Interaction between coxsackievirus B3 infection and α-synuclein in models of Parkinson's disease.

Parkinson's disease (PD) is one of the most common neurodegenerative diseases. PD is pathologically characterized by the death of midbrain dopaminergic neurons and the accumulation of intracellular protein inclusions called Lewy bodies or Lewy neurites. The major component of Lewy bodies is α-s...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Soo Jin Park, Uram Jin, Sang Myun Park
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/20f60384fc2e42ffa8164e7cc13893f2
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:20f60384fc2e42ffa8164e7cc13893f2
record_format	dspace
spelling	oai:doaj.org-article:20f60384fc2e42ffa8164e7cc13893f22021-12-02T19:59:58ZInteraction between coxsackievirus B3 infection and α-synuclein in models of Parkinson's disease.1553-73661553-737410.1371/journal.ppat.1010018https://doaj.org/article/20f60384fc2e42ffa8164e7cc13893f22021-10-01T00:00:00Zhttps://doi.org/10.1371/journal.ppat.1010018https://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374Parkinson's disease (PD) is one of the most common neurodegenerative diseases. PD is pathologically characterized by the death of midbrain dopaminergic neurons and the accumulation of intracellular protein inclusions called Lewy bodies or Lewy neurites. The major component of Lewy bodies is α-synuclein (α-syn). Prion-like propagation of α-syn has emerged as a novel mechanism in the progression of PD. This mechanism has been investigated to reveal factors that initiate Lewy pathology with the aim of preventing further progression of PD. Here, we demonstrate that coxsackievirus B3 (CVB3) infection can induce α-syn-associated inclusion body formation in neurons which might act as a trigger for PD. The inclusion bodies contained clustered organelles, including damaged mitochondria with α-syn fibrils. α-Syn overexpression accelerated inclusion body formation and induced more concentric inclusion bodies. In CVB3-infected mice brains, α-syn aggregates were observed in the cell body of midbrain neurons. Additionally, α-syn overexpression favored CVB3 replication and related cytotoxicity. α-Syn transgenic mice had a low survival rate, enhanced CVB3 replication, and exhibited neuronal cell death, including that of dopaminergic neurons in the substantia nigra. These results may be attributed to distinct autophagy-related pathways engaged by CVB3 and α-syn. This study elucidated the mechanism of Lewy body formation and the pathogenesis of PD associated with CVB3 infection.Soo Jin ParkUram JinSang Myun ParkPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 17, Iss 10, p e1010018 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
spellingShingle	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 Soo Jin Park Uram Jin Sang Myun Park Interaction between coxsackievirus B3 infection and α-synuclein in models of Parkinson's disease.
description	Parkinson's disease (PD) is one of the most common neurodegenerative diseases. PD is pathologically characterized by the death of midbrain dopaminergic neurons and the accumulation of intracellular protein inclusions called Lewy bodies or Lewy neurites. The major component of Lewy bodies is α-synuclein (α-syn). Prion-like propagation of α-syn has emerged as a novel mechanism in the progression of PD. This mechanism has been investigated to reveal factors that initiate Lewy pathology with the aim of preventing further progression of PD. Here, we demonstrate that coxsackievirus B3 (CVB3) infection can induce α-syn-associated inclusion body formation in neurons which might act as a trigger for PD. The inclusion bodies contained clustered organelles, including damaged mitochondria with α-syn fibrils. α-Syn overexpression accelerated inclusion body formation and induced more concentric inclusion bodies. In CVB3-infected mice brains, α-syn aggregates were observed in the cell body of midbrain neurons. Additionally, α-syn overexpression favored CVB3 replication and related cytotoxicity. α-Syn transgenic mice had a low survival rate, enhanced CVB3 replication, and exhibited neuronal cell death, including that of dopaminergic neurons in the substantia nigra. These results may be attributed to distinct autophagy-related pathways engaged by CVB3 and α-syn. This study elucidated the mechanism of Lewy body formation and the pathogenesis of PD associated with CVB3 infection.
format	article
author	Soo Jin Park Uram Jin Sang Myun Park
author_facet	Soo Jin Park Uram Jin Sang Myun Park
author_sort	Soo Jin Park
title	Interaction between coxsackievirus B3 infection and α-synuclein in models of Parkinson's disease.
title_short	Interaction between coxsackievirus B3 infection and α-synuclein in models of Parkinson's disease.
title_full	Interaction between coxsackievirus B3 infection and α-synuclein in models of Parkinson's disease.
title_fullStr	Interaction between coxsackievirus B3 infection and α-synuclein in models of Parkinson's disease.
title_full_unstemmed	Interaction between coxsackievirus B3 infection and α-synuclein in models of Parkinson's disease.
title_sort	interaction between coxsackievirus b3 infection and α-synuclein in models of parkinson's disease.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/20f60384fc2e42ffa8164e7cc13893f2
work_keys_str_mv	AT soojinpark interactionbetweencoxsackievirusb3infectionandasynucleininmodelsofparkinsonsdisease AT uramjin interactionbetweencoxsackievirusb3infectionandasynucleininmodelsofparkinsonsdisease AT sangmyunpark interactionbetweencoxsackievirusb3infectionandasynucleininmodelsofparkinsonsdisease
_version_	1718375709109387264

Interaction between coxsackievirus B3 infection and α-synuclein in models of Parkinson's disease.

Ejemplares similares