Binding of bovine prion protein to heparin: A fluorescence polarization study

Andrievskaia, Olga; Potetinova, Zhanna; Balachandran, Aru; Nielsen, Klaus

doi:10.1016/j.abb.2007.02.001

Cited by 20 publications

(26 citation statements)

References 34 publications

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“…Furthermore, our results showed that the abilities of CSA, CSB, and CSC to stimulate Bac-PrP Sc conversion differed according to prion strains; therefore, this strain-dependent difference in CS ability to promote PrP C conversion to PrP Sc might represent one of the underlying causes of strain-specific differences in neuropathology. The binding of HP and HS has been reported to increase the thermal stability, ␤-sheet structure, or PK resistance of recPrP (12,47,48) and alter the solubility of recPrP (38); these findings suggest that PrP C binding to HS and HP induces a conformational change in PrP C . Therefore, Bac-PrP binding to HP and HS might also induce a conformational change in Bac-PrP and contribute to the conversion of Bac-PrP into Bac-PrP Sc .…”

Section: Inoculummentioning

confidence: 73%

Heparan Sulfate and Heparin Promote Faithful Prion Replication in Vitro by Binding to Normal and Abnormal Prion Proteins in Protein Misfolding Cyclic Amplification

Imamura

Tabeta

Kato

et al. 2016

Journal of Biological Chemistry

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Edited by Paul FraserThe precise mechanism underlying the conversion of normal prion protein ( Sc by using a modified PMCA performed with baculovirusderived recombinant PrP (Bac-PrP) as a substrate. The addition of heparan sulfate (HS) or its analog heparin (HP) restored the conversion efficiency in PMCA that was inhibited through nucleic acid depletion. Moreover, the PMCA products obtained under these conditions were infectious and preserved the properties of the input PrP Sc . These data suggest that HS and HP play the same role as nucleic acids in facilitating faithful replication of prions in PMCA. Furthermore, we showed that HP binds to both Bac-PrP and Bac-PrP Sc through the sulfated groups present on HP and that the N-terminal domain of Bac-PrP Sc might potentially not be involved in the binding to HP. These results suggest that the interaction of GAGs such as HS and HP with PrP C and/or PrP Sc through their sulfate groups is critical for the faithful replication of prions.

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Section: Inoculummentioning

confidence: 73%

Heparan Sulfate and Heparin Promote Faithful Prion Replication in Vitro by Binding to Normal and Abnormal Prion Proteins in Protein Misfolding Cyclic Amplification

Imamura

Tabeta

Kato

et al. 2016

Journal of Biological Chemistry

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“…The octapeptide repeat exhibits binding ability to metal ions, particularly Cu 2þ , which affects the configuration of the flexible N-terminal region [36]. Previous studies have demonstrated PrP interaction with heparin in a Cu 2þ -enhanced fashion [16,37] or a Cu 2þ -weakened fashion [17,38]. However, Pan et al [16] have found that an octapeptide repeat-deleted mutant PrP also binds heparin.…”

Section: Discussionmentioning

confidence: 92%

Heparinase I-specific disaccharide unit of heparin is a key structure but insufficient for exerting anti-prion activity in prion-infected cells

Teruya

Wakao

Satō

et al. 2015

Biochemical and Biophysical Research Communications

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“…Copper binding to the octameric repeat domain alters GAG binding (Andrievskaia et al, 2007;Warner et al, 2002). Increased octarepeats, as seen in some genetic prion diseases, increases the binding capacity and affinity for GAGs, and both increased repeats and increased GAG binding decrease the ability of the cell to respond to ROS (Yin et al, 2006;Yin et al, 2007).…”

Section: Journal Of Cell Science 122 (10)mentioning

confidence: 99%

“…PrP C has several putative GAG-binding sites that might differentially mediate binding to proteoglycans, which are located at amino acid positions PrP23-50, 53-93 and 110-128 (Warner et al, 2002). The GAGs bound by cell-free recombinant PrP include heparin, heparan sulphate, chondroitin sulphate A and B, hyaluronic acid and dextran (Andrievskaia et al, 2007;Pan et al, 2002), and cellular PrP expressed by transfection binds heparin (Pan et al, 2002). Heparan sulphate has been shown to be a cell surface receptor for PrP Sc (Horonchik et al, 2005) and preincubation of infectious…”

Section: Journal Of Cell Science 122 (10)mentioning

confidence: 99%

Dominant roles of the polybasic proline motif and copper in the PrP23-89-mediated stress protection response

Haigh

Drew

Boland

et al. 2009

Journal of Cell Science

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Beta-cleavage of the neurodegenerative disease-associated prion protein (PrP) protects cells from death induced by oxidative insults. The beta-cleavage event produces two fragments, designated N2 and C2. We investigated the role of the N2 fragment (residues 23-89) in cellular stress response, determining mechanisms involved and regions important for this reaction. The N2 fragment differentially modulated the reactive oxygen species (ROS) response induced by serum deprivation, with amelioration when copper bound. Amino acid residues 23-50 alone mediated a ROS reduction response. PrP23-50 ROS reduction was not due to copper binding or direct antioxidant activity, but was instead mediated through proteoglycan binding partners localised in or interacting with cholesterol-rich membrane domains. Furthermore, mutational analyses of both PrP23-50 and N2 showed that their protective capacity requires the sterically constraining double proline motif within the N-terminal polybasic region. Our findings show that N2 is a biologically active fragment that is able to modulate stress-induced intracellular ROS through interaction of its structurally defined N-terminal polybasic region with cell-surface proteoglycans.

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Binding of bovine prion protein to heparin: A fluorescence polarization study

Cited by 20 publications

References 34 publications

Heparan Sulfate and Heparin Promote Faithful Prion Replication in Vitro by Binding to Normal and Abnormal Prion Proteins in Protein Misfolding Cyclic Amplification

Heparan Sulfate and Heparin Promote Faithful Prion Replication in Vitro by Binding to Normal and Abnormal Prion Proteins in Protein Misfolding Cyclic Amplification

Heparinase I-specific disaccharide unit of heparin is a key structure but insufficient for exerting anti-prion activity in prion-infected cells

Dominant roles of the polybasic proline motif and copper in the PrP23-89-mediated stress protection response

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