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Distinct molecular signature of bovine spongiform encephalopathy prion in pigs.

Seuberlich T, Zurbriggen A - Emerging Infect. Dis. (2010)

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In a recent article in Emerging Infectious Diseases, Espinosa et al. investigated the porcine transmission barrier to infection with bovine and ovine transmissible spongiform encephalopathies (TSEs) in transgenic mice expressing the porcine prion protein... Unexpectedly, the electrophoretic profile of the proteinase K–resistant prion protein (PrP) in Western immunoblot (WB) analysis of all 3 TSEs shifted toward a common signature upon transmission... This was a 3-band pattern with a predominant monoglycosylated PrP moiety and, therefore, clearly differed from those of the BSE and atypical scrapie inocula... The authors speculated that the porcine cellular prion protein (PrP) might allow only for few options as it changes its conformation to the disease-associated prion protein... However, whether this effect is attributable to the porcine PrP transgene or to the genetic background of the mouse model remains unknown... To our knowledge, BSE has been successfully transmitted to pigs in 1 study, but WB data were not reported... We had access to central nervous system tissues of 1 of these animals (kindly provided by the Veterinary Laboratories Agency TSE Archive, Weybridge, UK) and aimed at assessing whether a similar effect occurs when cattle BSE affects pigs... Our results show a PrP signature in BSE-infected pigs similar to that described for the porcine PrP transgenic mice and clearly different from that in cattle (Figure)... BSE prions are considered to transmit to other species, such as exotic ruminants, cats, macaques, humans, sheep, and goats, without any obvious alterations of the molecular phenotype... Our study provides evidence that the molecular phenotype of classical BSE also may shift upon genuine interspecies transmission... Attempts to discriminate BSE from other prion diseases in humans and animals often rely at first on the analysis of the PrP signature in WB... Whether this applies to other TSEs and species remains to be addressed.

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Molecular signature of bovine spongiform encephalopathy (BSE) in pigs. A) Comparative Western immunoblot analysis of the proteinase K–resistant core fragment (PrPres) of the pathologic prion protein in BSE in cattle and in an experimentally BSE-infected pig using the monoclonal antibody 6H4 (Prionics, Schlieren, Switzerland). B) Average relative intensities of the diglycosylated (black bars), monoglycosylated (gray bars), and unglycosylated (white bars) PrPres moieties as determined by the Quantity One software package (Bio-Rad, Rheinach, Switzerland). Data are based on 4 independent runs, and error bars indicate SD. Note the different extent of PrPres glycosylation in bovine and porcine BSE. By contrast, the molecular masses of the unglycosylated PrPres were similar and scored 18.89 kDa (SD ± 0.28 kDa) and 18.90 kDa (SD ± 0.42 kDa) in bovine and porcine BSE, respectively. Molecular masses of the standards are indicated on the left in panel A.
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Figure 1: Molecular signature of bovine spongiform encephalopathy (BSE) in pigs. A) Comparative Western immunoblot analysis of the proteinase K–resistant core fragment (PrPres) of the pathologic prion protein in BSE in cattle and in an experimentally BSE-infected pig using the monoclonal antibody 6H4 (Prionics, Schlieren, Switzerland). B) Average relative intensities of the diglycosylated (black bars), monoglycosylated (gray bars), and unglycosylated (white bars) PrPres moieties as determined by the Quantity One software package (Bio-Rad, Rheinach, Switzerland). Data are based on 4 independent runs, and error bars indicate SD. Note the different extent of PrPres glycosylation in bovine and porcine BSE. By contrast, the molecular masses of the unglycosylated PrPres were similar and scored 18.89 kDa (SD ± 0.28 kDa) and 18.90 kDa (SD ± 0.42 kDa) in bovine and porcine BSE, respectively. Molecular masses of the standards are indicated on the left in panel A.

Mentions: To our knowledge, BSE has been successfully transmitted to pigs in 1 study, but WB data were not reported (2). We had access to central nervous system tissues of 1 of these animals (kindly provided by the Veterinary Laboratories Agency TSE Archive, Weybridge, UK) and aimed at assessing whether a similar effect occurs when cattle BSE affects pigs. Our results show a PrPres signature in BSE-infected pigs similar to that described for the porcine PrPc transgenic mice and clearly different from that in cattle (Figure). These findings support the finding by Espinosa et al. that the molecular shift most likely was due to intrinsic properties of the porcine PrPc. Therefore, in this respect the mouse model appears to reflect the situation in the pig.


Distinct molecular signature of bovine spongiform encephalopathy prion in pigs.

Seuberlich T, Zurbriggen A - Emerging Infect. Dis. (2010)

Molecular signature of bovine spongiform encephalopathy (BSE) in pigs. A) Comparative Western immunoblot analysis of the proteinase K–resistant core fragment (PrPres) of the pathologic prion protein in BSE in cattle and in an experimentally BSE-infected pig using the monoclonal antibody 6H4 (Prionics, Schlieren, Switzerland). B) Average relative intensities of the diglycosylated (black bars), monoglycosylated (gray bars), and unglycosylated (white bars) PrPres moieties as determined by the Quantity One software package (Bio-Rad, Rheinach, Switzerland). Data are based on 4 independent runs, and error bars indicate SD. Note the different extent of PrPres glycosylation in bovine and porcine BSE. By contrast, the molecular masses of the unglycosylated PrPres were similar and scored 18.89 kDa (SD ± 0.28 kDa) and 18.90 kDa (SD ± 0.42 kDa) in bovine and porcine BSE, respectively. Molecular masses of the standards are indicated on the left in panel A.
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Related In: Results  -  Collection

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Figure 1: Molecular signature of bovine spongiform encephalopathy (BSE) in pigs. A) Comparative Western immunoblot analysis of the proteinase K–resistant core fragment (PrPres) of the pathologic prion protein in BSE in cattle and in an experimentally BSE-infected pig using the monoclonal antibody 6H4 (Prionics, Schlieren, Switzerland). B) Average relative intensities of the diglycosylated (black bars), monoglycosylated (gray bars), and unglycosylated (white bars) PrPres moieties as determined by the Quantity One software package (Bio-Rad, Rheinach, Switzerland). Data are based on 4 independent runs, and error bars indicate SD. Note the different extent of PrPres glycosylation in bovine and porcine BSE. By contrast, the molecular masses of the unglycosylated PrPres were similar and scored 18.89 kDa (SD ± 0.28 kDa) and 18.90 kDa (SD ± 0.42 kDa) in bovine and porcine BSE, respectively. Molecular masses of the standards are indicated on the left in panel A.
Mentions: To our knowledge, BSE has been successfully transmitted to pigs in 1 study, but WB data were not reported (2). We had access to central nervous system tissues of 1 of these animals (kindly provided by the Veterinary Laboratories Agency TSE Archive, Weybridge, UK) and aimed at assessing whether a similar effect occurs when cattle BSE affects pigs. Our results show a PrPres signature in BSE-infected pigs similar to that described for the porcine PrPc transgenic mice and clearly different from that in cattle (Figure). These findings support the finding by Espinosa et al. that the molecular shift most likely was due to intrinsic properties of the porcine PrPc. Therefore, in this respect the mouse model appears to reflect the situation in the pig.

View Article: PubMed Central - PubMed

AUTOMATICALLY GENERATED EXCERPT
Please rate it.

In a recent article in Emerging Infectious Diseases, Espinosa et al. investigated the porcine transmission barrier to infection with bovine and ovine transmissible spongiform encephalopathies (TSEs) in transgenic mice expressing the porcine prion protein... Unexpectedly, the electrophoretic profile of the proteinase K–resistant prion protein (PrP) in Western immunoblot (WB) analysis of all 3 TSEs shifted toward a common signature upon transmission... This was a 3-band pattern with a predominant monoglycosylated PrP moiety and, therefore, clearly differed from those of the BSE and atypical scrapie inocula... The authors speculated that the porcine cellular prion protein (PrP) might allow only for few options as it changes its conformation to the disease-associated prion protein... However, whether this effect is attributable to the porcine PrP transgene or to the genetic background of the mouse model remains unknown... To our knowledge, BSE has been successfully transmitted to pigs in 1 study, but WB data were not reported... We had access to central nervous system tissues of 1 of these animals (kindly provided by the Veterinary Laboratories Agency TSE Archive, Weybridge, UK) and aimed at assessing whether a similar effect occurs when cattle BSE affects pigs... Our results show a PrP signature in BSE-infected pigs similar to that described for the porcine PrP transgenic mice and clearly different from that in cattle (Figure)... BSE prions are considered to transmit to other species, such as exotic ruminants, cats, macaques, humans, sheep, and goats, without any obvious alterations of the molecular phenotype... Our study provides evidence that the molecular phenotype of classical BSE also may shift upon genuine interspecies transmission... Attempts to discriminate BSE from other prion diseases in humans and animals often rely at first on the analysis of the PrP signature in WB... Whether this applies to other TSEs and species remains to be addressed.

Show MeSH
Related in: MedlinePlus