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α-Synuclein seeding activity in duodenum biopsies from Parkinson’s disease patients

Vascellari, Sarah ; Orrù, Christina D. ; Groveman, Bradley R. ; [et al.]

Public Library of Science (PLoS) ; 2023

In: PLOS Pathogens Vol. 19, No. 6 ( 2023-6-30), p. e1011456-

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In: PLOS Pathogens, Public Library of Science (PLoS), Vol. 19, No. 6 ( 2023-6-30), p. e1011456-

Abstract: Abnormal deposition of α-synuclein is a key feature and biomarker of Parkinson’s disease. α-Synuclein aggregates can propagate themselves by a prion-like seeding-based mechanism within and between tissues and are hypothesized to move between the intestine and brain. α-Synuclein RT-QuIC seed amplification assays have detected Parkinson’s-associated α-synuclein in multiple biospecimens including post-mortem colon samples. Here we show intra vitam detection of seeds in duodenum biopsies from 22/23 Parkinson’s patients, but not in 6 healthy controls by RT-QuICR. In contrast, no tau seeding activity was detected in any of the biopsies. Our seed amplifications provide evidence that the upper intestine contains a form(s) of α-synuclein with self-propagating activity. The diagnostic sensitivity and specificity for PD in this biopsy panel were 95.7% and 100% respectively. End-point dilution analysis indicated up to 10 6 SD 50 seeding units per mg of tissue with positivity in two contemporaneous biopsies from individual patients suggesting widespread distribution within the superior and descending parts of duodenum. Our detection of α-synuclein seeding activity in duodenum biopsies of Parkinson’s disease patients suggests not only that such analyses may be useful in ante-mortem diagnosis, but also that the duodenum may be a source or a destination for pathological, self-propagating α-synuclein assemblies.

Type of Medium: Online Resource

ISSN: 1553-7374

URL: Article

DOI: 10.1371/journal.ppat.1011456

DOI: 10.1371/journal.ppat.1011456.g001

DOI: 10.1371/journal.ppat.1011456.g002

DOI: 10.1371/journal.ppat.1011456.g003

DOI: 10.1371/journal.ppat.1011456.g004

DOI: 10.1371/journal.ppat.1011456.g005

DOI: 10.1371/journal.ppat.1011456.g006

DOI: 10.1371/journal.ppat.1011456.g007

DOI: 10.1371/journal.ppat.1011456.t001

DOI: 10.1371/journal.ppat.1011456.t002

DOI: 10.1371/journal.ppat.1011456.s001

DOI: 10.1371/journal.ppat.1011456.s002

DOI: 10.1371/journal.ppat.1011456.s003

DOI: 10.1371/journal.ppat.1011456.s004

DOI: 10.1371/journal.ppat.1011456.s005

DOI: 10.1371/journal.ppat.1011456.r001

DOI: 10.1371/journal.ppat.1011456.r002

DOI: 10.1371/journal.ppat.1011456.r003

DOI: 10.1371/journal.ppat.1011456.r004

Language: English

Publisher: Public Library of Science (PLoS)

Publication Date: 2023

detail.hit.zdb_id: 2205412-1

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Consequences of variability in α-synuclein fibril structure on strain biology

Holec, Sara A. M. ; Liu, Samantha L. ; Woerman, Amanda L.

Springer Science and Business Media LLC ; 2022

In: Acta Neuropathologica Vol. 143, No. 3 ( 2022-03), p. 311-330

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In: Acta Neuropathologica, Springer Science and Business Media LLC, Vol. 143, No. 3 ( 2022-03), p. 311-330

Type of Medium: Online Resource

ISSN: 0001-6322 , 1432-0533

URL: Article

DOI: 10.1007/s00401-022-02403-w

RVK:

XA 10000

Language: English

Publisher: Springer Science and Business Media LLC

Publication Date: 2022

detail.hit.zdb_id: 1458410-4

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Tau interactome analyses in CRISPR-Cas9 engineered neuronal cells reveal ATPase-dependent binding of wild-type but not P301L Tau to non-muscle myosins

Wang, Xinzhu ; Williams, Declan ; Müller, Iris ; [et al.]

Springer Science and Business Media LLC ; 2019

In: Scientific Reports Vol. 9, No. 1 ( 2019-11-07)

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In: Scientific Reports, Springer Science and Business Media LLC, Vol. 9, No. 1 ( 2019-11-07)

Abstract: Protein interactions of Tau are of interest in efforts to decipher pathogenesis in Alzheimer’s disease, a subset of frontotemporal dementias, and other tauopathies. We CRISPR-Cas9 edited two human cell lines to generate broadly adaptable models for neurodegeneration research. We applied the system to inducibly express balanced levels of 3-repeat and 4-repeat wild-type or P301L mutant Tau. Following 12-h induction, quantitative mass spectrometry revealed the Parkinson’s disease-causing protein DJ-1 and non-muscle myosins as Tau interactors whose binding to Tau was profoundly influenced by the presence or absence of the P301L mutation. The presence of wild-type Tau stabilized non-muscle myosins at higher steady-state levels. Strikingly, in human differentiated co-cultures of neuronal and glial cells, the preferential interaction of non-muscle myosins to wild-type Tau depended on myosin ATPase activity. Consistently, transgenic P301L Tau mice exhibited reduced phosphorylation of regulatory myosin light chains known to activate this ATPase. The direct link of Tau to non-muscle myosins corroborates independently proposed roles of Tau in maintaining dendritic spines and mitochondrial fission biology, two subcellular niches affected early in tauopathies.

Type of Medium: Online Resource

ISSN: 2045-2322

URL: Article

DOI: 10.1038/s41598-019-52543-5

Language: English

Publisher: Springer Science and Business Media LLC

Publication Date: 2019

detail.hit.zdb_id: 2615211-3

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Cryo-EM of prion strains from the same genotype of host identifies conformational determinants

Hoyt, Forrest ; Alam, Parvez ; Artikis, Efrosini ; [et al.]

Public Library of Science (PLoS) ; 2022

In: PLOS Pathogens Vol. 18, No. 11 ( 2022-11-7), p. e1010947-

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In: PLOS Pathogens, Public Library of Science (PLoS), Vol. 18, No. 11 ( 2022-11-7), p. e1010947-

Abstract: Prion strains in a given type of mammalian host are distinguished by differences in clinical presentation, neuropathological lesions, survival time, and characteristics of the infecting prion protein (PrP) assemblies. Near-atomic structures of prions from two host species with different PrP sequences have been determined but comparisons of distinct prion strains of the same amino acid sequence are needed to identify purely conformational determinants of prion strain characteristics. Here we report a 3.2 Å resolution cryogenic electron microscopy-based structure of the 22L prion strain purified from the brains of mice engineered to express only PrP lacking glycophosphatidylinositol anchors [anchorless (a) 22L]. Comparison of this near-atomic structure to our recently determined structure of the aRML strain propagated in the same inbred mouse reveals that these two mouse prion strains have distinct conformational templates for growth via incorporation of PrP molecules of the same sequence. Both a22L and aRML are assembled as stacks of PrP molecules forming parallel in-register intermolecular β-sheets and intervening loops, with single monomers spanning the ordered fibril core. Each monomer shares an N-terminal steric zipper, three major arches, and an overall V-shape, but the details of these and other conformational features differ markedly. Thus, variations in shared conf ormational motifs within a parallel in-register β-stack fibril architecture provide a structural basis for prion strain differentiation within a single host genotype.

Type of Medium: Online Resource

ISSN: 1553-7374

URL: Article

DOI: 10.1371/journal.ppat.1010947

DOI: 10.1371/journal.ppat.1010947.g001

DOI: 10.1371/journal.ppat.1010947.g002

DOI: 10.1371/journal.ppat.1010947.g003

DOI: 10.1371/journal.ppat.1010947.g004

DOI: 10.1371/journal.ppat.1010947.g005

DOI: 10.1371/journal.ppat.1010947.g006

DOI: 10.1371/journal.ppat.1010947.t001

DOI: 10.1371/journal.ppat.1010947.s001

DOI: 10.1371/journal.ppat.1010947.s002

DOI: 10.1371/journal.ppat.1010947.s003

DOI: 10.1371/journal.ppat.1010947.r001

DOI: 10.1371/journal.ppat.1010947.r002

DOI: 10.1371/journal.ppat.1010947.r003

DOI: 10.1371/journal.ppat.1010947.r004

Language: English

Publisher: Public Library of Science (PLoS)

Publication Date: 2022

detail.hit.zdb_id: 2205412-1

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Multiple system atrophy prions retain strain specificity after serial propagation in two different Tg(SNCA*A53T) mouse lines

Woerman, Amanda L. ; Oehler, Abby ; Kazmi, Sabeen A. ; [et al.]

Springer Science and Business Media LLC ; 2019

In: Acta Neuropathologica Vol. 137, No. 3 ( 2019-3), p. 437-454

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In: Acta Neuropathologica, Springer Science and Business Media LLC, Vol. 137, No. 3 ( 2019-3), p. 437-454

Type of Medium: Online Resource

ISSN: 0001-6322 , 1432-0533

URL: Article

DOI: 10.1007/s00401-019-01959-4

RVK:

XA 10000

Language: English

Publisher: Springer Science and Business Media LLC

Publication Date: 2019

detail.hit.zdb_id: 1458410-4

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Multiple system atrophy prions transmit neurological disease to mice expressing wild-type human α-synuclein

Holec, Sara A. M. ; Lee, Jisoo ; Oehler, Abby ; [et al.]

Springer Science and Business Media LLC ; 2022

In: Acta Neuropathologica Vol. 144, No. 4 ( 2022-10), p. 677-690

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In: Acta Neuropathologica, Springer Science and Business Media LLC, Vol. 144, No. 4 ( 2022-10), p. 677-690

Type of Medium: Online Resource

ISSN: 0001-6322 , 1432-0533

URL: Article

DOI: 10.1007/s00401-022-02476-7

RVK:

XA 10000

Language: English

Publisher: Springer Science and Business Media LLC

Publication Date: 2022

detail.hit.zdb_id: 1458410-4

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P4‐233: AGED ALZHEIMER'S DISEASE BRAINS EXHIBIT NUMEROUS Aβ BUT ONLY FEW TAU PRIONS

Condello, Carlo ; Aoyagi, Atsushi ; Stöhr, Jan ; [et al.]

Wiley ; 2018

In: Alzheimer's & Dementia Vol. 14, No. 7S_Part_29 ( 2018-07)

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In: Alzheimer's & Dementia, Wiley, Vol. 14, No. 7S_Part_29 ( 2018-07)

Type of Medium: Online Resource

ISSN: 1552-5260 , 1552-5279

URL: Article

DOI: 10.1016/j.jalz.2018.07.054

Language: English

Publisher: Wiley

Publication Date: 2018

detail.hit.zdb_id: 2201940-6

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Kinetics of Human Mutant Tau Prion Formation in the Brains of 2 Transgenic Mouse Lines

Woerman, Amanda L. ; Patel, Smita ; Kazmi, Sabeen A. ; [et al.]

American Medical Association (AMA) ; 2017

In: JAMA Neurology Vol. 74, No. 12 ( 2017-12-01), p. 1464-

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In: JAMA Neurology, American Medical Association (AMA), Vol. 74, No. 12 ( 2017-12-01), p. 1464-

Type of Medium: Online Resource

ISSN: 2168-6149

URL: Article

DOI: 10.1001/jamaneurol.2017.2822

Language: English

Publisher: American Medical Association (AMA)

Publication Date: 2017

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α-Synuclein: Multiple System Atrophy Prions

Woerman, Amanda L. ; Watts, Joel C. ; Aoyagi, Atsushi ; [et al.]

Cold Spring Harbor Laboratory ; 2018

In: Cold Spring Harbor Perspectives in Medicine Vol. 8, No. 7 ( 2018-07), p. a024588-

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In: Cold Spring Harbor Perspectives in Medicine, Cold Spring Harbor Laboratory, Vol. 8, No. 7 ( 2018-07), p. a024588-

Type of Medium: Online Resource

ISSN: 2157-1422

URL: Article

DOI: 10.1101/cshperspect.a024588

Language: English

Publisher: Cold Spring Harbor Laboratory

Publication Date: 2018

detail.hit.zdb_id: 2628603-8

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Kinetics of α-synuclein prions preceding neuropathological inclusions in multiple system atrophy

Woerman, Amanda L. ; Patel, Smita ; Kazmi, Sabeen A. ; [et al.]

Public Library of Science (PLoS) ; 2020

In: PLOS Pathogens Vol. 16, No. 2 ( 2020-2-4), p. e1008222-

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In: PLOS Pathogens, Public Library of Science (PLoS), Vol. 16, No. 2 ( 2020-2-4), p. e1008222-

Type of Medium: Online Resource

ISSN: 1553-7374

URL: Article

DOI: 10.1371/journal.ppat.1008222

DOI: 10.1371/journal.ppat.1008222.g001

DOI: 10.1371/journal.ppat.1008222.g002

DOI: 10.1371/journal.ppat.1008222.g003

DOI: 10.1371/journal.ppat.1008222.g004

DOI: 10.1371/journal.ppat.1008222.g005

DOI: 10.1371/journal.ppat.1008222.g006

DOI: 10.1371/journal.ppat.1008222.g007

DOI: 10.1371/journal.ppat.1008222.s001

DOI: 10.1371/journal.ppat.1008222.s002

DOI: 10.1371/journal.ppat.1008222.s003

DOI: 10.1371/journal.ppat.1008222.s004

DOI: 10.1371/journal.ppat.1008222.s005

DOI: 10.1371/journal.ppat.1008222.s006

DOI: 10.1371/journal.ppat.1008222.s007

Language: English

Publisher: Public Library of Science (PLoS)

Publication Date: 2020

detail.hit.zdb_id: 2205412-1

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