α2,3 linkage of sialic acid to a GPI anchor and an unpredicted GPI attachment site in human prion protein
Prion diseases are transmissible, lethal neurodegenerative disorders caused by accumulation of the aggregated scrapie form of the prion protein (PrPSc) after conversion of the cellular prion protein (PrPC). The glycosylphosphatidylinositol (GPI) anchor of PrPC is involved in prion disease pathogenes...
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Published in | The Journal of biological chemistry Vol. 295; no. 22; pp. 7789 - 7798 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
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United States
Elsevier Inc
29.05.2020
American Society for Biochemistry and Molecular Biology |
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Abstract | Prion diseases are transmissible, lethal neurodegenerative disorders caused by accumulation of the aggregated scrapie form of the prion protein (PrPSc) after conversion of the cellular prion protein (PrPC). The glycosylphosphatidylinositol (GPI) anchor of PrPC is involved in prion disease pathogenesis, and especially sialic acid in a GPI side chain reportedly affects PrPC conversion. Thus, it is important to define the location and structure of the GPI anchor in human PrPC. Moreover, the sialic acid linkage type in the GPI side chain has not been determined for any GPI-anchored protein. Here we report GPI glycan structures of human PrPC isolated from human brains and from brains of a knock-in mouse model in which the mouse prion protein (Prnp) gene was replaced with the human PRNP gene. LC–electrospray ionization–MS analysis of human PrPC from both biological sources indicated that Gly229 is the ω site in PrPC to which GPI is attached. Gly229 in human PrPC does not correspond to Ser231, the previously reported ω site of Syrian hamster PrPC. We found that ∼41% and 28% of GPI anchors in human PrPCs from human and knock-in mouse brains, respectively, have N-acetylneuraminic acid in the side chain. Using a sialic acid linkage-specific alkylamidation method to discriminate α2,3 linkage from α2,6 linkage, we found that N-acetylneuraminic acid in PrPC's GPI side chain is linked to galactose through an α2,3 linkage. In summary, we report the GPI glycan structure of human PrPC, including the ω-site amino acid for GPI attachment and the sialic acid linkage type. |
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AbstractList | Prion diseases are transmissible, lethal neurodegenerative disorders caused by accumulation of the aggregated scrapie form of the prion protein (PrP
) after conversion of the cellular prion protein (PrP
). The glycosylphosphatidylinositol (GPI) anchor of PrP
is involved in prion disease pathogenesis, and especially sialic acid in a GPI side chain reportedly affects PrP
conversion. Thus, it is important to define the location and structure of the GPI anchor in human PrP
Moreover, the sialic acid linkage type in the GPI side chain has not been determined for any GPI-anchored protein. Here we report GPI glycan structures of human PrP
isolated from human brains and from brains of a knock-in mouse model in which the mouse prion protein (
) gene was replaced with the human
gene. LC-electrospray ionization-MS analysis of human PrP
from both biological sources indicated that Gly
is the ω site in PrP
to which GPI is attached. Gly
in human PrP
does not correspond to Ser
, the previously reported ω site of Syrian hamster PrP
We found that ∼41% and 28% of GPI anchors in human PrP
s from human and knock-in mouse brains, respectively, have
-acetylneuraminic acid in the side chain. Using a sialic acid linkage-specific alkylamidation method to discriminate α2,3 linkage from α2,6 linkage, we found that
-acetylneuraminic acid in PrP
's GPI side chain is linked to galactose through an α2,3 linkage. In summary, we report the GPI glycan structure of human PrP
, including the ω-site amino acid for GPI attachment and the sialic acid linkage type. Prion diseases are transmissible, lethal neurodegenerative disorders caused by accumulation of the aggregated scrapie form of the prion protein (PrP Sc ) after conversion of the cellular prion protein (PrP C ). The glycosylphosphatidylinositol (GPI) anchor of PrP C is involved in prion disease pathogenesis, and especially sialic acid in a GPI side chain reportedly affects PrP C conversion. Thus, it is important to define the location and structure of the GPI anchor in human PrP C . Moreover, the sialic acid linkage type in the GPI side chain has not been determined for any GPI-anchored protein. Here we report GPI glycan structures of human PrP C isolated from human brains and from brains of a knock-in mouse model in which the mouse prion protein ( Prnp ) gene was replaced with the human PRNP gene. LC–electrospray ionization–MS analysis of human PrP C from both biological sources indicated that Gly 229 is the ω site in PrP C to which GPI is attached. Gly 229 in human PrP C does not correspond to Ser 231 , the previously reported ω site of Syrian hamster PrP C . We found that ∼41% and 28% of GPI anchors in human PrP C s from human and knock-in mouse brains, respectively, have N -acetylneuraminic acid in the side chain. Using a sialic acid linkage-specific alkylamidation method to discriminate α2,3 linkage from α2,6 linkage, we found that N -acetylneuraminic acid in PrP C 's GPI side chain is linked to galactose through an α2,3 linkage. In summary, we report the GPI glycan structure of human PrP C , including the ω-site amino acid for GPI attachment and the sialic acid linkage type. Prion diseases are transmissible, lethal neurodegenerative disorders caused by accumulation of the aggregated scrapie form of the prion protein (PrPSc) after conversion of the cellular prion protein (PrPC). The glycosylphosphatidylinositol (GPI) anchor of PrPC is involved in prion disease pathogenesis, and especially sialic acid in a GPI side chain reportedly affects PrPC conversion. Thus, it is important to define the location and structure of the GPI anchor in human PrPC. Moreover, the sialic acid linkage type in the GPI side chain has not been determined for any GPI-anchored protein. Here we report GPI glycan structures of human PrPC isolated from human brains and from brains of a knock-in mouse model in which the mouse prion protein (Prnp) gene was replaced with the human PRNP gene. LC–electrospray ionization–MS analysis of human PrPC from both biological sources indicated that Gly229 is the ω site in PrPC to which GPI is attached. Gly229 in human PrPC does not correspond to Ser231, the previously reported ω site of Syrian hamster PrPC. We found that ∼41% and 28% of GPI anchors in human PrPCs from human and knock-in mouse brains, respectively, have N-acetylneuraminic acid in the side chain. Using a sialic acid linkage-specific alkylamidation method to discriminate α2,3 linkage from α2,6 linkage, we found that N-acetylneuraminic acid in PrPC's GPI side chain is linked to galactose through an α2,3 linkage. In summary, we report the GPI glycan structure of human PrPC, including the ω-site amino acid for GPI attachment and the sialic acid linkage type. |
Author | Kinoshita, Taroh Nishikaze, Takashi Takada, Yoko Ninomiya, Akinori Kobayashi, Atsushi Maki, Yuta Hirata, Tetsuya Kitamoto, Tetsuyuki |
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Keywords | sialic acid MS neurodegeneration glycosylphosphatidylinositol (GPI) glycosylation prion scrapie Creutzfeldt–Jakob disease |
Language | English |
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Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 These authors contributed equally to this work. Present address for Tetsuya Hirata: Center for Highly Advanced Integration of Nano and Life Sciences (G-CHAIN), Gifu University, Gifu, Japan. Edited by Gerald W. Hart |
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Snippet | Prion diseases are transmissible, lethal neurodegenerative disorders caused by accumulation of the aggregated scrapie form of the prion protein (PrPSc) after... Prion diseases are transmissible, lethal neurodegenerative disorders caused by accumulation of the aggregated scrapie form of the prion protein (PrP ) after... Prion diseases are transmissible, lethal neurodegenerative disorders caused by accumulation of the aggregated scrapie form of the prion protein (PrP Sc ) after... |
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SubjectTerms | Animals Carbohydrate Conformation Creutzfeldt–Jakob disease Glycobiology and Extracellular Matrices glycosylation glycosylphosphatidylinositol (GPI) Glycosylphosphatidylinositols - chemistry Glycosylphosphatidylinositols - genetics Glycosylphosphatidylinositols - metabolism Humans Male Mesocricetus Mice Mice, Knockout N-Acetylneuraminic Acid - chemistry N-Acetylneuraminic Acid - genetics N-Acetylneuraminic Acid - metabolism neurodegeneration prion Prion Diseases - genetics Prion Diseases - metabolism Prion Diseases - pathology Prion Proteins - chemistry Prion Proteins - genetics Prion Proteins - metabolism PrPC Proteins - chemistry PrPC Proteins - genetics PrPC Proteins - metabolism scrapie sialic acid |
Title | α2,3 linkage of sialic acid to a GPI anchor and an unpredicted GPI attachment site in human prion protein |
URI | https://dx.doi.org/10.1074/jbc.RA120.013444 https://www.ncbi.nlm.nih.gov/pubmed/32321762 https://search.proquest.com/docview/2394261726 https://pubmed.ncbi.nlm.nih.gov/PMC7261787 |
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