Stimulation of PrPC Retrograde Transport toward the Endoplasmic Reticulum Increases Accumulation of PrPSc in Prion-infected Cells

Béranger, Florence; Mangé, Alain; Goud, Bruno; Lehmann, Sylvain

doi:10.1074/jbc.m205110200

Cited by 104 publications

(95 citation statements)

References 40 publications

(41 reference statements)

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“…Although PrP Sc has been reported as detected on the cell surface of prion-infected immortalized neuronal cells (Goold et al, 2011;Rouvinski et al, 2014;Yamasaki et al, 2012), cell biological studies using immortalized cell lines strongly suggested that the PrP Sc formation takes place at cellular compartments along with the endocytic recycling pathway such as the endocytic recycling compartments, or those along with the endo-lysosomal pathway such as multivesicular bodies (Beranger et al, 2002;Borchelt et al, 1992;Marijanovic et al, 2009;Pimpinelli et al, 2005;Veith et al, 2009;Yamasaki et al, 2012Yamasaki et al, , 2014a. In contrast, ultrastructural analyses using brains of prion-infected mice and hamsters identified PrP Sc frequently at the plasma membranes and less frequently at synapses and compartments of the endolysosomal system (Arnold et al, 1995;Fournier et al, 2000;Godsave et al, 2008).…”

Section: Discussionmentioning

confidence: 99%

“…Earlier studies suggested that PrP Sc is generated from mature PrP C expressed on the cell surface and that the PrP Sc generation occurs at cellular compartments on the endocytotic pathway, including the cholesterol-rich membrane microdomains called lipid rafts Naslavsky et al, 1997;Vey et al, 1996). Further cell biological studies within the following decade indicated the involvement of endocytic recycling compartments and endocytic recycling pathway in PrP Sc formation (Beranger et al, 2002;Marijanovic et al, 2009;Pimpinelli et al, 2005;Veith et al, 2009;Yamasaki et al, 2012). We recently reported that after the inoculation of prions, newly generated PrP Sc appeared on the cell surface, early endosomes, and late endosomes of N2a cells (Yamasaki et al, 2014a).…”

Section: Introductionmentioning

confidence: 99%

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Comparison of abnormal isoform of prion protein in prion-infected cell lines and primary-cultured neurons by PrPSc-specific immunostaining

Tanaka

Fujiwara

Suzuki

et al. 2016

Journal of General Virology

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We established abnormal isoform of prion protein (PrP Sc )-specific double immunostaining using mAb 132, which recognizes aa 119-127 of the PrP molecule, and novel PrP Sc -specific mAb 8D5, which recognizes the N-terminal region of the PrP molecule. Using the PrP Sc -specific double immunostaining, we analysed PrP Sc in immortalized neuronal cell lines and primary cerebralneuronal cultures infected with prions. The PrP Sc -specific double immunostaining showed the existence of PrP Sc positive for both mAbs 132 and 8D5, as well as those positive only for either mAb 132 or mAb 8D5. This indicated that double immunostaining detects a greater number of PrP Sc species than single immunostaining. Double immunostaining revealed cell-type-dependent differences in PrP Sc staining patterns. In the 22 L prion strain-infected Neuro2a (N2a)-3 cells, a subclone of N2a neuroblastoma cell line, or GT1-7, a subclone of the GT1 hypothalamic neuronal cell line, granular PrP Sc stains were observed at the perinuclear regions and cytoplasm, whereas unique string-like PrP Sc stains were predominantly observed on the surface of the 22 L straininfected primary cerebral neurons. Only 14 % of PrP Sc in the 22 L strain-infected N2a-3 cells were positive for mAb 8D5, indicating that most of the PrP Sc in N2a-3 lack the N-terminal portion. In contrast, nearly half PrP Sc detected in the 22 L strain-infected primary cerebral neurons were positive for mAb 8D5, suggesting the abundance of full-length PrP Sc that possesses the Nterminal portion of PrP. Further analysis of prion-infected primary neurons using PrP Sc -specific immunostaining will reveal the neuron-specific mechanism for prion propagation.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Comparison of abnormal isoform of prion protein in prion-infected cell lines and primary-cultured neurons by PrPSc-specific immunostaining

Tanaka

Fujiwara

Suzuki

et al. 2016

Journal of General Virology

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“…7). Rab proteins are involved with different aspects of vesicular trafficking in cells by switching between GTP-and GDP-bound forms (Zerial and McBride, 2001) and can influence PrP-res formation (Beranger et al, 2002). GTP-bound Rab proteins are located on the cytoplasmic face of distinct intracellular compartments in which they regulate vesicle motility, docking, and fusion (Zerial and McBride, 2001).…”

Section: Discussionmentioning

confidence: 99%

Uptake and Neuritic Transport of Scrapie Prion Protein Coincident with Infection of Neuronal Cells

Magalhães¹,

Baron²,

Lee³

et al. 2005

J. Neurosci.

140

144

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Invasion of the nervous system and neuronal spread of infection are critical, but poorly understood, steps in the pathogenesis of transmissible spongiform encephalopathies or prion diseases. To characterize pathways for the uptake and intraneuronal trafficking of infectious, protease-resistant prion protein (PrP-res), fluorescent-labeled PrP-res was used to infect a neuronally derived murine cell line (SN56) and adult hamster cortical neurons in primary culture. Concurrent with the establishment of persistent scrapie infection, SN56 cells internalized PrP-res aggregates into vesicles positive for markers for late endosomes and/or lysosomes but not synaptic, early endocytic, or raft-derived vesicles. Internalized PrP-res was then transported along neurites to points of contact with other cells. Similar trafficking was observed with dextran, Alzheimer's A␤1-42 fibrils and noninfectious recombinant PrP fibrils, suggesting that PrP-res is internalized by a relatively nonspecific pinocytosis or transcytosis mechanism. Hamster cortical neurons were also capable of internalizing and disseminating exogenous PrP-res. Similar trafficking of exogenous PrP-res by cortical neurons cultured from the brains of PrP knock-out mice showed that uptake and neuritic transport did not require the presence of endogenous cellular PrP. These experiments visualize and characterize the initial steps associated with prion infection and transport within neuronal cells.

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“…The site of conversion of PrP C to PrP Sc has been proposed to be at the plasma membrane and/or in the endocytic compartment [45][46][47] with the requirement that PrP C and PrP Sc are attached to the same raft domain at the membrane in cell-free conversion reactions. 48 A recent study using tagged PrP C , which is able to be converted to PrP Sc , pinpointed de novo formation of PrP Sc at the plasma membrane to lipid raft-enriched domains.…”

Section: The Gpi-anchor Of Prp C and Its Role In Prion Diseasementioning

confidence: 99%

The GPI-anchoring of PrP

Puig

Altmeppen

Glatzel

2014

Prion

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Stimulation of PrPC Retrograde Transport toward the Endoplasmic Reticulum Increases Accumulation of PrPSc in Prion-infected Cells

Cited by 104 publications

References 40 publications

Comparison of abnormal isoform of prion protein in prion-infected cell lines and primary-cultured neurons by PrPSc-specific immunostaining

Comparison of abnormal isoform of prion protein in prion-infected cell lines and primary-cultured neurons by PrPSc-specific immunostaining

Uptake and Neuritic Transport of Scrapie Prion Protein Coincident with Infection of Neuronal Cells

The GPI-anchoring of PrP

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