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The glycosylation status of PrPC is a key factor in determining transmissible spongiform encephalopathy transmission between species.

Wiseman FK, Cancellotti E, Piccardo P, Iremonger K, Boyle A, Brown D, Ironside JW, Manson JC, Diack AB - J. Virol. (2015)

Bottom Line: The absence of glycosylation at both or the first PrP(C) glycosylation site in the host results in almost complete resistance to disease.We infected mice that express different forms of glycosylated PrP(C) with three different TSE agents.We demonstrate that changing the glycosylation status of the host can have profound effects on disease transmission, changing host susceptibility and incubation times.

View Article: PubMed Central - PubMed

Affiliation: Neurobiology Division, The Roslin Institute and R(D)SVS, University of Edinburgh, Easter Bush, United Kingdom.

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PrPC expression levels in the brains of glycosylation-deficient transgenic mice. Representative Western blots showing the different PrPC isoforms in wild-type (Wt), G1, G2, and G3 mice using BC6 (A) and BH1 (B) antibodies. Western blots underwent densitometry to measure levels of PrPC. α-Tubulin was used as a loading control. The different isoforms of PrPC are denoted Di (for diglycosylated), Mono (monoglycosylated), Un (unglycosylated), and C1 frag. (C1 fragments).
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Figure 4: PrPC expression levels in the brains of glycosylation-deficient transgenic mice. Representative Western blots showing the different PrPC isoforms in wild-type (Wt), G1, G2, and G3 mice using BC6 (A) and BH1 (B) antibodies. Western blots underwent densitometry to measure levels of PrPC. α-Tubulin was used as a loading control. The different isoforms of PrPC are denoted Di (for diglycosylated), Mono (monoglycosylated), Un (unglycosylated), and C1 frag. (C1 fragments).

Mentions: To ascertain whether the protein levels of PrPC in any of the lines of mice could influence the incubation times in the transmissions described above, we undertook analysis of the PrPC levels in all mouse lines. Immunoblot analysis showed the expected banding patterns for both the transgenic and wild-type mice. Truncated PrPC, designated C1, was observed in all mice and was included in the measurement of total PrPC (selected antibodies are shown in Fig. 4A and B). All of the glycosylation-deficient mice expressed significantly less PrPC than wild-type mice (P < 0.0001). G1 and G2 mice expressed approximately 50% and G3 mice only 32% of that found in wild-type mice, with G3 mice expressing significantly less (P < 0.01) than both G1 and G2 mice. There was no significant difference in total PrP in each mouse line using different antibodies (Fig. 4A and B).


The glycosylation status of PrPC is a key factor in determining transmissible spongiform encephalopathy transmission between species.

Wiseman FK, Cancellotti E, Piccardo P, Iremonger K, Boyle A, Brown D, Ironside JW, Manson JC, Diack AB - J. Virol. (2015)

PrPC expression levels in the brains of glycosylation-deficient transgenic mice. Representative Western blots showing the different PrPC isoforms in wild-type (Wt), G1, G2, and G3 mice using BC6 (A) and BH1 (B) antibodies. Western blots underwent densitometry to measure levels of PrPC. α-Tubulin was used as a loading control. The different isoforms of PrPC are denoted Di (for diglycosylated), Mono (monoglycosylated), Un (unglycosylated), and C1 frag. (C1 fragments).
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4403468&req=5

Figure 4: PrPC expression levels in the brains of glycosylation-deficient transgenic mice. Representative Western blots showing the different PrPC isoforms in wild-type (Wt), G1, G2, and G3 mice using BC6 (A) and BH1 (B) antibodies. Western blots underwent densitometry to measure levels of PrPC. α-Tubulin was used as a loading control. The different isoforms of PrPC are denoted Di (for diglycosylated), Mono (monoglycosylated), Un (unglycosylated), and C1 frag. (C1 fragments).
Mentions: To ascertain whether the protein levels of PrPC in any of the lines of mice could influence the incubation times in the transmissions described above, we undertook analysis of the PrPC levels in all mouse lines. Immunoblot analysis showed the expected banding patterns for both the transgenic and wild-type mice. Truncated PrPC, designated C1, was observed in all mice and was included in the measurement of total PrPC (selected antibodies are shown in Fig. 4A and B). All of the glycosylation-deficient mice expressed significantly less PrPC than wild-type mice (P < 0.0001). G1 and G2 mice expressed approximately 50% and G3 mice only 32% of that found in wild-type mice, with G3 mice expressing significantly less (P < 0.01) than both G1 and G2 mice. There was no significant difference in total PrP in each mouse line using different antibodies (Fig. 4A and B).

Bottom Line: The absence of glycosylation at both or the first PrP(C) glycosylation site in the host results in almost complete resistance to disease.We infected mice that express different forms of glycosylated PrP(C) with three different TSE agents.We demonstrate that changing the glycosylation status of the host can have profound effects on disease transmission, changing host susceptibility and incubation times.

View Article: PubMed Central - PubMed

Affiliation: Neurobiology Division, The Roslin Institute and R(D)SVS, University of Edinburgh, Easter Bush, United Kingdom.

Show MeSH
Related in: MedlinePlus