrel structure and are likely to be involved in the control of plant-microbial symbiosis. We demonstrated that the full-length RopA and RopB form bona fide amyloid fibrils in vitro. In particular, these fibrils are β-sheet-rich, bind Thioflavin T (ThT), exhibit green birefringence upon staining with Congo Red (CR), and resist treatment with ionic detergents and proteases. The heterologously expressed RopA and RopB intracellularly aggregate in yeast and assemble into amyloid fibrils at the surface of Escherichia coli. The capsules of the R. leguminosarum cells bind CR, exhibit green birefringence, and contain fibrils of RopA and RopB in vivo.

KW - Amyloid

KW - Bacteria

KW - Fibril

KW - Microbial interaction

KW - Outer membrane protein

KW - Plant

KW - Porin

KW - Rhizobium leguminosarum

KW - Root nodule

KW - RopA

KW - RopB

KW - bacteria

KW - ALZHEIMERS-DISEASE

KW - ESCHERICHIA-COLI

KW - FUNCTIONAL PRION

KW - BIOFILM

KW - outer membrane protein

KW - FIBRILS

KW - THIOFLAVIN-T

KW - plant-microbial interaction

KW - root nodule

KW - porin

KW - FORMS

KW - fibril

KW - amyloid

KW - GENE

KW - AGGREGATION

KW - YEAST PRION

UR - http://www.scopus.com/inward/record.url?scp=85074495842&partnerID=8YFLogxK

UR - http://www.mendeley.com/research/two-novel-amyloid-proteins-ropa-ropb-root-nodule-bacterium-rhizobium-leguminosarum

U2 - 10.3390/biom9110694

DO - 10.3390/biom9110694

M3 - Article

C2 - 31690032

AN - SCOPUS:85074495842

VL - 9

JO - Biomolecules

JF - Biomolecules

SN - 2218-273X

IS - 11

M1 - 694

ER -

ID: 48318997